satarupa22/MacromolecularLigandDB huggingface dataset:
DYRK1A in complex with XMD15-27-2 (PDB entry 6EIR)
Macromolecule: Dual specificity tyrosine-phosphorylation-regulated kinase 1A
Type: Protein, polypeptide(L)
Source organism: Homo sapiens
EC number: 2.7.12.1
Sequence length: 368 residues
Sequence: GASDSSHKKERKVYNDGYDDDNYDYIVKNGEKWMDRYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIKNKKAFLNQAQIEVRLLELMNKHDTEMKYYIVHLKRHFMFRNHLCLVFEMLSYNLYDLLRNTNFRGVSLNLTRKFAQQMCTALLFLATPELSIIHCDLKPENILLCNPKRSAIKIVDFGSSCQLGQRIYQYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVEVLGIPPAHILDQAPKARKFFEKLPDGTWNLKKTKDGKREYKPPGTRKLHNILGVETGGPGGRRAGESGHTVADYLKFKDLILRMLDYDPKTRIQPYYALQHSFFKKTADEGTNTS
Oligomeric state: Monomer
Stoichiometry: A1
Experimental method: X-RAY DIFFRACTION
Refinement resolution (Å): 2.4
R work: 0.23371
R free: 0.25813
Average B factor: 48.756
Crystallization method: VAPOR DIFFUSION, HANGING DROP
Crystallization temperature (K): 293
Crystal growth procedure: 0.1 M KSCN; 0.1 M NaCl; 10% PEG 3350, pH 6.8
Matthews coefficient: 2.57
Solvent content (%): 52.23
Ligand: ~{N}-[4-[[4-azanyl-2-[[2-methoxy-4-(4-methylpiperazin-1-yl)phenyl]amino]-1,3-thiazol-5-yl]carbonyl]phenyl]propanamide (B6H)
Ligand formula: C25 H30 N6 O3 S
Ligand molecular weight: 494.609
Ligand SMILES: CCC(=O)Nc1ccc(cc1)C(=O)c2c(nc(s2)Nc3ccc(cc3OC)N4CCN(CC4)C)N
Ligand InChI: InChI=1S/C25H30N6O3S/c1-4-21(32)27-17-7-5-16(6-8-17)22(33)23-24(26)29-25(35-23)28-19-10-9-18(15-20(19)34-3)31-13-11-30(2)12-14-31/h5-10,15H,4,11-14,26H2,1-3H3,(H,27,32)(H,28,29)
Release date: 2018-08-29
Aspartyl/Asparaginyl beta-hydroxylase (AspH) oxygenase and TPR domains in complex with manganese, 4,4-dimethyl-2-oxoglutarate, and factor X substrate peptide fragment(39mer-4Ser) (PDB entry 6YYY)
Macromolecule: Coagulation factor X
Type: Protein, polypeptide(L)
Source organism: Homo sapiens
EC number: 3.4.21.6
Sequence length: 39 residues
Sequence: DGDQSETSPSQNQGKCKDGLGEYTCTSLEGFEGKNSELF
Oligomeric state: Hetero 2-mer
Stoichiometry: A1, B1
Experimental method: X-RAY DIFFRACTION
Refinement resolution (Å): 2.29
R work: 0.209
R free: 0.2438
Average B factor: 42.85
Crystallization method: VAPOR DIFFUSION, SITTING DROP
Crystallization temperature (K): 277
Crystal growth procedure: 200 mM sodium bromide, 20% w/v PEG 3350, 1 mM manganese chloride, 2 mM 4,4-dimethyl-2-oxoglutarate, 18 mg/ml protein
Matthews coefficient: 2.68
Solvent content (%): 54.07
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: 2021-03-17
Crystal structure of Aurora-A bound to a hydrocarbon-stapled proteomimetic of TPX2 (PDB entry 5LXM)
Macromolecule: Aurora kinase A
Type: Protein, polypeptide(L)
Source organism: Homo sapiens
EC number: 2.7.11.1
Sequence length: 283 residues
Sequence: MESKKRQWALEDFEIGRPLGKGKFGNVYLAREKQSKFILALKVLFKAQLEKAGVEHQLRREVEIQSHLRHPNILRLYGYFHDATRVYLILEYAPLGTVYRELQKLSKFDEQRTATYITELANALSYCHSKRVIHRDIKPENLLLGSAGELKIADFGWSVHAPSSRRTTLAGTLDYLPPEMIEGRMHDEKVDLWSLGVLCYEFLVGKPPFEANTYQETYKRISRVEFTFPDFVTEGARDLISRLLKHNPSQRPMLREVLEHPWITANSSKPSNAQNKESASKQS
Oligomeric state: Hetero 2-mer
Stoichiometry: A1, B1
Experimental method: X-RAY DIFFRACTION
Refinement resolution (Å): 2.08
R work: 0.1996
R free: 0.2429
Average B factor: 74.378
Crystallization method: VAPOR DIFFUSION, SITTING DROP
Crystallization temperature (K): 295
Crystal growth procedure: MORPHEUS Crystallization Screen condition C1
Matthews coefficient: 3.63
Solvent content (%): 66.11
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: 2016-11-02
JAK2 Pseudokinase in complex with NU6140 (PDB entry 5WIJ)
Macromolecule: Tyrosine-protein kinase JAK2
Type: Protein, polypeptide(L)
Source organism: Homo sapiens
EC number: 2.7.10.2
Sequence length: 277 residues
Sequence: VFHKIRNEDLIFNESLGQGTFTKIFKGVRREVGDYGQLHETEVLLKVLDKAHRNYSESFFEAASMMSKLSHKHLVLNYGVCVCGDENILVQEFVKFGSLDTYLKKNKNCINILWKLEVAKQLAAAMHFLEENTLIHGNVCAKNILLIREEDRKTGNPPFIKLSDPGISITVLPKDILQERIPWVPPECIENPKNLNLATDKWSFGTTLWEICSGGDKPLSALDSQRKLQFYEDRHQLPAPKAAELANLINNCMDYEPDHRPSFRAIIRDLNSLFTPD
Oligomeric state: Monomer
Stoichiometry: A1
Experimental method: X-RAY DIFFRACTION
Refinement resolution (Å): 2.04
R work: 0.2083
R free: 0.231
Crystallization method: VAPOR DIFFUSION, HANGING DROP
Crystallization pH: 8
Crystallization temperature (K): 277
Crystal growth procedure: 200 mM Sodium Acetate, 100 mM Tris-HCl, 18%-30%(w/v) polyethylene glycol 4000.
Matthews coefficient: 2.5
Solvent content (%): 50.83
Ligand: 4-{[6-(cyclohexylmethoxy)-7H-purin-2-yl]amino}-N,N-diethylbenzamide (AQG)
Ligand formula: C23 H30 N6 O2
Ligand molecular weight: 422.523
Ligand SMILES: CCN(CC)C(=O)c1ccc(cc1)Nc2nc3c(c(n2)OCC4CCCCC4)[nH]cn3
Ligand InChI: InChI=1S/C23H30N6O2/c1-3-29(4-2)22(30)17-10-12-18(13-11-17)26-23-27-20-19(24-15-25-20)21(28-23)31-14-16-8-6-5-7-9-16/h10-13,15-16H,3-9,14H2,1-2H3,(H2,24,25,26,27,28)
Release date: 2018-08-01
Tankyrase 2 in complex with an inhibitor (OUL211) (PDB entry 7R5X)
Macromolecule: Poly [ADP-ribose] polymerase tankyrase-2
Type: Protein, polypeptide(L)
Source organism: Homo sapiens
EC number: 2.4.2.30
Sequence length: 171 residues
Sequence: SMLNTSGSGTILIDLSPDDKEFQSVEEEMQSTVREHRDGGHAGGIFNRYNILKIQKVCNKKLWERYTHRRKEVSEENHNHANERMLFHGSPFVNAIIHKGFDERHAYIGGMFGAGIYFAENSSKSNQYVYGIGGGTGCPVHKDRSCYICHRQLLFCRVTLGKSFLQFSAMK
Oligomeric state: Hetero 2-mer
Stoichiometry: A1, B1
Experimental method: X-RAY DIFFRACTION
Refinement resolution (Å): 2.052
R work: 0.1887
R free: 0.2244
Average B factor: 35.436
Crystallization method: VAPOR DIFFUSION, SITTING DROP
Crystallization temperature (K): 277.15
Crystal growth procedure: 100 mM Tris pH=8.5, 200mM Lithium Sulphate, 20% PEG3350
Matthews coefficient: 2.68
Solvent content (%): 54.12
Ligand: SULFATE ION (SO4)
Ligand formula: O4 S
Ligand molecular weight: 96.063
Ligand SMILES: [O-]S(=O)(=O)[O-]
Ligand InChI: InChI=1S/H2O4S/c1-5(2,3)4/h(H2,1,2,3,4)/p-2
Release date: 2023-02-08
Crystal structure of CDK2 in complex with TW8672 (PDB entry 7RWF)
Macromolecule: Cyclin-dependent kinase 2
Type: Protein, polypeptide(L)
Source organism: Homo sapiens
EC number: 2.7.11.22
Sequence length: 299 residues
Sequence: FMENFQKVEKIGEGTYGVVYKARNKLTGEVVALKKIRLDTETEGVPSTAIREISLLKELNHPNIVKLLDVIHTENKLYLVFEFLHQDLKKFMDASALTGIPLPLIKSYLFQLLQGLAFCHSHRVLHRDLKPQNLLINTEGAIKLADFGLARAFGVPVRTYTHEVVTLWYRAPEILLGCKYYSTAVDIWSLGCIFAEMVTRRALFPGDSEIDQLFRIFRTLGTPDEVVWPGVTSMPDYKPSFPKWARQDFSKVVPPLDEDGRSLLSQMLHYDPNKRISAKAALAHPFFQDVTKPVPHLRL
Oligomeric state: Monomer
Stoichiometry: A1
Experimental method: X-RAY DIFFRACTION
Refinement resolution (Å): 1.5
R work: 0.1917
R free: 0.2093
Average B factor: 21.0979
Crystallization method: VAPOR DIFFUSION, HANGING DROP
Crystallization pH: 7.5
Crystallization temperature (K): 291
Crystal growth procedure: 4.5mg/mL, 15% Jeffamine ED-2001, 0.1M HEPES pH7.5, VAPOR DIFFUSION, HANGING DROP, temperature 291K
Matthews coefficient: 1.92
Solvent content (%): 35.95
Ligand: 1,2-ETHANEDIOL (EDO)
Ligand formula: C2 H6 O2
Ligand molecular weight: 62.068
Ligand SMILES: C(CO)O
Ligand InChI: InChI=1S/C2H6O2/c3-1-2-4/h3-4H,1-2H2
Release date: 2022-08-24
Human MYST histone acetyltransferase 1 (PDB entry 5WCI)
Macromolecule: Histone acetyltransferase KAT8
Type: Protein, polypeptide(L)
Source organism: Homo sapiens
EC number: 2.3.1.48
Sequence length: 295 residues
Sequence: MGSSHHHHHHSSGLVPRGSTKVKYVDKIHIGNYEIDAWYFSPFPEDYGKQPKLWLCEYCLKYMKYEKSYRFHLGQCQWRQPPGKEIYRKSNISVHEVDGKDHKIYCQNLCLLAKLFLDHKTLYFDVEPFVFYILTEVDRQGAHIVGYFSKEKESPDGNNVACILTLPPYQRRGYGKFLIAFSYELSKLESTVGSPEKPLSDLGKLSYRSYWSWVLLENLRDFRGTLSIKDLSQMTSITQNDIISTLQSLNMVKYWKGQHVICVTPKLVEEHLKSAQYKKPPITVDSVCLKWAPPK
Oligomeric state: Monomer
Stoichiometry: A1
Experimental method: X-RAY DIFFRACTION
Refinement resolution (Å): 1.78
R work: 0.1826
R free: 0.2183
Average B factor: 24.099
Crystallization method: VAPOR DIFFUSION, SITTING DROP
Crystallization pH: 5
Crystallization temperature (K): 291
Crystal growth procedure: 20% PEG 3350, 0.2 M Na malonate pH5.0
Matthews coefficient: 2.38
Solvent content (%): 48.26
Ligand: ZINC ION (ZN)
Ligand formula: Zn
Ligand molecular weight: 65.409
Ligand SMILES: [Zn+2]
Ligand InChI: InChI=1S/Zn/q+2
Release date: 2017-07-26
Human angiogenin PD variant R95Q (PDB entry 5M9Q)
Macromolecule: Angiogenin
Type: Protein, polypeptide(L)
Source organism: Homo sapiens
EC number: 3.1.27
Sequence length: 124 residues
Sequence: MQDNSRYTHFLTQHYDAKPQGRDDRYCESIMRRRGLTSPCKDINTFIHGNKRSIKAICENKNGNPHRENLRISKSSFQVTTCKLHGGSPWPPCQYQATAGFRNVVVACENGLPVHLDQSIFRRP
Oligomeric state: Monomer
Stoichiometry: A1
Experimental method: X-RAY DIFFRACTION
Refinement resolution (Å): 1.35
R work: 0.15069
R free: 0.1793
Average B factor: 20.03
Crystallization method: VAPOR DIFFUSION, SITTING DROP
Crystallization pH: 6.5
Crystallization temperature (K): 289
Crystal growth procedure: 0.2 M ammonium sulphate
0.1 M Na cacodylate
30% PEG 8000
Matthews coefficient: 2.33
Solvent content (%): 47.22
Ligand: SULFATE ION (SO4)
Ligand formula: O4 S
Ligand molecular weight: 96.063
Ligand SMILES: [O-]S(=O)(=O)[O-]
Ligand InChI: InChI=1S/H2O4S/c1-5(2,3)4/h(H2,1,2,3,4)/p-2
Release date: 2017-02-22
ATAD2 bromodomain in complex with H4S1phK5ac (res 1-15) ligand (PDB entry 8SDQ)
Macromolecule: ATPase family AAA domain-containing protein 2
Type: Protein, polypeptide(L)
Source organism: Homo sapiens
EC number: 3.6.1
Sequence length: 152 residues
Sequence: GPLGSEPRSLTAEEVKRLEEQEEDTFRELRIFLRNVTHRLAIDKRFRVFTKPVDPDEVPDYVTVIKQPMDLSSVISKIDLHKYLTVKDYLRDIDLICSNALEYNPDRDPGDRLIRHRACALRDTAYAIIKEELDEDFEQLAEEIQESRKKRG
Oligomeric state: Hetero 2-mer
Stoichiometry: A1, B1
Experimental method: X-RAY DIFFRACTION
Refinement resolution (Å): 1.85
R work: 0.205
R free: 0.2384
Average B factor: 34.24
Crystallization method: VAPOR DIFFUSION, SITTING DROP
Crystallization temperature (K): 277
Crystal growth procedure: 60% v/v TascimateTM pH 7.0
Matthews coefficient: 2.95
Solvent content (%): 58.32
Release date: 2024-06-05
Crystal structure of RNAse 6 (PDB entry 6MV7)
Macromolecule: Ribonuclease K6
Type: Protein, polypeptide(L)
Source organism: Homo sapiens
EC number: 3.1.27
Sequence length: 128 residues
Sequence: MWPKRLTKAHWFEIQHIQPSPLQCNRAMSGINNYTQHCKHQNTFLHDSFQNVAAVCDLLSIVCKNRRHNCHQSSKPVNMTDCRLTSGKYPQCRYSAAAQYKFFIVACDPPQKSDPPYKLVPVHLDSIL
Oligomeric state: Monomer
Stoichiometry: A1
Experimental method: X-RAY DIFFRACTION
Refinement resolution (Å): 2.59
R work: 0.2168
R free: 0.2519
Average B factor: 19.0356
Crystallization method: VAPOR DIFFUSION
Crystallization temperature (K): 298
Crystal growth procedure: PEG 4000, 50mM Sodium phosphate
Matthews coefficient: 1.78
Solvent content (%): 30.71
Ligand: ADENOSINE MONOPHOSPHATE (AMP)
Ligand formula: C10 H14 N5 O7 P
Ligand molecular weight: 347.221
Ligand SMILES: c1nc(c2c(n1)n(cn2)C3C(C(C(O3)COP(=O)(O)O)O)O)N
Ligand InChI: InChI=1S/C10H14N5O7P/c11-8-5-9(13-2-12-8)15(3-14-5)10-7(17)6(16)4(22-10)1-21-23(18,19)20/h2-4,6-7,10,16-17H,1H2,(H2,11,12,13)(H2,18,19,20)/t4-,6-,7-,10-/m1/s1
Release date: 2019-11-13
Structure of human plasma factor XIIa in complex with (2S)-4-(5-chloro-1,3-benzoxazol-2-yl)-1-(N,3-dicyclohexyl-D-alanyl)-N-[(thiophen-2-yl)methyl]piperazine-2-carboxamide (compound 7) (PDB entry 6X0S)
Macromolecule: Coagulation factor XII
Type: Protein, polypeptide(L)
Source organism: Homo sapiens
EC number: 3.4.21.38
Sequence length: 259 residues
Sequence: LSCGQRLRKSLSSMTRVVGGLVALRGAHPYIAALYWGHSFCAGSLIAPCWVLTAAHCLQDRPAPEDLTVVLGQERRNHSCEPCQTLAVRSYRLHEAFSPVSYQHDLALLRLQEDADGSCALLSPYVQPVCLPSGAARPSETTLCQVAGWGHQFEGAEEYASFLQEAQVPFLSLERCSAPDVHGSSILPGMLCAGFLEGGTDACQGDSGGPLVCEDQAAERRLTLQGIISWGSGCGDRNKPGVYTDVAYYLAWIREHTVS
Oligomeric state: Monomer
Stoichiometry: A1
Experimental method: X-RAY DIFFRACTION
Refinement resolution (Å): 1.898
R work: 0.2146
R free: 0.2509
Average B factor: 19.46
Crystallization method: VAPOR DIFFUSION, HANGING DROP
Crystallization temperature (K): 291
Crystal growth procedure: 18% PEG3350, 200 mM lithium sulfate, 0.7 mM cadmium chloride, 100 mM Bis-Tris, pH 6.3
Matthews coefficient: 2.64
Solvent content (%): 53.46
Ligand: (2S)-4-(5-chloro-1,3-benzoxazol-2-yl)-1-(N,3-dicyclohexyl-D-alanyl)-N-[(thiophen-2-yl)methyl]piperazine-2-carboxamide (UJA)
Ligand formula: C32 H42 Cl N5 O3 S
Ligand molecular weight: 612.226
Ligand SMILES: c1cc(sc1)CNC(=O)C2CN(CCN2C(=O)C(CC3CCCCC3)NC4CCCCC4)c5nc6cc(ccc6o5)Cl
Ligand InChI: InChI=1S/C32H42ClN5O3S/c33-23-13-14-29-26(19-23)36-32(41-29)37-15-16-38(28(21-37)30(39)34-20-25-12-7-17-42-25)31(40)27(18-22-8-3-1-4-9-22)35-24-10-5-2-6-11-24/h7,12-14,17,19,22,24,27-28,35H,1-6,8-11,15-16,18,20-21H2,(H,34,39)/t27-,28+/m1/s1
Release date: 2021-05-19
Irak4-inhibitor co-structure (PDB entry 4XS2)
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): 2.73
R work: 0.264
R free: 0.285
Average B factor: 71.26
Crystallization method: VAPOR DIFFUSION, HANGING DROP
Crystallization pH: 6.4
Crystallization temperature (K): 289
Crystal growth procedure: 1.80 to 2.0 M Sodium Malonate pH 7.4, 0.2 M Sodium Acetate, 25 mM Hexamminecobalt(III)chloride, 0.05%w/v Pluronic-F-68
Matthews coefficient: 2.62
Solvent content (%): 53.06
Ligand: (1R,2S,3R,5R)-3-({5-(1,3-benzothiazol-2-yl)-6-chloro-2-[(3-methoxypropyl)amino]pyrimidin-4-yl}amino)-5-(hydroxymethyl)cyclopentane-1,2-diol (42P)
Ligand formula: C21 H26 Cl N5 O4 S
Ligand molecular weight: 479.98
Ligand SMILES: COCCCNc1nc(c(c(n1)Cl)c2nc3ccccc3s2)NC4CC(C(C4O)O)CO
Ligand InChI: InChI=1S/C21H26ClN5O4S/c1-31-8-4-7-23-21-26-18(22)15(20-25-12-5-2-3-6-14(12)32-20)19(27-21)24-13-9-11(10-28)16(29)17(13)30/h2-3,5-6,11,13,16-17,28-30H,4,7-10H2,1H3,(H2,23,24,26,27)/t11-,13-,16-,17+/m1/s1
Release date: 2015-05-13
Carbonic anhydrase 2 in complex with [(2R,3S,4R,5R)-5-(6-AMINO-9H-PURIN-9-YL)-3,4-DIHYDROXYTETRAHYDRO-2-FURANYL]METHYL SULFAMATE inhibitor (PDB entry 6C7W)
Macromolecule: Carbonic anhydrase 2
Type: Protein, polypeptide(L)
Source organism: Homo sapiens
EC number: 4.2.1.1
Sequence length: 260 residues
Sequence: MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLKGGPLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVVDVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELMVDNWRPAQPLKNRQIKASFK
Oligomeric state: Monomer
Stoichiometry: A1
Experimental method: X-RAY DIFFRACTION
Refinement resolution (Å): 1.28
R work: 0.11741
R free: 0.1515
Average B factor: 14.74
Crystallization method: VAPOR DIFFUSION, SITTING DROP
Crystallization pH: 8
Crystallization temperature (K): 281
Crystal growth procedure: Protein was at 10 mg/mL and was set up in 250 plus 250 nL drops with a reservoir of 50 mM Tris pH 8.0, 2.8 M ammonium sulfate
Matthews coefficient: 2.1
Solvent content (%): 41.3
Ligand: ZINC ION (ZN)
Ligand formula: Zn
Ligand molecular weight: 65.409
Ligand SMILES: [Zn+2]
Ligand InChI: InChI=1S/Zn/q+2
Release date: 2018-05-23
Structure of cathepsin K in complex with the azadipeptide nitrile inhibitor Gu1303 (PDB entry 7QBN)
Macromolecule: Cathepsin K
Type: Protein, polypeptide(L)
Source organism: Homo sapiens
EC number: 3.4.22.38
Sequence length: 217 residues
Sequence: GRAPDSVDYRKKGYVTPVKNQGQCGSCWAFSSVGALEGQLKKKTGKLLNLSPQNLVDCVSENDGCGGGYMTNAFQYVQKNRGIDSEDAYPYVGQEESCMYNPTGKAAKCRGYREIPEGNEKALKRAVARVGPVSVAIDASLTSFQFYSKGVYYDESCNSDNLNHAVLAVGYGIQKGNKHWIIKNSWGENWGNKGYILMARNKNNACGIANLASFPKM
Oligomeric state: Monomer
Stoichiometry: A1
Experimental method: X-RAY DIFFRACTION
Refinement resolution (Å): 1.55
R work: 0.1426
R free: 0.1665
Average B factor: 13.033
Crystallization method: VAPOR DIFFUSION, HANGING DROP
Crystallization temperature (K): 290
Crystal growth procedure: 12.5% PEG 1000, 12.5% PEG 3350, 12.5% MPD, 0.03 M sodium nitrate, 0.03 M disodium hydrogen phosphate, 0.03 M ammonium sulfate, 0.1 M MES/imidazole pH 6.5
Matthews coefficient: 1.98
Solvent content (%): 37.84
Ligand: (phenylmethyl) ~{N}-[(2~{S})-1-[[aminomethyl(methyl)amino]-methyl-amino]-1-oxidanylidene-3-phenyl-propan-2-yl]carbamate (9ZG)
Ligand formula: C20 H26 N4 O3
Ligand molecular weight: 370.445
Ligand SMILES: CN(CN)N(C)C(=O)C(Cc1ccccc1)NC(=O)OCc2ccccc2
Ligand InChI: InChI=1S/C20H26N4O3/c1-23(15-21)24(2)19(25)18(13-16-9-5-3-6-10-16)22-20(26)27-14-17-11-7-4-8-12-17/h3-12,18H,13-15,21H2,1-2H3,(H,22,26)/t18-/m0/s1
Release date: 2022-01-26
Structure of Scp1 D96N bound to REST-pS861/4 peptide (PDB entry 6DU3)
Macromolecule: Carboxy-terminal domain RNA polymerase II polypeptide A small phosphatase 1
Type: Protein, polypeptide(L)
Source organism: Homo sapiens
EC number: 3.1.3.16
Sequence length: 180 residues
Sequence: QYLLPEAKAQDSDKICVVINLDETLVHSSFKPVNNADFIIPVEIDGVVHQVYVLKRPHVDEFLQRMGELFECVLFTASLAKYADPVADLLDKWGAFRARLFRESCVFHRGNYVKDLSRLGRDLRRVLILDNSPASYVFHPDNAVPVASWFDNMSDTELHDLLPFFEQLSRVDDVYSVLRQ
Oligomeric state: Hetero 2-mer
Stoichiometry: A1, B1
Experimental method: X-RAY DIFFRACTION
Refinement resolution (Å): 2.58
Average B factor: 38.2103
Crystallization method: VAPOR DIFFUSION, SITTING DROP
Crystallization temperature (K): 298
Crystal growth procedure: 30% PEG 3350
0.2 M Magnesium acetate
Matthews coefficient: 3.35
Solvent content (%): 63.32
Ligand: MAGNESIUM ION (MG)
Ligand formula: Mg
Ligand molecular weight: 24.305
Ligand SMILES: [Mg+2]
Ligand InChI: InChI=1S/Mg/q+2
Release date: 2018-09-26
Crystal structure of human 14-3-3 beta in complex with CFTR R-domain peptide pS753-pS768 (PDB entry 6HEP)
Macromolecule: 14-3-3 protein beta/alpha
Type: Protein, polypeptide(L)
Source organism: Homo sapiens
Sequence length: 235 residues
Sequence: MGSMTMDKSELVQKAKLAEQAERYDDMAAAMKAVTEQGHELSNEERNLLSVAYKNVVGARRSSWRVISSIEQKTERNEKKQQMGKEYREKIEAELQDICNDVLELLDKYLIPNATQPESKVFYLKMKGDYFRYLSEVASGDNKQTTVSNSQQAYQEAFEISKKEMQPTHPIRLGLALNFSVFYYEILNSPEKACSLAKTAFDEAIAELDTLNEESYKDSTLIMQLLRDNLTLWTS
Oligomeric state: Hetero 3-mer
Stoichiometry: A2, B1
Experimental method: X-RAY DIFFRACTION
Refinement resolution (Å): 1.86
R work: 0.201
R free: 0.251
Crystallization method: VAPOR DIFFUSION, SITTING DROP
Crystallization pH: 8
Crystallization temperature (K): 278
Crystal growth procedure: 0.1M Tris, 25% v/v PEG350 MME
Matthews coefficient: 2.25
Solvent content (%): 45.35
Ligand: 2-{2-[2-2-(METHOXY-ETHOXY)-ETHOXY]-ETHOXY}-ETHANOL (ETE)
Ligand formula: C9 H20 O5
Ligand molecular weight: 208.252
Ligand SMILES: COCCOCCOCCOCCO
Ligand InChI: InChI=1S/C9H20O5/c1-11-4-5-13-8-9-14-7-6-12-3-2-10/h10H,2-9H2,1H3
Release date: 2018-10-24
Crystal structure of Endoplasmic Reticulum Aminopeptidase 2 (ERAP2) in complex with a hydroxamic derivative ligand (PDB entry 5J6S)
Macromolecule: Endoplasmic reticulum aminopeptidase 2
Type: Protein, polypeptide(L)
Source organism: Homo sapiens
EC number: 3.4.11
Sequence length: 967 residues
Sequence: MFHSSAMVNSHRKPMFNIHRGFYCLTAILPQICICSQFSVPSSYHFTEDPGAFPVATNGERFPWQELRLPSVVIPLHYDLFVHPNLTSLDFVASEKIEVLVSNATQFIILHSKDLEITNATLQSEEDSRYMKPGKELKVLSYPAHEQIALLVPEKLTPHLKYYVAMDFQAKLGDGFEGFYKSTYRTLGGETRILAVTDFEPTQARMAFPCFDEPLFKANFSIKIRRESRHIALSNMPKVKTIELEGGLLEDHFETTVKMSTYLVAYIVCDFHSLSGFTSSGVKVSIYASPDKRNQTHYALQASLKLLDFYEKYFDIYYPLSKLDLIAIPDFAPGAMENWGLITYRETSLLFDPKTSSASDKLWVTRVIAHELAHQWFGNLVTMEWWNDIWLNEGFAKYMELIAVNATYPELQFDDYFLNVCFEVITKDSLNSSRPISKPAETPTQIQEMFDEVSYNKGACILNMLKDFLGEEKFQKGIIQYLKKFSYRNAKNDDLWSSLSNSCLESDFTSGGVCHSDPKMTSNMLAFLGENAEVKEMMTTWTLQKGIPLLVVKQDGCSLRLQQERFLQGVFQEDPEWRALQERYLWHIPLTYSTSSSNVIHRHILKSKTDTLDLPEKTSWVKFNVDSNGYYIVHYEGHGWDQLITQLNQNHTLLRPKDRVGLIHDVFQLVGAGRLTLDKALDMTYYLQHETSSPALLEGLSYLESFYHMMDRRNISDISENLKRYLLQYFKPVIDRQSWSDKGSVWDRMLRSALLKLACDLNHAPCIQKAAELFSQWMESSGKLNIPTDVLKIVYSVGAQTTAGWNYLLEQYELSMSSAEQNKILYALSTSKHQEKLLKLIELGMEGKVIKTQNLAALLHAIARRPKGQQLAWDFVRENWTHLLKKFDLGSYDIRMIISGTTAHFSSKDKLQEVKLFFESLEAQGSHLDIFQTVLETITKNIKWLEKNLPTLRTWLMVNTRHHHHHH
Oligomeric state: Monomer
Stoichiometry: A1
Experimental method: X-RAY DIFFRACTION
Refinement resolution (Å): 2.8
R work: 0.2049
R free: 0.2756
Crystallization method: VAPOR DIFFUSION
Crystallization pH: 6.3
Crystallization temperature (K): 277
Crystal growth procedure: 7 %(w/v) PEG 8000, 20 %(v/v) ethylene glycol, 59 mM MES, 41 mM imidazole
Matthews coefficient: 2.82
Solvent content (%): 56.43
Ligand: ZINC ION (ZN)
Ligand formula: Zn
Ligand molecular weight: 65.409
Ligand SMILES: [Zn+2]
Ligand InChI: InChI=1S/Zn/q+2
Release date: 2017-03-15
Sterol carrier protein Artifical metalloenzyme incorporating Q111C mutation coupled to 2,2'-bipyridine (PDB entry 8AF3)
Macromolecule: Enoyl-CoA hydratase 2
Type: Protein, polypeptide(L)
Source organism: Homo sapiens
EC number: 4.2.1.107
Sequence length: 120 residues
Sequence: MEGGKLQSTFVFEEIGRRLKDIGPEVVKKVNAVFEWHITKGGNIGAKWTIDLKSGSGKVYQGPAKGAADTTIILSDEDFMEVVLGKLDPQKAFFSGRLKARGNIMLSQKLCMILKDYAKL
Oligomeric state: Monomer
Stoichiometry: A1
Experimental method: X-RAY DIFFRACTION
Refinement resolution (Å): 1.52
R work: 0.2266
R free: 0.2389
Average B factor: 56.8164
Crystallization method: VAPOR DIFFUSION, HANGING DROP
Crystallization pH: 5.6
Crystallization temperature (K): 278
Crystal growth procedure: well solution 2.3M ammonium sulphate, 100 mM citric acid pH 5.6 and 200 mM NaCl
Matthews coefficient: 2.11
Solvent content (%): 41.79
Ligand: FRAGMENT OF TRITON X-100 (TRT)
Ligand formula: C21 H36 O4
Ligand molecular weight: 352.508
Ligand SMILES: CC(C)(C)CC(C)(C)c1ccc(cc1)OCCOCCOCCOC
Ligand InChI: InChI=1S/C21H36O4/c1-20(2,3)17-21(4,5)18-7-9-19(10-8-18)25-16-15-24-14-13-23-12-11-22-6/h7-10H,11-17H2,1-6H3
Release date: 2023-08-16
Crystal Structure of human cyclic GMP-AMP synthase in complex with 8-chloro-2-(2-hydroxyphenyl)quinoline-4-carboxylic acid (PDB entry 7FU3)
Macromolecule: Cyclic GMP-AMP synthase
Type: Protein, polypeptide(L)
Source organism: Homo sapiens
EC number: 2.7.7.86
Sequence length: 362 residues
Sequence: GASKLRAVLEKLKLSRDDISTAAGMVKGVVDHLLLRLKCDSAFRGVGLLNTGSYYEHVKISAPNEFDVMFKLEVPRIQLEEYSNTRAYYFVKFKRNPKENPLSQFLEGEILSASKMLSKFRKIIKEEINDIKDTDVIMKRKRGGSPAVTLLISEKISVDITLALESKSSWPASTQEGLRIQNWLSAKVRKQLRLKPFYLVPKHAKEGNGFQEETWRLSFSHIEKEILNNHGKSKTCCENKEEKCCRKDCLKLMKYLLEQLKERFKDKKHLDKFSSYHVKTAFFHVCTQNPQDSQWDRKDLGLCFDNCVTYFLQCLRTEKLENYFIPEFNLFSSNLIDKRSKEFLTKQIEYERNNEFPVFDEF
Oligomeric state: Monomer
Stoichiometry: A1
Experimental method: X-RAY DIFFRACTION
Refinement resolution (Å): 1.822
R work: 0.1937
R free: 0.2644
Average B factor: 58.5103
Crystallization method: VAPOR DIFFUSION, SITTING DROP
Crystallization pH: 7
Crystallization temperature (K): 293
Crystal growth procedure: 10-12 mg/mL protein in 25 mM Tris/HCl pH7.5, 500mM NaCl, 2mM TCEP, supplemented with 10x molar excess of ligand and, if needed, with 10 mM MgCl2 and 5mM ATP, then mixed 1:1 with reservoir of the Procomplex screen. Several conditions resulted in crystals.
Matthews coefficient: 2.07
Solvent content (%): 40.47
Ligand: ZINC ION (ZN)
Ligand formula: Zn
Ligand molecular weight: 65.409
Ligand SMILES: [Zn+2]
Ligand InChI: InChI=1S/Zn/q+2
Release date: 2024-02-21