satarupa22/MacromolecularLigandDB huggingface dataset:
Structure of PP1-spectrin alpha II chimera [PP1(7-304) + linker (G/S)x9 + spectrin alpha II (1025-1039)] bound to Phactr1 (516-580) (PDB entry 6ZEH)
Macromolecule: Serine/threonine-protein phosphatase PP1-alpha catalytic subunit,Spectrin alpha chain, non-erythrocytic 1
Type: Protein, polypeptide(L)
Source organism: Homo sapiens
EC number: 3.1.3.16
Sequence length: 336 residues
Sequence: GHMGSLNLDSIIGRLLEVQGSRPGKNVQLTENEIRGLCLKSREIFLSQPILLELEAPLKICGDIHGQYYDLLRLFEYGGFPPESNYLFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFYDECKRRYNIKLWKTFTDCFNCLPIAAIVDEKIFCCHGGLSPDLQSMEQIRRIMRPTDVPDQGLLCDLLWSDPDKDVQGWGENDRGVSFTFGAEVVAKFLHKHDLDLICRAHQVVEDGYEFFAKRQLVTLFSAPNYCGEFDNAGAMMSVDETLMCSFQILKPADKNKGSGSGSGSGSGSGSGSGSGDPAQSASRENLLEEQ
Oligomeric state: Hetero 2-mer
Stoichiometry: A1, B1
Experimental method: X-RAY DIFFRACTION
Refinement resolution (Å): 1.3
R work: 0.1368
R free: 0.1693
Average B factor: 19.08
Crystallization method: VAPOR DIFFUSION, SITTING DROP
Crystallization pH: 8.5
Crystallization temperature (K): 293
Crystal growth procedure: 20% (w/v) polyethylene glycol 3350, 0.2 M NaI and 0.1 M BIS-Tris propane pH 8.5
Matthews coefficient: 2.26
Solvent content (%): 45.69
Ligand: MANGANESE (II) ION (MN)
Ligand formula: Mn
Ligand molecular weight: 54.938
Ligand SMILES: [Mn+2]
Ligand InChI: InChI=1S/Mn/q+2
Release date: 2020-09-30
PIM1 in complex with Cpd9 ((R)-5-amino-N-(3-(4-aminoazepan-1-yl)-1H-pyrazol-4-yl)-2-(2,6-difluorophenyl)thiazole-4-carboxamide) (PDB entry 6NO8)
Macromolecule: Serine/threonine-protein kinase pim-1
Type: Protein, polypeptide(L)
Source organism: Homo sapiens
EC number: 2.7.11.1
Sequence length: 273 residues
Sequence: PLESQYQVGPLLGSGGFGSVYSGIRVSDNLPVAIKHVEKDRISDWGELPNGTRVPMEVVLLKKVSSGFSGVIRLLDWFERPDSFVLILERPEPVQDLFDFITERGALQEELARSFFWQVLEAVRHCHNCGVLHRDIKDENILIDLNRGELKLIDFGSGALLKDTVYTDFDGTRVYSPPEWIRYHRYHGRSAAVWSLGILLYDMVCGDIPFEHDEEIIRGQVFFRQRVSSECQHLIRWCLALRPSDRPTFEEIQNHPWMQDVLLPQETAEIHLH
Oligomeric state: Monomer
Stoichiometry: A1
Experimental method: X-RAY DIFFRACTION
Refinement resolution (Å): 2.377
R work: 0.1847
R free: 0.2321
Average B factor: 64.7072
Crystallization method: EVAPORATION
Crystallization pH: 8.5
Crystallization temperature (K): 292
Crystal growth procedure: of 0.1 M Tris 8.5, 0.1-0.3M LiSO4, and 29-33% PEG 4000
Matthews coefficient: 3.44
Solvent content (%): 64.2
Ligand: 5-amino-N-{5-[(4S)-4-aminoazepan-1-yl]-1-methyl-1H-pyrazol-4-yl}-2-(2,6-difluorophenyl)-1,3-thiazole-4-carboxamide (KUY)
Ligand formula: C20 H23 F2 N7 O S
Ligand molecular weight: 447.505
Ligand SMILES: Cn1c(c(cn1)NC(=O)c2c(sc(n2)c3c(cccc3F)F)N)N4CCCC(CC4)N
Ligand InChI: InChI=1S/C20H23F2N7OS/c1-28-20(29-8-3-4-11(23)7-9-29)14(10-25-28)26-18(30)16-17(24)31-19(27-16)15-12(21)5-2-6-13(15)22/h2,5-6,10-11H,3-4,7-9,23-24H2,1H3,(H,26,30)/t11-/m0/s1
Release date: 2019-11-27
XChem group deposition -- Crystal Structure of human ACVR1 in complex with FM010957a (PDB entry 5S89)
Macromolecule: Activin receptor type-1
Type: Protein, polypeptide(L)
Source organism: Homo sapiens
EC number: 2.7.11.30
Sequence length: 301 residues
Sequence: SMQRTVARDITLLECVGKGRYGEVWRGSWQGENVAVKIFSSRDEKSWFRETELYNTVMLRHENILGFIASDMTSRHSSTQLWLITHYHEMGSLYDYLQLTTLDTVSCLRIVLSIASGLAHLHIEIFGTQGKPAIAHRDLKSKNILVKKNGQCCIADLGLAVMHSQSTNQLDVGNNPRVGTKRYMAPEVLDETIQVDCFDSYKRVDIWAFGLVLWEVARRMVSNGIVEDYKPPFYDVVPNDPSFEDMRKVVCVDQQRPNIPNRWFSDPTLTSLAKLMKECWYQNPSARLTALRIKKTLTKID
Oligomeric state: Monomer
Stoichiometry: A1
Experimental method: X-RAY DIFFRACTION
Refinement resolution (Å): 1.3
R work: 0.1553
R free: 0.1738
Average B factor: 16.809
Crystallization method: VAPOR DIFFUSION, SITTING DROP
Crystallization pH: 6
Crystallization temperature (K): 277
Crystal growth procedure: 0.1M citrate pH 6.0, 1.4M ammonium sulfate, 0.2M sodium/potassium tartrate
Matthews coefficient: 2.59
Solvent content (%): 52.58
Ligand: 4-methyl-3-[4-(1-methylpiperidin-4-yl)phenyl]-5-(3,4,5-trimethoxyphenyl)pyridine (LU8)
Ligand formula: C27 H32 N2 O3
Ligand molecular weight: 432.555
Ligand SMILES: Cc1c(cncc1c2cc(c(c(c2)OC)OC)OC)c3ccc(cc3)C4CCN(CC4)C
Ligand InChI: InChI=1S/C27H32N2O3/c1-18-23(21-8-6-19(7-9-21)20-10-12-29(2)13-11-20)16-28-17-24(18)22-14-25(30-3)27(32-5)26(15-22)31-4/h6-9,14-17,20H,10-13H2,1-5H3
Release date: 2021-06-23
Thrombin in complex with D-Phe-Pro-m-Trifluoromethylbenzylamide derivative (phe2) (PDB entry 6Y9H)
Macromolecule: Prothrombin
Type: Protein, polypeptide(L)
Source organism: Homo sapiens
EC number: 3.4.21.5
Sequence length: 36 residues
Sequence: TFGSGEADCGLRPLFEKKSLEDKTERELLESYIDGR
Oligomeric state: Hetero 3-mer
Stoichiometry: A1, B1, C1
Experimental method: X-RAY DIFFRACTION
Refinement resolution (Å): 1.48
R work: 0.1375
R free: 0.1697
Average B factor: 22.3901
Crystallization method: VAPOR DIFFUSION, HANGING DROP
Crystallization temperature (K): 277
Crystal growth procedure: 20mM sodium dihydrogen phosphate ph 7.5
350mM NaCl
27% PEG 8000
Matthews coefficient: 2.85
Solvent content (%): 56.89
Ligand: SODIUM ION ()
Ligand formula: Na
Ligand molecular weight: 22.99
Ligand SMILES: [Na+]
Ligand InChI: InChI=1S/Na/q+1
Release date: 2021-03-31
Crystal structure of RAR-related orphan receptor C (NHIS-RORGT(244-487)-L6-SRC1(678-692)) in complex with a phenyl (3-phenylpyrrolidin-3-yl)sulfone inhibitor (PDB entry 6P9F)
Macromolecule: Nuclear receptor ROR-gamma, Nuclear receptor coactivator 1 chimera
Type: Protein, polypeptide(L)
Source organism: Homo sapiens
EC number: 2.3.1.48
Sequence length: 285 residues
Sequence: MGSSHHHHHHSSGLVPRGSHMASLTEIEHLVQSVCKSYRETCQLRLEDLLRQRSNIFSREEVTGYQRKSMWEMWERCAHHLTEAIQYVVEFAKRLSGFMELCQNDQIVLLKAGAMEVVLVRMCRAYNADNRTVFFEGKYGGMELFRALGCSELISSIFDFSHSLSALHFSEDEIALYTALVLINAHRPGLQEKRKVEQLQYNLELAFHHHLCKTHRQSILAKLPPKGKLRSLCSQHVERLQIFQHLHPIVVQAAFPPLYKELFSTSGGSGGLTERHKILHRLLQE
Oligomeric state: Monomer
Stoichiometry: A1
Experimental method: X-RAY DIFFRACTION
Refinement resolution (Å): 2.8
R work: 0.184
R free: 0.223
Average B factor: 72.79
Crystallization method: VAPOR DIFFUSION, HANGING DROP
Crystallization temperature (K): 298
Crystal growth procedure: 20-26% PEG3350, 0.2 M magnesium chloride, 0.1 M Bis-Tris pH 5.5-6.5
Matthews coefficient: 2.5
Solvent content (%): 50.72
Ligand: trans-4-{(3R)-3-[(4-fluorophenyl)sulfonyl]-3-[4-(1,1,1,2,3,3,3-heptafluoropropan-2-yl)phenyl]pyrrolidine-1-carbonyl}cyclohexane-1-carboxylic acid (O5A)
Ligand formula: C27 H25 F8 N O5 S
Ligand molecular weight: 627.543
Ligand SMILES: c1cc(ccc1C2(CCN(C2)C(=O)C3CCC(CC3)C(=O)O)S(=O)(=O)c4ccc(cc4)F)C(C(F)(F)F)(C(F)(F)F)F
Ligand InChI: InChI=1S/C27H25F8NO5S/c28-20-9-11-21(12-10-20)42(40,41)24(13-14-36(15-24)22(37)16-1-3-17(4-2-16)23(38)39)18-5-7-19(8-6-18)25(29,26(30,31)32)27(33,34)35/h5-12,16-17H,1-4,13-15H2,(H,38,39)/t16-,17-,24-/m0/s1
Release date: 2019-07-17
CRYSTAL STRUCTURE OF HUMAN DNA POLYMERASE ETA EXTENDING AN 1,N6-ETHENODEOXYADENOSINE : dT PAIR BY INSERTING dTMPNPP OPPOSITE TEMPLATE dA (PDB entry 5DGA)
Macromolecule: DNA (5'-D(*CP*AP*TP*AP*(EDA)P*TP*GP*AP*CP*GP*CP*T)-3')
Type: DNA, polydeoxyribonucleotide
Source organism: synthetic construct
Sequence length: 12 residues
Sequence: CATAATGACGCT
Oligomeric state: Monomer
Stoichiometry: A1
Experimental method: X-RAY DIFFRACTION
Refinement resolution (Å): 2.3
R work: 0.1564
R free: 0.2328
Average B factor: 27
Crystallization method: VAPOR DIFFUSION, HANGING DROP
Crystallization pH: 5.5
Crystallization temperature (K): 291
Crystal growth procedure: 0.1M MES pH 5.5, 5mM magnesium chloride, 18% PEG 2000 MME
Matthews coefficient: 2.09
Solvent content (%): 41.28
Ligand: 5'-O-[(R)-hydroxy{[(R)-hydroxy(phosphonooxy)phosphoryl]amino}phosphoryl]thymidine (1FZ)
Ligand formula: C10 H18 N3 O13 P3
Ligand molecular weight: 481.184
Ligand SMILES: CC1=CN(C(=O)NC1=O)C2CC(C(O2)COP(=O)(NP(=O)(O)OP(=O)(O)O)O)O
Ligand InChI: InChI=1S/C10H18N3O13P3/c1-5-3-13(10(16)11-9(5)15)8-2-6(14)7(25-8)4-24-27(17,18)12-28(19,20)26-29(21,22)23/h3,6-8,14H,2,4H2,1H3,(H,11,15,16)(H2,21,22,23)(H3,12,17,18,19,20)/t6-,7+,8+/m0/s1
Release date: 2016-06-08
Crystal Structure of human phosphodiesterase 10 in complex with 6-cyclopropyl-N-(3-oxo-1,2-dihydroisoindol-5-yl)-3-(pyrimidin-5-ylamino)pyridine-2-carboxamide (PDB entry 5SF2)
Macromolecule: cAMP and cAMP-inhibited cGMP 3',5'-cyclic phosphodiesterase 10A
Type: Protein, polypeptide(L)
Source organism: Homo sapiens
EC number: 3.1.4.17
Sequence length: 343 residues
Sequence: GSSICTSEEWQGLMQFTLPVRLCKEIELFHFDIGPFENMWPGIFVYMVHRSCGTSCFELEKLCRFIMSVKKNYRRVPYHNWKHAVTVAHCMYAILQNNHTLFTDLERKGLLIACLCHDLDHRGFSNSYLQKFDHPLAALYSTSTMEQHHFSQTVSILQLEGHNIFSTLSSSEYEQVLEIIRKAIIATDLALYFGNRKQLEEMYQTGSLNLNNQSHRDRVIGLMMTACDLCSVTKLWPVTKLTANDIYAEFWAEGDEMKKLGIQPIPMMDRDKKDEVPQGQLGFYNAVAIPCYTTLTQILPPTEPLLKACRDNLSQWEKVIRGEETATWISSPSVAQKAAASED
Oligomeric state: Monomer
Stoichiometry: A1
Experimental method: X-RAY DIFFRACTION
Refinement resolution (Å): 2.02
R work: 0.1954
R free: 0.2292
Average B factor: 45.511
Crystallization method: VAPOR DIFFUSION, SITTING DROP
Crystallization pH: 7.5
Crystallization temperature (K): 295
Crystal growth procedure: 5-20 mg/mL protein in 25mM HEPES/NaOH pH7.5, 150mM NaCl, 50mM BME mixed 1:1 with reservoir 0.1M HEPES/NaOH pH7.5, 30% PEG550MME, 50mM MgCl2
Matthews coefficient: 3.03
Solvent content (%): 59.36
Ligand: 6-cyclopropyl-N-(3-oxo-2,3-dihydro-1H-isoindol-5-yl)-3-[(pyrimidin-5-yl)amino]pyridine-2-carboxamide (IJ7)
Ligand formula: C21 H18 N6 O2
Ligand molecular weight: 386.407
Ligand SMILES: c1cc2c(cc1NC(=O)c3c(ccc(n3)C4CC4)Nc5cncnc5)C(=O)NC2
Ligand InChI: InChI=1S/C21H18N6O2/c28-20-16-7-14(4-3-13(16)8-24-20)26-21(29)19-18(25-15-9-22-11-23-10-15)6-5-17(27-19)12-1-2-12/h3-7,9-12,25H,1-2,8H2,(H,24,28)(H,26,29)
Release date: 2022-10-12
Crystal structure of MAPK13 complex with inhibitor (PDB entry 5EKN)
Macromolecule: Mitogen-activated protein kinase 13
Type: Protein, polypeptide(L)
Source organism: Homo sapiens
EC number: 2.7.11.24
Sequence length: 371 residues
Sequence: MGSSHHHHHHSSGLVPRGSMSLIRKKGFYKQDVNKTAWELPKTYVSPTHVGSGAYGSVCSAIDKRSGEKVAIKKLSRPFQSEIFAKRAYRELLLLKHMQHENVIGLLDVFTPASSLRNFYDFYLVMPFMQTDLQKIMGMEFSEEKIQYLVYQMLKGLKYIHSAGVVHRDLKPGNLAVNEDCELKILDFGLARHADAEMTGYVVTRWYRAPEVILSWMHYNQTVDIWSVGCIMAEMLTGKTLFKGKDYLDQLTQILKVTGVPGTEFVQKLNDKAAKSYIQSLPQTPRKDFTQLFPRASPQAADLLEKMLELDVDKRLTAAQALTHPFFEPFRDPEEETEAQQPFDDSLEHEKLTVDEWKQHIYKEIVNFSPI
Oligomeric state: Monomer
Stoichiometry: A1
Experimental method: X-RAY DIFFRACTION
Refinement resolution (Å): 2.594
R work: 0.218
R free: 0.2731
Crystallization method: VAPOR DIFFUSION, HANGING DROP
Crystallization pH: 6.5
Crystallization temperature (K): 290
Crystal growth procedure: 50 MM AMMONIUM TARTRATE, 18% PEG3350
Matthews coefficient: 2.33
Solvent content (%): 47.15
Ligand: 1-(3-tert-butyl-1-methyl-1H-pyrazol-5-yl)-3-[4-(pyridin-4-ylsulfanyl)phenyl]urea (N58)
Ligand formula: C20 H23 N5 O S
Ligand molecular weight: 381.495
Ligand SMILES: CC(C)(C)c1cc(n(n1)C)NC(=O)Nc2ccc(cc2)Sc3ccncc3
Ligand InChI: InChI=1S/C20H23N5OS/c1-20(2,3)17-13-18(25(4)24-17)23-19(26)22-14-5-7-15(8-6-14)27-16-9-11-21-12-10-16/h5-13H,1-4H3,(H2,22,23,26)
Release date: 2016-07-06
MST3 in complex with compound MRIA13 (PDB entry 7B35)
Macromolecule: Serine/threonine-protein kinase 24
Type: Protein, polypeptide(L)
Source organism: Homo sapiens
EC number: 2.7.11.1
Sequence length: 306 residues
Sequence: MRAQLWGLALNKRRATLPHPGGSTNLKADPEELFTKLEKIGKGSFGEVFKGIDNRTQKVVAIKIIDLEEAEDEIEDIQQEITVLSQCDSPYVTKYYGSYLKDTKLWIIMEYLGGGSALDLLEPGPLDETQIATILREILKGLDYLHSEKKIHRDIKAANVLLSEHGEVKLADFGVAGQLTDTQIKRNTFVGTPFWMAPEVIKQSAYDSKADIWSLGITAIELARGEPPHSELHPMKVLFLIPKNNPPTLEGNYSKPLKEFVEACLNKEPSFRPTAKELLKHKFILRNAKKTSYLTELIDAHHHHHH
Oligomeric state: Monomer
Stoichiometry: A1
Experimental method: X-RAY DIFFRACTION
Refinement resolution (Å): 2.40005138292
R work: 0.205015470048
R free: 0.26347576468
Average B factor: 49.3716855479
Crystallization method: VAPOR DIFFUSION, SITTING DROP
Crystallization temperature (K): 293
Crystal growth procedure: Protein solution: 10 mg/ml in buffer 25 mM HEPES pH 7.5, 200 mM NaCl, 5% glycerol, 0.5 mM TCEP.
reservoir: 24% PEG 3550, 0.1M citrate pH 5.6.
Matthews coefficient: 2.67
Solvent content (%): 54
Ligand: 8-[(5-azanyl-1,3-dioxan-2-yl)methyl]-6-[2-chloranyl-4-(3-methoxy-6-methyl-pyridin-2-yl)phenyl]-2-(methylamino)pyrido[2,3-d]pyrimidin-7-one (SQB)
Ligand formula: C26 H27 Cl N6 O4
Ligand molecular weight: 522.983
Ligand SMILES: Cc1ccc(c(n1)c2ccc(c(c2)Cl)C3=Cc4cnc(nc4N(C3=O)CC5OCC(CO5)N)NC)OC
Ligand InChI: InChI=1S/C26H27ClN6O4/c1-14-4-7-21(35-3)23(31-14)15-5-6-18(20(27)9-15)19-8-16-10-30-26(29-2)32-24(16)33(25(19)34)11-22-36-12-17(28)13-37-22/h4-10,17,22H,11-13,28H2,1-3H3,(H,29,30,32)/t17-,22-
Release date: 2020-12-16
Structure of the STUB1 TPR domain in complex with H204, an all-D Helicon Polypeptide (PDB entry 8F17)
Macromolecule: E3 ubiquitin-protein ligase CHIP
Type: Protein, polypeptide(L)
Source organism: Homo sapiens
EC number: 2.3.2.27
Sequence length: 134 residues
Sequence: GASPSAQELKEQGNRLFVGRKYPEAAACYGRAITRNPLVAVYYTNRALCYLKMQQHEQALADCRRALELDGQSVKAHFFLGQCQLEMESYDEAIANLQRAYSLAKEQRLNFGDDIPSALRIAKKKRWNSIEERR
Oligomeric state: Monomer
Stoichiometry: A1
Experimental method: X-RAY DIFFRACTION
Refinement resolution (Å): 2.21
R work: 0.216
R free: 0.254
Average B factor: 50.18
Crystallization method: VAPOR DIFFUSION, SITTING DROP
Crystallization temperature (K): 291
Crystal growth procedure: 0.15 M Sodium chloride, 0.1 M TRIS pH 8, 8% w/v PEG 6000
Matthews coefficient: 2.4
Solvent content (%): 48.82
Ligand: N,N'-(1,4-phenylene)diacetamide (WHL)
Ligand formula: C10 H12 N2 O2
Ligand molecular weight: 192.214
Ligand SMILES: CC(=O)Nc1ccc(cc1)NC(=O)C
Ligand InChI: InChI=1S/C10H12N2O2/c1-7(13)11-9-3-5-10(6-4-9)12-8(2)14/h3-6H,1-2H3,(H,11,13)(H,12,14)
Release date: 2023-02-15
Crystal structure of JAK1 in complex with ADP (PDB entry 5KHW)
Macromolecule: Tyrosine-protein kinase JAK1
Type: Protein, polypeptide(L)
Source organism: Homo sapiens
EC number: 2.7.10.2
Sequence length: 316 residues
Sequence: GSIMRDINKLEEQNPDIVSEKKPATEVDPTHFEKRFLKRIRDLGEGHFGKVELCRYDPEGDNTGEQVAVKSLKPESGGNHIADLKKEIEILRNLYHENIVKYKGICTEDGGNGIKLIMEFLPSGSLKEYLPKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETDKEYYTVKDDRDSPVFWYAPECLMQSKFYIASDVWSFGVTLHELLTYCDSDSSPMALFLKMIGPTHGQMTVTRLVNTLKEGKRLPCPPNCPDEVYQLMRKCWEFQPSNRTSFQNLIEGFEALLK
Oligomeric state: Monomer
Stoichiometry: A1
Experimental method: X-RAY DIFFRACTION
Refinement resolution (Å): 2.47
R work: 0.1851
R free: 0.2312
Average B factor: 49.51
Crystallization method: VAPOR DIFFUSION, HANGING DROP
Crystallization temperature (K): 281
Crystal growth procedure: 30% PEG1500, 8% MPD, 0.1M Tris pH 9.0
Matthews coefficient: 2.05
Solvent content (%): 39.95
Ligand: ADENOSINE-5'-DIPHOSPHATE (ADP)
Ligand formula: C10 H15 N5 O10 P2
Ligand molecular weight: 427.201
Ligand SMILES: c1nc(c2c(n1)n(cn2)C3C(C(C(O3)COP(=O)(O)OP(=O)(O)O)O)O)N
Ligand InChI: InChI=1S/C10H15N5O10P2/c11-8-5-9(13-2-12-8)15(3-14-5)10-7(17)6(16)4(24-10)1-23-27(21,22)25-26(18,19)20/h2-4,6-7,10,16-17H,1H2,(H,21,22)(H2,11,12,13)(H2,18,19,20)/t4-,6-,7-,10-/m1/s1
Release date: 2016-11-09
IRAK4 in complex with AZ3864 (PDB entry 5K7I)
Macromolecule: Interleukin-1 receptor-associated kinase 4
Type: Protein, polypeptide(L)
Source organism: Homo sapiens
EC number: 2.7.11.1
Sequence length: 301 residues
Sequence: VSDTRFHSFSFYELKNVTNNFDERPISVGGNKMGEGGFGVVYKGYVNNTTVAVKKLAAMVDITTEELKQQFDQEIKVMAKCQHENLVELLGFSSDGDDLCLVYVYMPNGSLLDRLSCLDGTPPLSWHMRCKIAQGAANGINFLHENHHIHRDIKSANILLDEAFTAKISDFGLARASEKFAQTVMTSRIVGTTAYMAPEALRGEITPKSDIYSFGVVLLEIITGLPAVDEHREPQLLLDIKEEIEDEEKTIEDYIDKKMNDADSTSVEAMYSVASQCLHEKKNKRPDIKKVQQLLQEMTAS
Oligomeric state: Monomer
Stoichiometry: A1
Experimental method: X-RAY DIFFRACTION
Refinement resolution (Å): 2.31
R work: 0.219
R free: 0.257
Average B factor: 85.67
Crystallization method: VAPOR DIFFUSION, HANGING DROP
Crystallization pH: 7.2
Crystallization temperature (K): 293
Crystal growth procedure: 2.5 M ammonium sulfate, 0.1 M Hepes
Matthews coefficient: 2.55
Solvent content (%): 51.85
Ligand: (3~{a}~{R},7~{a}~{S})-1-methyl-5-[4-[[5-(oxan-4-yl)-7~{H}-pyrrolo[2,3-d]pyrimidin-4-yl]amino]cyclohexyl]-3,3~{a},4,6,7,7~{a}-hexahydropyrrolo[3,2-c]pyridin-2-one (6QZ)
Ligand formula: C25 H36 N6 O2
Ligand molecular weight: 452.592
Ligand SMILES: CN1C2CCN(CC2CC1=O)C3CCC(CC3)Nc4c5c(c[nH]c5ncn4)C6CCOCC6
Ligand InChI: InChI=1S/C25H36N6O2/c1-30-21-6-9-31(14-17(21)12-22(30)32)19-4-2-18(3-5-19)29-25-23-20(16-7-10-33-11-8-16)13-26-24(23)27-15-28-25/h13,15-19,21H,2-12,14H2,1H3,(H2,26,27,28,29)/t17-,18-,19-,21+/m1/s1
Release date: 2017-12-06
Crystal Structure of human JMJD2A complexed with KDOOA011340 (PDB entry 5F5I)
Macromolecule: Lysine-specific demethylase 4A
Type: Protein, polypeptide(L)
Source organism: Homo sapiens
EC number: 1.14.11
Sequence length: 363 residues
Sequence: YFQSMASESETLNPSARIMTFYPTMEEFRNFSRYIAYIESQGAHRAGLAKVVPPKEWKPRASYDDIDDLVIPAPIQQLVTGQSGLFTQYNIQKKAMTVREFRKIANSDKYCTPRYSEFEELERKYWKNLTFNPPIYGADVNGTLYEKHVDEWNIGRLRTILDLVEKESGITIEGVNTPYLYFGMWKTSFAWHTEDMDLYSINYLHFGEPKSWYSVPPEHGKRLERLAKGFFPGSAQSCEAFLRHKMTLISPLMLKKYGIPFDKVTQEAGEFMITFPYGYHAGFNHGFNCAESTNFATRRWIEYGKQAVLCSCRKDMVKISMDVFVRKFQPERYKLWKAGKDNTVIDHTLPTPEAAEFLKESEL
Oligomeric state: Monomer
Stoichiometry: A1
Experimental method: X-RAY DIFFRACTION
Refinement resolution (Å): 2.63
R work: 0.2109
R free: 0.2433
Average B factor: 53.513
Crystallization method: VAPOR DIFFUSION, SITTING DROP
Crystallization pH: 5.9
Crystallization temperature (K): 277
Crystal growth procedure: 0.1M bis-tris pH 5.9 , 0.15M ammonium sulfate , 13% PEG3350
Matthews coefficient: 2.59
Solvent content (%): 52.45
Ligand: NICKEL (II) ION (NI)
Ligand formula: Ni
Ligand molecular weight: 58.693
Ligand SMILES: [Ni+2]
Ligand InChI: InChI=1S/Ni/q+2
Release date: 2015-12-30
EGFR (T79M/V948R) in complex with naquotinib and an allosteric inhibitor (PDB entry 7LG8)
Macromolecule: Epidermal growth factor receptor
Type: Protein, polypeptide(L)
Source organism: Homo sapiens
EC number: 2.7.10.1
Sequence length: 331 residues
Sequence: GSTSGEAPNQALLRILKETEFKKIKVLGSGAFGTVYKGLWIPEGEKVKIPVAIKELREATSPKANKEILDEAYVMASVDNPHVCRLLGICLTSTVQLIMQLMPFGCLLDYVREHKDNIGSQYLLNWCVQIAKGMNYLEDRRLVHRDLAARNVLVKTPQHVKITDFGLAKLLGAEEKEYHAEGGKVPIKWMALESILHRIYTHQSDVWSYGVTVWELMTFGSKPYDGIPASEISSILEKGERLPQPPICTIDVYMIMRKCWMIDADSRPKFRELIIEFSKMARDPQRYLVIQGDERMHLPSPTDSNFYRALMDEEDMDDVVDADEYLIPQQG
Oligomeric state: Monomer
Stoichiometry: A1
Experimental method: X-RAY DIFFRACTION
Refinement resolution (Å): 2.93
R work: 0.2354
R free: 0.2696
Average B factor: 61.2507
Crystallization method: VAPOR DIFFUSION, HANGING DROP
Crystallization pH: 5.5
Crystallization temperature (K): 293
Crystal growth procedure: 0.1 M Bis-Tris pH 5.5, 30% (w/v) PEG 3350
Matthews coefficient: 2.11
Solvent content (%): 41.66
Ligand: 6-ethyl-3-[[4-[4-(4-methylpiperazin-1-yl)piperidin-1-yl]phenyl]amino]-5-[(3R)-1-prop-2-enoylpyrrolidin-3-yl]oxy-pyrazin
e-2-carboxamide (8RC)
Ligand formula: C30 H42 N8 O3
Ligand molecular weight: 562.706
Ligand SMILES: CCc1c(nc(c(n1)C(=O)N)Nc2ccc(cc2)N3CCC(CC3)N4CCN(CC4)C)OC5CCN(C5)C(=O)C=C
Ligand InChI: InChI=1S/C30H42N8O3/c1-4-25-30(41-24-12-15-38(20-24)26(39)5-2)34-29(27(33-25)28(31)40)32-21-6-8-22(9-7-21)36-13-10-23(11-14-36)37-18-16-35(3)17-19-37/h5-9,23-24H,2,4,10-20H2,1,3H3,(H2,31,40)(H,32,34)/t24-/m1/s1
Release date: 2022-02-23
Crystal Structure of Drosophila DHX36 helicase in complex with polyU (PDB entry 5N94)
Macromolecule: RNA (5'-R(P*UP*UP*UP*UP*UP*UP*UP*U)-3')
Type: RNA, polyribonucleotide
Source organism: Homo sapiens
Sequence length: 8 residues
Sequence: UUUUUUUU
Oligomeric state: Monomer
Stoichiometry: A1
Experimental method: X-RAY DIFFRACTION
Refinement resolution (Å): 2.428
R work: 0.2119
R free: 0.278
Crystallization method: VAPOR DIFFUSION, SITTING DROP
Crystallization pH: 6.5
Crystallization temperature (K): 298
Crystal growth procedure: 0.1M MES monohydrate-imidazole
20mM sodium formate
20mM ammonium acetate
20mM sodium citrate tribasic hydrate
20mM sodium oxamate
20mM potassium sodium tartrate tetrahydrate
Matthews coefficient: 2.69
Solvent content (%): 54.3
Release date: 2018-03-14
HUMAN CK2 KINASE ALPHA SUBUNIT IN COMPLEX WITH THE ATP-COMPETITIVE INHIBITOR 4,7-DIBROMOBENZOTRIAZOLE (PDB entry 6TLR)
Macromolecule: Casein kinase II subunit alpha
Type: Protein, polypeptide(L)
Source organism: Homo sapiens
EC number: 2.7.11.1
Sequence length: 399 residues
Sequence: MSGPVPSRARVYTDVNTHRPREYWDYESHVVEWGNQDDYQLVRKLGRGKYSEVFEAINITNNEKVVVKILKPVKKKKIKREIKILENLRGGPNIITLADIVKDPVSRTPALVFEHVNNTDFKQLYQTLTDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEHRKLRLIDWGLAEFYHPGQEYNVRVASRYFKGPELLVDYQMYDYSLDMWSLGCMLASMIFRKEPFFHGHDNYDQLVRIAKVLGTEDLYDYIDKYNIELDPRFNDILGRHSRKRWERFVHSENQHLVSPEALDFLDKLLRYDHQSRLTAREAMEHPYFYTVVKDQARMGSSSMPGGSTPVSSANMMSGISSVPTPSPLGPLAGSPVIAAANPLGMPVPAAAGAQQLEHHHHHH
Oligomeric state: Monomer
Stoichiometry: A1
Experimental method: X-RAY DIFFRACTION
Refinement resolution (Å): 1.64
R work: 0.1486
R free: 0.1776
Average B factor: 35.248
Crystallization method: VAPOR DIFFUSION, SITTING DROP
Crystallization pH: 7.5
Crystallization temperature (K): 290
Crystal growth procedure: 0.1 M sodium HEPES/MOPS buffer pH 7.5, 20 mM sodium formate, 20 mM ammonium acetate, 20 mM sodium citrate tribasic dihydrate, 20 mM sodium potassium tartrate tetrahydrate, 20 mM sodium oxamate, 20% polyethylene glycol 550 monomethyl ester, 10% polyethylene glycol 20000
Matthews coefficient: 2.72
Ligand: 4,7-bis(bromanyl)-1~{H}-benzotriazole (NKE)
Ligand formula: C6 H3 Br2 N3
Ligand molecular weight: 276.916
Ligand SMILES: c1cc(c2c(c1Br)[nH]nn2)Br
Ligand InChI: InChI=1S/C6H3Br2N3/c7-3-1-2-4(8)6-5(3)9-11-10-6/h1-2H,(H,9,10,11)
Release date: 2020-12-16
Crystal structure of TNKS2 in complex with 2-[4-(diethylamino)phenyl]-3,4-dihydroquinazolin-4-one (PDB entry 5NWD)
Macromolecule: Tankyrase-2
Type: Protein, polypeptide(L)
Source organism: Homo sapiens
EC number: 2.4.2.30
Sequence length: 49 residues
Sequence: KMAHSPPGHHSVTGRPSVNGLALAEYVIYRGEQAYPEYLITYQIMRPEG
Oligomeric state: Hetero 2-mer
Stoichiometry: A1, B1
Experimental method: X-RAY DIFFRACTION
Refinement resolution (Å): 1.45
R work: 0.17726
R free: 0.19184
Average B factor: 24.148
Crystallization method: VAPOR DIFFUSION, SITTING DROP
Crystallization pH: 8.5
Crystallization temperature (K): 277
Crystal growth procedure: 0.2 M LISO4, 0.1 M TRIS HCL, 24/26 %         
PEG3350
Matthews coefficient: 2.43
Solvent content (%): 49.46
Ligand: 2-[4-(diethylamino)phenyl]-3~{H}-quinazolin-4-one (9C8)
Ligand formula: C18 H19 N3 O
Ligand molecular weight: 293.363
Ligand SMILES: CCN(CC)c1ccc(cc1)C2=Nc3ccccc3C(=O)N2
Ligand InChI: InChI=1S/C18H19N3O/c1-3-21(4-2)14-11-9-13(10-12-14)17-19-16-8-6-5-7-15(16)18(22)20-17/h5-12H,3-4H2,1-2H3,(H,19,20,22)
Release date: 2018-03-14
Crystal Structure of human phosphodiesterase 10 in complex with 2-methyl-4-N-(1,3-oxazol-4-ylmethyl)-3-N-(2-phenylimidazo[1,2-a]pyrimidin-7-yl)pyrazole-3,4-dicarboxamide (PDB entry 5SDV)
Macromolecule: cAMP and cAMP-inhibited cGMP 3',5'-cyclic phosphodiesterase 10A
Type: Protein, polypeptide(L)
Source organism: Homo sapiens
EC number: 3.1.4.17
Sequence length: 343 residues
Sequence: GSSICTSEEWQGLMQFTLPVRLCKEIELFHFDIGPFENMWPGIFVYMVHRSCGTSCFELEKLCRFIMSVKKNYRRVPYHNWKHAVTVAHCMYAILQNNHTLFTDLERKGLLIACLCHDLDHRGFSNSYLQKFDHPLAALYSTSTMEQHHFSQTVSILQLEGHNIFSTLSSSEYEQVLEIIRKAIIATDLALYFGNRKQLEEMYQTGSLNLNNQSHRDRVIGLMMTACDLCSVTKLWPVTKLTANDIYAEFWAEGDEMKKLGIQPIPMMDRDKKDEVPQGQLGFYNAVAIPCYTTLTQILPPTEPLLKACRDNLSQWEKVIRGEETATWISSPSVAQKAAASED
Oligomeric state: Monomer
Stoichiometry: A1
Experimental method: X-RAY DIFFRACTION
Refinement resolution (Å): 2.15
R work: 0.1752
R free: 0.2318
Average B factor: 36.574
Crystallization method: VAPOR DIFFUSION, SITTING DROP
Crystallization pH: 7.5
Crystallization temperature (K): 295
Crystal growth procedure: 5-20 mg/mL protein in 25mM HEPES/NaOH pH7.5, 150mM NaCl, 50mM BME mixed 1:1 with reservoir 0.1M HEPES/NaOH pH7.5, 30% PEG550MME, 50mM MgCl2
Matthews coefficient: 2.63
Solvent content (%): 53.31
Ligand: 1-methyl-N~4~-[(1,3-oxazol-4-yl)methyl]-N~5~-[(4R)-2-phenylimidazo[1,2-a]pyrimidin-7-yl]-1H-pyrazole-4,5-dicarboxamide (IAI)
Ligand formula: C22 H18 N8 O3
Ligand molecular weight: 442.43
Ligand SMILES: Cn1c(c(cn1)C(=O)NCc2cocn2)C(=O)Nc3ccn4cc(nc4n3)c5ccccc5
Ligand InChI: InChI=1S/C22H18N8O3/c1-29-19(16(10-25-29)20(31)23-9-15-12-33-13-24-15)21(32)27-18-7-8-30-11-17(26-22(30)28-18)14-5-3-2-4-6-14/h2-8,10-13H,9H2,1H3,(H,23,31)(H,26,27,28,32)
Release date: 2022-10-12