satarupa22/MacromolecularLigandDB huggingface dataset:
Crystal structure of PIM1 in complex with a Pyrrolo-Pyrazinone compound (PDB entry 7ZUN)
Macromolecule: Isoform 2 of Serine/threonine-protein kinase pim-1
Type: Protein, polypeptide(L)
Source organism: Homo sapiens
EC number: 2.7.11.1
Sequence length: 314 residues
Sequence: GPLLSKINSLAHLRAAPCNDLHATKLAPGKEKEPLESQYQVGPLLGSGGFGSVYSGIRVSDNLPVAIKHVEKDRISDWGELPNGTRVPMEVVLLKKVSSGFSGVIRLLDWFERPDSFVLILERPEPVQDLFDFITERGALQEELARSFFWQVLEAVRHCHNCGVLHRDIKDENILIDLNRGELKLIDFGSGALLKDTVYTDFDGTRVYSPPEWIRYHRYHGRSAAVWSLGILLYDMVCGDIPFEHDEEIIRGQVFFRQRVSSECQHLIRWCLALRPSDRPTFEEIQNHPWMQDVLLPQETAEIHLHSLSPGPSK
Oligomeric state: Monomer
Stoichiometry: A1
Experimental method: X-RAY DIFFRACTION
Refinement resolution (Å): 2.5
R work: 0.1744
R free: 0.235
Average B factor: 47.926
Crystallization method: VAPOR DIFFUSION
Crystallization pH: 7.6
Crystallization temperature (K): 293
Crystal growth procedure: 20% PEG 3350K, 0.3 M NACL, 0.1 M TRIS-HCL PH 7.6
Matthews coefficient: 2.91
Solvent content (%): 57.78
Ligand: (4~{S})-4-(2-azanylethyl)-6-phenyl-7-[3-(trifluoromethyloxy)phenyl]-3,4-dihydropyrrolo[1,2-a]pyrazin-1-ol (JYO)
Ligand formula: C22 H20 F3 N3 O2
Ligand molecular weight: 415.408
Ligand SMILES: c1ccc(cc1)c2c(cc3n2C(CN=C3O)CCN)c4cccc(c4)OC(F)(F)F
Ligand InChI: InChI=1S/C22H20F3N3O2/c23-22(24,25)30-17-8-4-7-15(11-17)18-12-19-21(29)27-13-16(9-10-26)28(19)20(18)14-5-2-1-3-6-14/h1-8,11-12,16H,9-10,13,26H2,(H,27,29)/t16-/m0/s1
Release date: 2022-10-05
Structure of the catalytic domain of PARP1 in complex with niraparib (PDB entry 7KK5)
Macromolecule: Poly [ADP-ribose] polymerase 1
Type: Protein, polypeptide(L)
Source organism: Homo sapiens
EC number: 2.4.2.30
Sequence length: 352 residues
Sequence: GSKSKLPKPVQDLIKMIFDVESMKKAMVEYEIDLQKMPLGKLSKRQIQAAYSILSEVQQAVSQGSSDSQILDLSNRFYTLIPHDFGMKKPPLLNNADSVQAKVEMLDNLLDIEVAYSLLRGGSDDSSKDPIDVNYEKLKTDIKVVDRDSEEAEIIRKYVKNTHATTHNAYDLEVIDIFKIEREGECQRYKPFKQLHNRRLLWHGSRTTNFAGILSQGLRIAPPEAPVTGYMFGKGIYFADMVSKSANYCHTSQGDPIGLILLGEVALGNMYELKHASHISKLPKGKHSVKGLGKTTPDPSANISLDGVDVPLGTGISSGVNDTSLLYNEYIVYDIAQVNLKYLLKLKFNFKT
Oligomeric state: Monomer
Stoichiometry: A1
Experimental method: X-RAY DIFFRACTION
Refinement resolution (Å): 1.7
R work: 0.206
R free: 0.238
Average B factor: 38.64
Crystallization method: VAPOR DIFFUSION
Crystallization temperature (K): 294
Crystal growth procedure: Salt: 0.2 M Ammonium sulfate
Buffer: 0.1 M HEPES (pH 7.50)
Precipitant: 25.0 %w/v PEG 3350
Matthews coefficient: 2.54
Solvent content (%): 51.64
Ligand: 2-{4-[(3S)-piperidin-3-yl]phenyl}-2H-indazole-7-carboxamide (3JD)
Ligand formula: C19 H20 N4 O
Ligand molecular weight: 320.388
Ligand SMILES: c1cc2cn(nc2c(c1)C(=O)N)c3ccc(cc3)C4CCCNC4
Ligand InChI: InChI=1S/C19H20N4O/c20-19(24)17-5-1-3-15-12-23(22-18(15)17)16-8-6-13(7-9-16)14-4-2-10-21-11-14/h1,3,5-9,12,14,21H,2,4,10-11H2,(H2,20,24)/t14-/m1/s1
Release date: 2021-01-06
Structure of human PARP1 catalytic domain bound to a quinazoline-2,4(1H,3H)-dione inhibitor (PDB entry 5KPN)
Macromolecule: Poly [ADP-ribose] polymerase 1
Type: Protein, polypeptide(L)
Source organism: Homo sapiens
EC number: 2.4.2.30
Sequence length: 352 residues
Sequence: HMKSKLPKPVQDLIKMIFDVESMKKAMVEYEIDLQKMPLGKLSKRQIQAAYSILSEVQQAVSQGSSDSQILDLSNRFYTLIPHDFGMKKPPLLNNADSVQAKAEMLDNLLDIEVAYSLLRGGSDDSSKDPIDVNYEKLKTDIKVVDRDSEEAEIIRKYVKNTHATTHNAYDLEVIDIFKIEREGECQRYKPFKQLHNRRLLWHGSRTTNFAGILSQGLRIAPPEAPVTGYMFGKGIYFADMVSKSANYCHTSQGDPIGLILLGEVALGNMYELKHASHISKLPKGKHSVKGLGKTTPDPSANISLDGVDVPLGTGISSGVNDTSLLYNEYIVYDIAQVNLKYLLKLKFNFKT
Oligomeric state: Monomer
Stoichiometry: A1
Experimental method: X-RAY DIFFRACTION
Refinement resolution (Å): 2.3
R work: 0.23323
R free: 0.29293
Average B factor: 25.485
Crystallization method: VAPOR DIFFUSION, HANGING DROP
Crystallization pH: 7.5
Crystallization temperature (K): 298
Crystal growth procedure: 2.5M AMMONIUM SULFATE, 100mM TRIS
Matthews coefficient: 2.35
Solvent content (%): 47.59
Ligand: 1-[[4-fluoranyl-3-(3-oxidanylidene-4-propyl-piperazin-1-yl)carbonyl-phenyl]methyl]quinazoline-2,4-dione (6WX)
Ligand formula: C23 H23 F N4 O4
Ligand molecular weight: 438.452
Ligand SMILES: CCCN1CCN(CC1=O)C(=O)c2cc(ccc2F)CN3c4ccccc4C(=O)NC3=O
Ligand InChI: InChI=1S/C23H23FN4O4/c1-2-9-26-10-11-27(14-20(26)29)22(31)17-12-15(7-8-18(17)24)13-28-19-6-4-3-5-16(19)21(30)25-23(28)32/h3-8,12H,2,9-11,13-14H2,1H3,(H,25,30,32)
Release date: 2016-12-21
Crystal structure of JAK2 JH2-V617F in complex with Reversine (PDB entry 8BAK)
Macromolecule: Tyrosine-protein kinase JAK2
Type: Protein, polypeptide(L)
Source organism: Homo sapiens
EC number: 2.7.10.2
Sequence length: 289 residues
Sequence: VFHKIRNEDLIFNESLGQGTFTKIFKGVRREVGDYGQLHETEVLLKVLDKAHRNYSESFFEAASMMSKLSHKHLVLNYGVCFCGDENILVQEFVKFGSLDTYLKKNKNCINILWKLEVAKQLAWAMHFLEENTLIHGNVCAKNILLIREEDRKTGNPPFIKLSDPGISITVLPKDILQERIPWVPPECIENPKNLNLATDKWSFGTTLWEICSGGDKPLSALDSQRKLQFYEDRHQLPAPKAAELANLINNCMDYEPDHRPSFRAIIRDLNSLFTPDLVPRGSHHHHHH
Oligomeric state: Monomer
Stoichiometry: A1
Experimental method: X-RAY DIFFRACTION
Refinement resolution (Å): 1.65
R work: 0.1841
R free: 0.2066
Average B factor: 39.54
Crystallization method: VAPOR DIFFUSION, HANGING DROP
Crystallization pH: 8
Crystallization temperature (K): 277
Crystal growth procedure: 0.1M Tris pH 8, 20% PEG4000, 0.2M Na-acetate
Matthews coefficient: 2.75
Solvent content (%): 55.31
Ligand: GLYCEROL (GOL)
Ligand formula: C3 H8 O3
Ligand molecular weight: 92.094
Ligand SMILES: C(C(CO)O)O
Ligand InChI: InChI=1S/C3H8O3/c4-1-3(6)2-5/h3-6H,1-2H2
Release date: 2023-02-01
Crystal structure of Sirt2 in complex with selective inhibitor A2I (PDB entry 5YQL)
Macromolecule: NAD-dependent protein deacetylase sirtuin-2
Type: Protein, polypeptide(L)
Source organism: Homo sapiens
EC number: 3.5.1
Sequence length: 306 residues
Sequence: GASGSERLLDELTLEGVARYMQSERCRRVICLVGAGISTSAGIPDFRSPSTGLYDNLEKYHLPYPEAIFEISYFKKHPEPFFALAKELYPGQFKPTICHYFMRLLKDKGLLLRCYTQNIDTLERIAGLEQEDLVEAHGTFYTSHCVSASCRHEYPLSWMKEKIFSEVTPKCEDCQSLVKPDIVFFGESLPARFFSCMQSDFLKVDLLLVMGTSLQVQPFASLISKAPLSTPRLLINKEKAGQSDPFLGMIMGLGGGMDFDSKKAYRDVAWLGECDQGCLALAELLGWKKELEDLVRREHASIDAQS
Oligomeric state: Monomer
Stoichiometry: A1
Experimental method: X-RAY DIFFRACTION
Refinement resolution (Å): 1.601
R work: 0.1577
R free: 0.1853
Crystallization method: VAPOR DIFFUSION, HANGING DROP
Crystallization temperature (K): 293
Crystal growth procedure: 0.2M Magnesium Formate, 23-30% (v/v) Polyethylene glycol 3350
Matthews coefficient: 2.15
Solvent content (%): 42.78
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: 2018-10-17
Human REXO2 bound to pAA (PDB entry 6N6J)
Macromolecule: RNA exonuclease 2 homolog,Small fragment nuclease
Type: Protein, polypeptide(L)
Source organism: Homo sapiens
EC number: 3.1
Sequence length: 205 residues
Sequence: MAAGESMAQRMVWVDLEMTGLDIEKDQIIEMACLITDSDLNILAEGPNLIIKQPDELLDSMSDWCKEHHGKSGLTKAVKESTITLQQAEYEFLSFVRQQTPPGLCPLAGNSVHEDKKFLDKYMPQFMKHLHYRIIDVSTVKELCRRWYPEEYEFAPKKAASHRALDDISESIKELQFYRNNIFKKKIDEKKRKIIENGENEKTVS
Oligomeric state: Monomer
Stoichiometry: A1
Experimental method: X-RAY DIFFRACTION
Refinement resolution (Å): 1.317
R work: 0.1528
R free: 0.1701
Average B factor: 19.686
Crystallization method: VAPOR DIFFUSION, HANGING DROP
Crystallization pH: 5.5
Crystallization temperature (K): 277
Crystal growth procedure: 0.2 M sodium malonate (pH 5.5) and 15-20% polyethylene glycol 3350, 25% glycerol
Matthews coefficient: 2.56
Solvent content (%): 51.87
Ligand: GLYCEROL (GOL)
Ligand formula: C3 H8 O3
Ligand molecular weight: 92.094
Ligand SMILES: C(C(CO)O)O
Ligand InChI: InChI=1S/C3H8O3/c4-1-3(6)2-5/h3-6H,1-2H2
Release date: 2019-06-12
Crystal Structure of Factor VIIa in complex with 2-(4-ethoxy-3-methoxyphenyl)-2-(isoquinolin-6-ylamino)acetic acid (PDB entry 5PB0)
Macromolecule: Coagulation factor VII light chain
Type: Protein, polypeptide(L)
Source organism: Homo sapiens
EC number: 3.4.21.21
Sequence length: 64 residues
Sequence: LICVNENGGCEQYCSDHTGTKRSCRCHEGYSLLADGVSCTPTVEYPCGKIPILEKRNASKPQGR
Oligomeric state: Hetero 2-mer
Stoichiometry: A1, B1
Experimental method: X-RAY DIFFRACTION
Refinement resolution (Å): 1.98
R work: 0.1675
R free: 0.1931
Average B factor: 25.314
Crystallization method: VAPOR DIFFUSION, SITTING DROP
Crystallization pH: 8.5
Crystallization temperature (K): 277
Crystal growth procedure: 16 mg/ml protein in 20mM Tris/HCl pH 8.4, 5 mM benzamidine, 0.1 M NaCl, 50 mM CaCl2 mixed 1+1 with 32-35% AMMONIUM SULPHATE, 2% PEG 4000, 0.1 M Bicine-NaOH pH 8.5, 15% glycerol
Matthews coefficient: 3.76
Solvent content (%): 67.24
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: 2017-06-21
Cocrystal structure of human CaMKII-alpha (CAMK2A)kinase domain and GluN2B(S1303D) (PDB entry 7KL2)
Macromolecule: Calcium/calmodulin-dependent protein kinase type II subunit alpha
Type: Protein, polypeptide(L)
Source organism: Homo sapiens
EC number: 2.7.11.17
Sequence length: 268 residues
Sequence: TRFTEEYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIFDLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRNLKPENLLLASKLKGAAVKLADFGLAIEVEGEQQAWFGFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYKQIKAGAYDFPSPEWDTVTPEAKDLINKMLTINPSKRITAAEALKHPWISHR
Oligomeric state: Hetero 2-mer
Stoichiometry: A1, B1
Experimental method: X-RAY DIFFRACTION
Refinement resolution (Å): 2.56
R work: 0.2439
R free: 0.293
Average B factor: 45.386
Crystallization method: VAPOR DIFFUSION, HANGING DROP
Crystallization pH: 6.5
Crystallization temperature (K): 277
Crystal growth procedure: 0.15 M DL-Malic acid pH 7, 20% PEG 3350
Matthews coefficient: 2.36
Solvent content (%): 47.79
Release date: 2020-12-23
Biochemical, Cellular and Structural Characterization of Novel ERK3 Inhibitors (PDB entry 6YLC)
Macromolecule: Mitogen-activated protein kinase 6
Type: Protein, polypeptide(L)
Source organism: Homo sapiens
EC number: 2.7.11.24
Sequence length: 319 residues
Sequence: MNIHGFDLGSRYMDLKPLGCGGNGLVFSAVDNDCDKRVAIKKIVLTDPQSVKHALREIKIIRRLDHDNIVKVFEILGPSGSQLTDDVGSLTELNSVYIVQEYMETDLANVLEQGPLLEEHARLFMYQLLRGLKYIHSANVLHRDLKPANLFINTEDLVLKIGDFGLARIMDPHYSHKGHLSEGLVTKWYRSPRLLLSPNNYTKAIDMWAAGCIFAEMLTGKTLFAGAHELEQMQLILESIPVVHEEDRQELLSVIPVYIRNDMTEPHKPLTQLLPGISREAVDFLEQILTFSPMDRLTAEEALSHPYMSIYSFPMDEPI
Oligomeric state: Monomer
Stoichiometry: A1
Experimental method: X-RAY DIFFRACTION
Refinement resolution (Å): 2.43
R work: 0.189
R free: 0.231
Average B factor: 91.82
Crystallization method: VAPOR DIFFUSION, SITTING DROP
Crystallization pH: 6
Crystallization temperature (K): 277
Crystal growth procedure: 100 mM Bis-Tris (pH 6), 100 mM Lithium acetate, 18%v/v Sokalan CP42, 3%v/v Glycerol
Matthews coefficient: 2.49
Solvent content (%): 50.67
Ligand: 5-fluoranyl-2-[5-[[1-(1-methylpiperidin-4-yl)pyrazol-4-yl]amino]-[1,2,3]triazolo[4,5-d]pyrimidin-3-yl]benzenecarbonitrile (OXW)
Ligand formula: C20 H19 F N10
Ligand molecular weight: 418.43
Ligand SMILES: CN1CCC(CC1)n2cc(cn2)Nc3ncc4c(n3)n(nn4)c5ccc(cc5C#N)F
Ligand InChI: InChI=1S/C20H19FN10/c1-29-6-4-16(5-7-29)30-12-15(10-24-30)25-20-23-11-17-19(26-20)31(28-27-17)18-3-2-14(21)8-13(18)9-22/h2-3,8,10-12,16H,4-7H2,1H3,(H,23,25,26)
Release date: 2020-09-23
Crystal structure of the IBR-RING2 domain of HOIL-1 (PDB entry 8BVL)
Macromolecule: RanBP-type and C3HC4-type zinc finger-containing protein 1
Type: Protein, polypeptide(L)
Source organism: Homo sapiens
EC number: 2.3.2.31
Sequence length: 145 residues
Sequence: GPSYHCKTPDCKGWCFFEDDVNEFTCPVCFHVNCLLCKAIHEQMNCKEYQEDLALRAQNDVAARQTTEMLKVMLQQGEAMRCPQCQIVVQKKDGCDWIRCTVCHTEICWVTKGPRWGPGGPGDTSGGCRCRVNGIPCHPSCQNCH
Oligomeric state: Monomer
Stoichiometry: A1
Experimental method: X-RAY DIFFRACTION
Refinement resolution (Å): 2.24
R work: 0.2341
R free: 0.2961
Crystallization method: VAPOR DIFFUSION, SITTING DROP
Crystallization pH: 7
Crystallization temperature (K): 291
Crystal growth procedure: 200 mM magnesium chloride hexahydrate
100mM Tris-HCl pH 7.0
10% PEG 8000
Matthews coefficient: 2.83
Solvent content (%): 56.52
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: 2023-01-18
The DDR1 Kinase Domain Bound To SR302 (PDB entry 7BCM)
Macromolecule: Epithelial discoidin domain-containing receptor 1
Type: Protein, polypeptide(L)
Source organism: Homo sapiens
EC number: 2.7.10.1
Sequence length: 315 residues
Sequence: SMPRVDFPRSRLRFKEKLGEGQFGEVHLCEVDSPQDLVSLDFPLNVRKGHPLLVAVKILRPDATKNARNDFLKEVKIMSRLKDPNIIRLLGVCVQDDPLCMITDYMENGDLNQFLSAHQLEDKAAEGAPGDGQAAQGPTISYPMLLHVAAQIASGMRYLATLNFVHRDLATRNCLVGENFTIKIADFGMSRNLYAGDYYRVQGRAVLPIRWMAWECILMGKFTTASDVWAFGVTLWEVLMLCRAQPFGQLTDEQVIENAGEFFRDQGRQVYLSRPPACPQGLYELMLRCWSRESEQRPPFSQLHRFLAEDALNTV
Oligomeric state: Monomer
Stoichiometry: A1
Experimental method: X-RAY DIFFRACTION
Refinement resolution (Å): 2.3
R work: 0.243
R free: 0.308
Average B factor: 33.79
Crystallization method: VAPOR DIFFUSION, SITTING DROP
Crystallization pH: 7.5
Crystallization temperature (K): 277
Crystal growth procedure: 20% PEG10,000
0.1 M HEPES pH 7.5
Matthews coefficient: 2.74
Solvent content (%): 55.07
Ligand: ~{N}-[[4-[[(2~{S})-4-cyclohexyl-1-[[(3~{S})-1-methylsulfonylpiperidin-3-yl]amino]-1-oxidanylidene-butan-2-yl]carbamoyl]phenyl]methyl]imidazo[1,2-a]pyridine-3-carboxamide (TBK)
Ligand formula: C32 H42 N6 O5 S
Ligand molecular weight: 622.778
Ligand SMILES: CS(=O)(=O)N1CCCC(C1)NC(=O)C(CCC2CCCCC2)NC(=O)c3ccc(cc3)CNC(=O)c4cnc5n4cccc5
Ligand InChI: InChI=1S/C32H42N6O5S/c1-44(42,43)37-18-7-10-26(22-37)35-31(40)27(17-14-23-8-3-2-4-9-23)36-30(39)25-15-12-24(13-16-25)20-34-32(41)28-21-33-29-11-5-6-19-38(28)29/h5-6,11-13,15-16,19,21,23,26-27H,2-4,7-10,14,17-18,20,22H2,1H3,(H,34,41)(H,35,40)(H,36,39)/t26-,27-/m0/s1
Release date: 2021-03-03
Cocrystal structure of human CaMKII-alpha (CAMK2A)kinase domain and GluN2B(S1303D) (PDB entry 7UIS)
Macromolecule: Calcium/calmodulin-dependent protein kinase type II subunit alpha
Type: Protein, polypeptide(L)
Source organism: Homo sapiens
EC number: 2.7.11.17
Sequence length: 268 residues
Sequence: TRFTEEYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIFDLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRNLKPENLLLASKLKGAAVKLADFGLAIEVEGEQQAWFGFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYKQIKAGAYDFPSPEWDTVTPEAKDLINKMLTINPSKRITAAEALKHPWISHR
Oligomeric state: Hetero 2-mer
Stoichiometry: A1, B1
Experimental method: X-RAY DIFFRACTION
Refinement resolution (Å): 2.58
R work: 0.2173
R free: 0.2675
Average B factor: 39.422
Crystallization method: VAPOR DIFFUSION, HANGING DROP
Crystallization pH: 7
Crystallization temperature (K): 277
Crystal growth procedure: 0.1 M Bis-tris propane pH 6.5, 0.2 M Sodium chloride, 25% PEG 3350
Matthews coefficient: 2.09
Solvent content (%): 41.09
Release date: 2022-04-06
The FK1 domain of FKBP51 in complex with peptide-inhibitor hit QFPFV (PDB entry 7ETT)
Macromolecule: peptide-inhibitor hit
Type: Protein, polypeptide(L)
Source organism: synthetic construct
Sequence length: 5 residues
Sequence: QFPFV
Oligomeric state: Hetero 2-mer
Stoichiometry: A1, B1
Experimental method: X-RAY DIFFRACTION
Refinement resolution (Å): 1.5
R work: 0.185
R free: 0.1977
Average B factor: 15.927
Crystallization method: VAPOR DIFFUSION, HANGING DROP
Crystallization temperature (K): 298
Crystal growth procedure: 30%-36% PEG 3350, 0.2 M Ammonium Acetate and 0.1 M HEPES pH 7.5
Matthews coefficient: 2.21
Solvent content (%): 44.45
Release date: 2022-02-23
Notum_Piperine complex (PDB entry 7BLW)
Macromolecule: Palmitoleoyl-protein carboxylesterase NOTUM
Type: Protein, polypeptide(L)
Source organism: Homo sapiens
EC number: 3.1.1.98
Sequence length: 383 residues
Sequence: ETGSAQQLNEDLRLHLLLNTSVTCNDGSPAGYYLKESRGSRRWLLFLEGGWYCFNRENCDSRYDTMRRLMSSRDWPRTRTGTGILSSQPEENPYWWNANMVFIPYCSSDVWSGASSKSEKNEYAFMGALIIQEVVRELLGRGLSGAKVLLLAGSSAGGTGVLLNVDRVAEQLEKLGYPAIQVRGLADSGWFLDNKQYRHTDCVDTITCAPTEAIRRGIRYWNGVVPERCRRQFQEGEEWNCFFGYKVYPTLRSPVFVVQWLFDEAQLTVDNVHLTGQPVQEGLRLYIQNLGRELRHTLKDVPASFAPACLSHEIIIRSHWTDVQVKGTSLPRALHCWDRSLHDSHKASKTPLKGCPVHLVDSCPWPHCNPSCPTGTKHHHHHH
Oligomeric state: Monomer
Stoichiometry: A1
Experimental method: X-RAY DIFFRACTION
Refinement resolution (Å): 1.45
R work: 0.1741
R free: 0.2111
Average B factor: 25.2974
Crystallization method: VAPOR DIFFUSION, SITTING DROP
Crystallization temperature (K): 296
Crystal growth procedure: 1.5 M Ammonium Sulphate
0.1 M Sodium Citrate, pH4.2
Matthews coefficient: 2
Solvent content (%): 38.52
Ligand: (2E,4E)-5-(2H-1,3-benzodioxol-5-yl)-1-(piperidin-1-yl)penta-2,4-dien-1-one (AYR)
Ligand formula: C17 H19 N O3
Ligand molecular weight: 285.338
Ligand SMILES: c1cc2c(cc1C=CC=CC(=O)N3CCCCC3)OCO2
Ligand InChI: InChI=1S/C17H19NO3/c19-17(18-10-4-1-5-11-18)7-3-2-6-14-8-9-15-16(12-14)21-13-20-15/h2-3,6-9,12H,1,4-5,10-11,13H2/b6-2+,7-3+
Release date: 2022-03-02
Crystal structure of the catalytic domain of the proto-oncogene tyrosine-protein kinase MER in complex with inhibitor UNC2434 (PDB entry 5K0K)
Macromolecule: Tyrosine-protein kinase Mer
Type: Protein, polypeptide(L)
Source organism: Homo sapiens
EC number: 2.7.10.1
Sequence length: 313 residues
Sequence: MGSSHHHHHHSSGLVPRGSEELQNKLEDVVIDRNLLILGKILGEGEFGSVMEGNLKQEDGTSLKVAVKTMKLDNSSQREIEEFLSEAACMKDFSHPNVIRLLGVCIEMSSQGIPKPMVILPFMKYGDLHTYLLYSRLETGPKHIPLQTLLKFMVDIALGMEYLSNRNFLHRDLAARNCMLRDDMTVCVADFGLSKKIYSGDYYRQGRIAKMPVKWIAIESLADRVYTSKSDVWAFGVTMWEIATRGMTPYPGVQNHEMYDYLLHGHRLKQPEDCLDELYEIMYSCWRTDPLDRPTFSVLRLQLEKLLESLPDV
Oligomeric state: Monomer
Stoichiometry: A1
Experimental method: X-RAY DIFFRACTION
Refinement resolution (Å): 2.545
R work: 0.1979
R free: 0.2543
Average B factor: 56.6
Crystallization method: VAPOR DIFFUSION, SITTING DROP
Crystallization pH: 8.5
Crystallization temperature (K): 285.2
Crystal growth procedure: Protein at 32.5 mg/mL (in 20 mM Tris pH 8.0, 500 mM NaCl, 2mM BME) was incubated overnight with inhibitor at 2.5 mM final concentration, and then was mixed 1:1 with crystallization solution (27-33% (v/v) Peg 400, 200 mM MgCl2, 100 mM Tris pH 8.5).
Matthews coefficient: 2.21
Solvent content (%): 44.37
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: 2017-01-11
CDK2 in complex 9K-DOS (PDB entry 7ZPC)
Macromolecule: Cyclin-dependent kinase 2
Type: Protein, polypeptide(L)
Source organism: Homo sapiens
EC number: 2.7.11.22
Sequence length: 306 residues
Sequence: GPLGSPEFMENFQKVEKIGEGTYGVVYKARNKLTGEVVALKKIRLDTETEGVPSTAIREISLLKELNHPNIVKLLDVIHTENKLYLVFEFLHQDLKKFMDASALTGIPLPLIKSYLFQLLQGLAFCHSHRVLHRDLKPQNLLINTEGAIKLADFGLARAFGVPVRTYTHEVVTLWYRAPEILLGCKYYSTAVDIWSLGCIFAEMVTRRALFPGDSEIDQLFRIFRTLGTPDEVVWPGVTSMPDYKPSFPKWARQDFSKVVPPLDEDGRSLLSQMLHYDPNKRISAKAALAHPFFQDVTKPVPHLRL
Oligomeric state: Monomer
Stoichiometry: A1
Experimental method: X-RAY DIFFRACTION
Refinement resolution (Å): 1.4
R work: 0.2014
R free: 0.2211
Average B factor: 26.987
Crystallization method: VAPOR DIFFUSION, HANGING DROP
Crystallization pH: 7.5
Crystallization temperature (K): 293
Crystal growth procedure: 10MG/ML CDK2 10% V/V PEG3350, 50 MM      
HEPES/NAOH, 50 MM NA/K PHOSPHATE, PH 7.5
Matthews coefficient: 1.99
Solvent content (%): 38.04
Ligand: ~{N}-(1-methylpyrazol-4-yl)-5-phenyl-pyrazolo[1,5-a]pyrimidine-7-carboxamide (JLC)
Ligand formula: C17 H14 N6 O
Ligand molecular weight: 318.333
Ligand SMILES: Cn1cc(cn1)NC(=O)c2cc(nc3n2ncc3)c4ccccc4
Ligand InChI: InChI=1S/C17H14N6O/c1-22-11-13(10-19-22)20-17(24)15-9-14(12-5-3-2-4-6-12)21-16-7-8-18-23(15)16/h2-11H,1H3,(H,20,24)
Release date: 2023-02-01
Extracellular domain of type II Transforming Growth Factor Beta receptor in complex with 2-(2-Hydroxyethyl)NDSB-201 (PDB entry 4XJJ)
Macromolecule: TGF-beta receptor type-2
Type: Protein, polypeptide(L)
Source organism: Homo sapiens
EC number: 2.7.11.30
Sequence length: 112 residues
Sequence: MALCKFCDVRFSTCDNQKSCMSNCSITSICEKPQEVCVAVWRKNDENITLETVCHDPKLPYHDFILEDAASPTCIMKEKKKPGETFFMCSCSSDECNDNIIFSEEYNTSNPD
Oligomeric state: Monomer
Stoichiometry: A1
Experimental method: X-RAY DIFFRACTION
Refinement resolution (Å): 1.4
R work: 0.153
R free: 0.1853
Average B factor: 21.0997
Crystallization method: VAPOR DIFFUSION, HANGING DROP
Crystallization pH: 5
Crystallization temperature (K): 298
Crystal growth procedure: 100 mM sodium citrate, 30% PEG 2000
Matthews coefficient: 2.26
Solvent content (%): 45.55
Ligand: 3-[2-(2-hydroxyethyl)pyridinium-1-yl]propane-1-sulfonate (41D)
Ligand formula: C10 H15 N O4 S
Ligand molecular weight: 245.295
Ligand SMILES: c1cc[n+](c(c1)CCO)CCCS(=O)(=O)[O-]
Ligand InChI: InChI=1S/C10H15NO4S/c12-8-5-10-4-1-2-6-11(10)7-3-9-16(13,14)15/h1-2,4,6,12H,3,5,7-9H2
Release date: 2015-06-24
Nucleotide-bound structure of a functional construct of eukaryotic elongation factor 2 kinase. (PDB entry 8FNY)
Macromolecule: Eukaryotic elongation factor 2 kinase
Type: Protein, polypeptide(L)
Source organism: Homo sapiens
EC number: 2.7.11.20
Sequence length: 531 residues
Sequence: SSSGSPANSFHFKEAWKHAIQKAKHMPDPWAEFHLEDIATERATRHRYNAVTGEWLDDEVLIKMASQPFGRGAMRECFRTKKLSNFLHAQQWKGASNYVAKRYIEPVDRDVYFEDVRLQMEAKLWGEEYNRHKPPKQVDIMQMCIIELKDRPGKPLFHLEHYIEGKYIKYNSNSGFVRDDNIRLTPQAFSHFTFERSGHQLIVVDIQGVGDLYTDPQIHTETGTDFGDGNLGVRGMALFFYSHACNRICESMGLAPFDLSPRERDAVNQNTKLLQSAKTILRGTEEKCGGGGGGGNSSRLHLPRASAVALEVQRLNALDLEKKIGKSILGKVHLAMVRYHEGGRFCEKGEEWDQESAVFHLEHAANLGELEAIVGLGLMYSQLPHHILADVSLKETEENKTKGFDYLLKAAEAGDRQSMILVARAFDSGQNLSPDRCQDWLEALHWYNTALEMTDCDEGGEYDGMQDEPRYMMLAREAEMLFTGGYGLEKDPQRSGDLYTQAAEAAMEAMKGRLANQYYQKAEEAWAQMEE
Oligomeric state: Hetero 2-mer
Stoichiometry: A1, B1
Experimental method: X-RAY DIFFRACTION
Refinement resolution (Å): 2.22
R work: 0.2079
R free: 0.229
Average B factor: 35.33
Crystallization method: VAPOR DIFFUSION
Crystallization pH: 7.5
Crystallization temperature (K): 293
Crystal growth procedure: 100 mM Bis-trispropane, 100 mM NaF, 20.5 % w/v PEG-3350 (2protein/1solution)
Matthews coefficient: 2.6
Solvent content (%): 52.43
Ligand: ADENOSINE-5'-TRIPHOSPHATE (ATP)
Ligand formula: C10 H16 N5 O13 P3
Ligand molecular weight: 507.181
Ligand SMILES: c1nc(c2c(n1)n(cn2)C3C(C(C(O3)COP(=O)(O)OP(=O)(O)OP(=O)(O)O)O)O)N
Ligand InChI: InChI=1S/C10H16N5O13P3/c11-8-5-9(13-2-12-8)15(3-14-5)10-7(17)6(16)4(26-10)1-25-30(21,22)28-31(23,24)27-29(18,19)20/h2-4,6-7,10,16-17H,1H2,(H,21,22)(H,23,24)(H2,11,12,13)(H2,18,19,20)/t4-,6-,7-,10-/m1/s1
Release date: 2023-05-03
Crystal structure of human OAS3 domain I in complex with dsRNA (PDB entry 4S3N)
Macromolecule: 2'-5'-oligoadenylate synthase 3
Type: Protein, polypeptide(L)
Source organism: Homo sapiens
EC number: 2.7.7.84
Sequence length: 373 residues
Sequence: GPMDLYSTPAAALDRFVARKLQPRKEFVEKARRALGALAAALRERGGRLGAAAPRVLKTVKGGSSGRGTALKGGCDSELVIFLDCFKSYVDQRARRAEILSEMRASLESWWQNPVPGLRLTFPEQSVPGALQFRLTSVDLEDWMDVSLVPAFNVLGQAGSGVKPKPQVYSTLLNSGCQGGEHAACFTELRRNFVNIRPAKLKNLILLVKHWYHQVCLQGLWKETLPPVYALELLTIFAWEQGCKKDAFSLAEGLRTVLGLIQQHQHLCVFWTVNYGFEDPAVGQFLQRQLKRPRPVILDPADPTWDLGNGAAWHWDLLAQEAASCYDHPCFLRGMGDPVQSWKGPGLPRAGCSGLGHPIQLDPNQKTPENSKS
Oligomeric state: Monomer
Stoichiometry: A1
Experimental method: X-RAY DIFFRACTION
Refinement resolution (Å): 2.0
R work: 0.1818
R free: 0.2113
Crystallization method: VAPOR DIFFUSION, HANGING DROP
Crystallization pH: 8.5
Crystallization temperature (K): 293.15
Crystal growth procedure: 200 mM trisodium citrate, 150 mM NaCl, 12% PEG 3350, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 293.15K
Matthews coefficient: 3.02
Solvent content (%): 59.25
Release date: 2015-03-25