satarupa22/MacromolecularLigandDB huggingface dataset:
Mutant Human DNA Polymerase Eta R61M Inserting dATP Opposite an 8-Oxoguanine Lesion (PDB entry 4YR2)
Macromolecule: DNA (5'-D(*AP*TP*(8OG)P*AP*TP*GP*AP*CP*GP*CP*T)-3')
Type: DNA, polydeoxyribonucleotide
Source organism: synthetic construct
Sequence length: 12 residues
Sequence: CATGATGACGCT
Oligomeric state: Monomer
Stoichiometry: A1
Experimental method: X-RAY DIFFRACTION
Refinement resolution (Å): 1.95
R work: 0.168
R free: 0.218
Crystallization method: VAPOR DIFFUSION, HANGING DROP
Crystallization pH: 6
Crystallization temperature (K): 291
Crystal growth procedure: NaMES (pH 6.0), polyethylene glycol monomethyl ether 2000, and calcium chloride
Matthews coefficient: 2.12
Solvent content (%): 42.09
Ligand: 2'-DEOXYADENOSINE 5'-TRIPHOSPHATE (DTP)
Ligand formula: C10 H16 N5 O12 P3
Ligand molecular weight: 491.182
Ligand SMILES: c1nc(c2c(n1)n(cn2)C3CC(C(O3)COP(=O)(O)OP(=O)(O)OP(=O)(O)O)O)N
Ligand InChI: InChI=1S/C10H16N5O12P3/c11-9-8-10(13-3-12-9)15(4-14-8)7-1-5(16)6(25-7)2-24-29(20,21)27-30(22,23)26-28(17,18)19/h3-7,16H,1-2H2,(H,20,21)(H,22,23)(H2,11,12,13)(H2,17,18,19)/t5-,6+,7+/m0/s1
Release date: 2015-05-13
Structural Insights into Substrate and Inhibitor Binding Sites in Human Indoleamine 2,3-Dioxygenase I (PDB entry 5WMU)
Macromolecule: Indoleamine 2,3-dioxygenase 1
Type: Protein, polypeptide(L)
Source organism: Homo sapiens
EC number: 1.13.11.52
Sequence length: 425 residues
Sequence: MSKEYHIDEEVGFALPNPQENLPDFYNDWMFIAKHLPDLIESGQLRERVEKLNMLSIDHLTDHKSQRLARLVLGCITMAYVWGKGHGDVRKVLPRNIAVPYCQLSKKLELPPILVYADCVLANWKKKDPNKPLTYENMDVLFSFRDGDCSKGFFLVSLLVEIAAASAIKVIPTVFKAMQMQERDTLLKALLEIASCLEKALQVFHQIHDHVNPKAFFSVLRIYLSGWKGNPQLSDGLVYEGFWEDPKEFAGGSAGQSSVFQCFDVLLGIQQTAGGGHAAQFLQDMRRYMPPAHRNFLCSLESNPSVREFVLSKGDAGLREAYDACVKALVSLRSYHLQIVTKYILIPASQQPKENKTSEDPSKLEAKGTGGTDLMNFLKTVRSTTEKSLLKEGKGELNSKLEGKPIPNPLLGLDSTRTGHHHHHH
Oligomeric state: Monomer
Stoichiometry: A1
Experimental method: X-RAY DIFFRACTION
Refinement resolution (Å): 2.4
R work: 0.21404
R free: 0.25791
Average B factor: 76.791
Crystallization method: MICROBATCH
Crystallization pH: 10
Crystallization temperature (K): 277.15
Crystal growth procedure: 100 mM Sodium thiosulfate, 100 mM pH 10.0 CAPS buffer, 20% (w/v) PEG 8000)
Matthews coefficient: 3.02
Solvent content (%): 59.29
Ligand: PROTOPORPHYRIN IX CONTAINING FE (HEM)
Ligand formula: C34 H32 Fe N4 O4
Ligand molecular weight: 616.487
Ligand SMILES: Cc1c2n3c(c1CCC(=O)O)C=C4C(=C(C5=[N]4[Fe]36[N]7=C(C=C8N6C(=C5)C(=C8C)C=C)C(=C(C7=C2)C)C=C)C)CCC(=O)O
Ligand InChI: InChI=1S/C34H34N4O4.Fe/c1-7-21-17(3)25-13-26-19(5)23(9-11-33(39)40)31(37-26)16-32-24(10-12-34(41)42)20(6)28(38-32)15-30-22(8-2)18(4)27(36-30)14-29(21)35-25;/h7-8,13-16H,1-2,9-12H2,3-6H3,(H4,35,36,37,38,39,40,41,42);/q;+2/p-2/b25-13-,26-13-,27-14-,28-15-,29-14-,30-15-,31-16-,32-16-;
Release date: 2017-12-06
Discovery of VX-509 (Decernotinib): A Potent and Selective Janus kinase (JAK) 3 Inhibitor for the Treatment of Autoimmune Disease (PDB entry 4YTI)
Macromolecule: Tyrosine-protein kinase JAK2
Type: Protein, polypeptide(L)
Source organism: Homo sapiens
EC number: 2.7.10.2
Sequence length: 296 residues
Sequence: GSHNMTQFEERHLKFLQQLGKGNFGSVEMCRYDPLQDNTGEVVAVKKLQHSTEEHLRDFEREIEILKSLQHDNIVKYKGVCYSAGRRNLKLIMEYLPYGSLRDYLQKHKERIDHIKLLQYTSQICKGMEYLGTKRYIHRDLATRNILVENENRVKIGDFGLTKVLPQDKEYYKVKEPGESPIFWYAPESLTESKFSVASDVWSFGVVLYELFTYIEKSKSPPAEFMRMIGNDKQGQMIVFHLIELLKNNGRLPRPDGCPDEIYMIMTECWNNNVNQRPSFRDLALRVDQIRDNMAG
Oligomeric state: Monomer
Stoichiometry: A1
Experimental method: X-RAY DIFFRACTION
Refinement resolution (Å): 2.52
R work: 0.2072
R free: 0.2172
Average B factor: 40.16
Crystallization method: VAPOR DIFFUSION, HANGING DROP
Crystallization temperature (K): 293
Crystal growth procedure: 1.7-2.1 DL-malic acid pH 7.0, 2mM DTT
Matthews coefficient: 2.41
Solvent content (%): 49.05
Ligand: (2R)-2-methyl-2-[[2-(1H-pyrrolo[2,3-b]pyridin-3-yl)pyrimidin-4-yl]amino]-N-[2,2,2-tris(fluoranyl)ethyl]butanamide (VJK)
Ligand formula: C18 H19 F3 N6 O
Ligand molecular weight: 392.378
Ligand SMILES: CCC(C)(C(=O)NCC(F)(F)F)Nc1ccnc(n1)c2c[nH]c3c2cccn3
Ligand InChI: InChI=1S/C18H19F3N6O/c1-3-17(2,16(28)25-10-18(19,20)21)27-13-6-8-23-15(26-13)12-9-24-14-11(12)5-4-7-22-14/h4-9H,3,10H2,1-2H3,(H,22,24)(H,25,28)(H,23,26,27)/t17-/m1/s1
Release date: 2015-08-12
Crystal structure of FGFR2 in complex with 1,3,5-triazine derivative (PDB entry 6LVK)
Macromolecule: Fibroblast growth factor receptor 2
Type: Protein, polypeptide(L)
Source organism: Homo sapiens
EC number: 2.7.10.1
Sequence length: 313 residues
Sequence: GSHMLAGVSEYELPEDPKWEFPRDKLTLGKPLGEGCFGQVVMAEAVGIDKDKPKEAVTVAVKMLKDDATEKDLSDLVSEMEMMKMIGKHKNIINLLGACTQDGPLYVIVEYASKGNLREYLRARRPPGMEYSYDINRVPEEQMTFKDLVSCTYQLARGMEYLASQKCIHRDLAARNVLVTENNVMKIADFGLARDINNIDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLMWEIFTLGGSPYPGIPVEELFKLLKEGHRMDKPANCTNELYMMMRDCWHAVPSQRPTFKQLVEDLDRILTLTTNEE
Oligomeric state: Monomer
Stoichiometry: A1
Experimental method: X-RAY DIFFRACTION
Refinement resolution (Å): 2.29
R work: 0.2035
R free: 0.247
Average B factor: 32.682
Crystallization method: VAPOR DIFFUSION, SITTING DROP
Crystallization pH: 8.5
Crystallization temperature (K): 296
Crystal growth procedure: Tris, Ammonium sulfate, PEG 8000
Matthews coefficient: 2.75
Solvent content (%): 55.24
Ligand: N-ethyl-2-[[4-[[4-(4-methylpiperazin-1-yl)-3-(2-morpholin-4-ylethoxy)phenyl]amino]-1,3,5-triazin-2-yl]amino]benzenesulfonamide (EVC)
Ligand formula: C28 H39 N9 O4 S
Ligand molecular weight: 597.732
Ligand SMILES: CCNS(=O)(=O)c1ccccc1Nc2ncnc(n2)Nc3ccc(c(c3)OCCN4CCOCC4)N5CCN(CC5)C
Ligand InChI: InChI=1S/C28H39N9O4S/c1-3-31-42(38,39)26-7-5-4-6-23(26)33-28-30-21-29-27(34-28)32-22-8-9-24(37-12-10-35(2)11-13-37)25(20-22)41-19-16-36-14-17-40-18-15-36/h4-9,20-21,31H,3,10-19H2,1-2H3,(H2,29,30,32,33,34)
Release date: 2020-04-08
Crystal structure of di-phosphorylated human CLK1 in complex with 5-(1-methyl-1H-indol-3-yl)pyrimidin-4-amine (PDB entry 6R6X)
Macromolecule: Dual specificity protein kinase CLK1
Type: Protein, polypeptide(L)
Source organism: Homo sapiens
EC number: 2.7.12.1
Sequence length: 337 residues
Sequence: HLICQSGDVLSARYEIVDTLGEGAFGKVVECIDHKAGGRHVAVKIVKNVDRYCEAARSEIQVLEHLNTTDPNSTFRCVQMLEWFEHHGHICIVFELLGLSTYDFIKENGFLPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQSDYTEAYNPKIKRDERTLINPDIKVVDFGSATYDDEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFPTHDSKEHLAMMERILGPLPKHMIQKTRKRKYFHHDRLDWDEHSSAGRYVSRRCKPLKEFMLSQDVEHERLFDLIQKMLEYDPAKRITLREALKHPFFDLLKKSI
Oligomeric state: Monomer
Stoichiometry: A1
Experimental method: X-RAY DIFFRACTION
Refinement resolution (Å): 2.05
R work: 0.19859
R free: 0.247
Average B factor: 47.978
Crystallization method: VAPOR DIFFUSION, SITTING DROP
Crystallization pH: 6.5
Crystallization temperature (K): 293
Crystal growth procedure: 24% PEG 3350, 200mM MgCl2, 100mM BisTris (pH 6.5)
Matthews coefficient: 2.47
Solvent content (%): 50.11
Ligand: 5-(1-methylindol-3-yl)pyrimidin-4-amine (JU8)
Ligand formula: C13 H12 N4
Ligand molecular weight: 224.261
Ligand SMILES: Cn1cc(c2c1cccc2)c3cncnc3N
Ligand InChI: InChI=1S/C13H12N4/c1-17-7-11(9-4-2-3-5-12(9)17)10-6-15-8-16-13(10)14/h2-8H,1H3,(H2,14,15,16)
Release date: 2020-05-06
Bruton's tyrosine kinase in complex with compound 51 (PDB entry 7LTZ)
Macromolecule: Isoform BTK-C of Tyrosine-protein kinase BTK
Type: Protein, polypeptide(L)
Source organism: Homo sapiens
EC number: 2.7.10.2
Sequence length: 267 residues
Sequence: GSWEIDPKDLTFLKELGTGQFGVVKYGKWRGQYDVAIKMIKEGSMSEDEFIEEAKVMMNLSHEKLVQLYGVCTKQRPIFIITEYMANGCLLNYLREMRHRFQTQQLLEMCKDVCEAMEYLESKQFLHRDLAARNCLVNDQGVVKVSDFGLSRYVLDDEYTSSVGSKFPVRWSPPEVLMYSKFSSKSDIWAFGVLMWEIYSLGKMPYERFTNSETAEHIAQGLRLYRPHLASEKVYTIMYSCWHEKADERPTFKILLSNILDVMDEES
Oligomeric state: Monomer
Stoichiometry: A1
Experimental method: X-RAY DIFFRACTION
Refinement resolution (Å): 1.53
R work: 0.179
R free: 0.2129
Average B factor: 20.16
Crystallization method: VAPOR DIFFUSION, SITTING DROP
Crystallization temperature (K): 277
Crystal growth procedure: 0.1M BisTRIS pH 6.5, 0.2M Ammonium Acetate, 0.1M Guanidine HCl, 20% PEG2200 MME
Matthews coefficient: 2.34
Solvent content (%): 47.45
Ligand: 1-~{tert}-butyl-~{N}-[(5~{R})-8-[2-[(1-methylpyrazol-4-yl)amino]pyrimidin-4-yl]-2-(oxetan-3-yl)-1,3,4,5-tetrahydro-2-benzazepin-5-yl]-1,2,3-triazole-4-carboxamide (YDA)
Ligand formula: C28 H34 N10 O2
Ligand molecular weight: 542.635
Ligand SMILES: CC(C)(C)n1cc(nn1)C(=O)NC2CCN(Cc3c2ccc(c3)c4ccnc(n4)Nc5cnn(c5)C)C6COC6
Ligand InChI: InChI=1S/C28H34N10O2/c1-28(2,3)38-15-25(34-35-38)26(39)32-24-8-10-37(21-16-40-17-21)13-19-11-18(5-6-22(19)24)23-7-9-29-27(33-23)31-20-12-30-36(4)14-20/h5-7,9,11-12,14-15,21,24H,8,10,13,16-17H2,1-4H3,(H,32,39)(H,29,31,33)/t24-/m1/s1
Release date: 2022-01-12
Crystal Structure of BACE1 in complex with N-(3-((4S,5S)-2-amino-4-methyl-5-phenyl-5,6-dihydro-4H-1,3-thiazin-4-yl)-4-fluorophenyl)-5-(fluoromethoxy)pyrazine-2-carboxamide (PDB entry 6JSF)
Macromolecule: Beta-secretase 1
Type: Protein, polypeptide(L)
Source organism: Homo sapiens
EC number: 3.4.23.46
Sequence length: 416 residues
Sequence: GSHMLPRETDEEPEEPGRRGSFVEMVDNLRGKSGQGYYVEMTVGSPPQTLNILVDTGSSNFAVGAAPHPFLHRYYQRQLSSTYRDLRKGVYVPYTQGKWEGELGTDLVSIPHGPNVTVRANIAAITESDKFFINGSNWEGILGLAYAEIARPDDSLEPFFDSLVKQTHVPNLFSLQLCGAGFPLNQSEVLASVGGSMIIGGIDHSLYTGSLWYTPIRREWYYEVIIVRVEINGQDLKMDCKEYNYDKSIVDSGTTNLRLPKKVFEAAVKSIKAASSTEKFPDGFWLGEQLVCWQAGTTPWNIFPVISLYLMGEVTNQSFRITILPQQYLRPVEDVATSQDDCYKFAISQSSTGTVMGAVIMEGFYVVFDRARKRIGFAVSACHVHDEFRTAAVEGPFVTLDMEDCGYNIPQTDEST
Oligomeric state: Monomer
Stoichiometry: A1
Experimental method: X-RAY DIFFRACTION
Refinement resolution (Å): 2.3
R work: 0.1831
R free: 0.2127
Average B factor: 39.439
Crystallization method: VAPOR DIFFUSION, SITTING DROP
Crystallization pH: 6.5
Crystallization temperature (K): 293.15
Crystal growth procedure: 0.2 M sodium citrate, 0.2 M ammonium iodide, 18.4%(w/v) polyethylene glycol 5000 monomethyl ether, pH 6.5
Matthews coefficient: 2.79
Solvent content (%): 60.28
Ligand: IODIDE ION (IOD)
Ligand formula: I
Ligand molecular weight: 126.904
Ligand SMILES: [I-]
Ligand InChI: InChI=1S/HI/h1H/p-1
Release date: 2019-08-28
JAK2 JH1 in complex with BL2-084 (PDB entry 6VNB)
Macromolecule: Tyrosine-protein kinase JAK2
Type: Protein, polypeptide(L)
Source organism: Homo sapiens
EC number: 2.7.10.2
Sequence length: 308 residues
Sequence: HHHHHHHHENLYFQGDPTQFEERHLKFLQQLGKGNFGSVEMCRYDPLQDNTGEVVAVKKLQHSTEEHLRDFEREIEILKSLQHDNIVKYKGVCYSAGRRNLKLIMEYLPYGSLRDYLQKHKERIDHIKLLQYTSQICKGMEYLGTKRYIHRDLATRNILVENENRVKIGDFGLTKVLPQDKEYYKVKEPGESPIFWYAPESLTESKFSVASDVWSFGVVLYELFTYIEKSKSPPAEFMRMIGNDKQGQMIVFHLIELLKNNGRLPRPDGCPDEIYMIMTECWNNNVNQRPSFRDLALRVDQIRDNMAG
Oligomeric state: Monomer
Stoichiometry: A1
Experimental method: X-RAY DIFFRACTION
Refinement resolution (Å): 2.19
R work: 0.2162
R free: 0.2612
Average B factor: 57.9509
Crystallization method: VAPOR DIFFUSION, HANGING DROP
Crystallization pH: 5.5
Crystallization temperature (K): 291
Crystal growth procedure: 0.1 M Bis-Tris pH 5.5, 0.2 M NaCl, 25% PEG 3350
Matthews coefficient: 3.1
Solvent content (%): 60.32
Ligand: (3S)-3-cyclopentyl-3-[4-(2-{[4-(piperidin-4-yl)phenyl]amino}-7H-pyrrolo[2,3-d]pyrimidin-4-yl)-1H-pyrazol-1-yl]propanenitrile (R6P)
Ligand formula: C28 H32 N8
Ligand molecular weight: 480.607
Ligand SMILES: c1cc(ccc1C2CCNCC2)Nc3nc(c4cc[nH]c4n3)c5cnn(c5)C(CC#N)C6CCCC6
Ligand InChI: InChI=1S/C28H32N8/c29-13-9-25(21-3-1-2-4-21)36-18-22(17-32-36)26-24-12-16-31-27(24)35-28(34-26)33-23-7-5-19(6-8-23)20-10-14-30-15-11-20/h5-8,12,16-18,20-21,25,30H,1-4,9-11,14-15H2,(H2,31,33,34,35)/t25-/m0/s1
Release date: 2021-02-17
PanDDA analysis group deposition -- Crystal structure of PTP1B in complex with compound_FMOPL000632a (PDB entry 5QE5)
Macromolecule: Tyrosine-protein phosphatase non-receptor type 1
Type: Protein, polypeptide(L)
Source organism: Homo sapiens
EC number: 3.1.3.48
Sequence length: 321 residues
Sequence: MEMEKEFEQIDKSGSWAAIYQDIRHEASDFPSRVAKLPKNKNRNRYRDVSPFDHSRIKLHQEDNDYINASLIKMEEAQRSYILTQGPLPNTVGHFWEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEKEMIFEDTNLKLTLISEDIKSYYTVRQLELENLTTQETREILHFHYTTWPDFGVPESPASFLNFLFKVRESGSLSPEHGPVVVHCSAGIGRSGTFCLADTCLLLMDKRKDPSSVDIKKVLLEMRKFRMGLIQTADQLRFSYLAVIEGAKFIMGDSSVQDQWKELSHEDLEPPPEHIPPPPRPPKRILEPHN
Oligomeric state: Monomer
Stoichiometry: A1
Experimental method: X-RAY DIFFRACTION
Refinement resolution (Å): 1.773
R work: 0.1828
R free: 0.2119
Average B factor: 39.9734
Crystallization method: VAPOR DIFFUSION
Crystallization pH: 7.5
Crystallization temperature (K): 277
Crystal growth procedure: well solution: 0.3 M magnesium acetate, 0.1 M HEPES pH 7.5, 0.1% beta-mercaptoethanol, 13-14% PEG 8000, 2% ethanol
Matthews coefficient: 3.33
Solvent content (%): 63.08
Ligand: 1-methyl-5-(phenylamino)-1,2-dihydro-3H-pyrazol-3-one (JH7)
Ligand formula: C10 H11 N3 O
Ligand molecular weight: 189.214
Ligand SMILES: CN1C(=CC(=O)N1)Nc2ccccc2
Ligand InChI: InChI=1S/C10H11N3O/c1-13-9(7-10(14)12-13)11-8-5-3-2-4-6-8/h2-7,11H,1H3,(H,12,14)
Release date: 2018-10-10
Crystal structure of mouse autotaxin in complex with a DNA aptamer (PDB entry 5HRT)
Macromolecule: Ectonucleotide pyrophosphatase/phosphodiesterase family member 2
Type: Protein, polypeptide(L)
Source organism: Mus musculus
EC number: 3.1.4.39
Sequence length: 831 residues
Sequence: AEWDEGPPTVLSDSPWTNTSGSCKGRCFELQEVGPPDCRCDNLCKSYSSCCHDFDELCLKTARGWECTKDRCGEVRNEENACHCSEDCLSRGDCCTNYQVVCKGESHWVDDDCEEIRVPECPAGFVRPPLIIFSVDGFRASYMKKGSKVMPNIEKLRSCGTHAPYMRPVYPTKTFPNLYTLATGLYPESHGIVGNSMYDPVFDATFHLRGREKFNHRWWGGQPLWITATKQGVRAGTFFWSVSIPHERRILTILQWLSLPDNERPSVYAFYSEQPDFSGHKYGPFGPEMTNPLREIDKTVGQLMDGLKQLKLHRCVNVIFVGDHGMEDVTCDRTEFLSNYLTNVDDITLVPGTLGRIRPKIPNNLKYDPKAIIANLTCKKPDQHFKPYMKQHLPKRLHYANNRRIEDLHLLVERRWHVARKPLDVYKKPSGKCFFQGDHGFDNKVNSMQTVFVGYGPTFKYRTKVPPFENIELYNVMCDLLGLKPAPNNGTHGSLNHLLRTNTFRPTLPEEVSRPNYPGIMYLQSDFDLGCTCDDKNKLEELNKRLHTKGSTEERHLLYGRPAVLYRTSYDILYHTDFESGYSEIFLMPLWTSYTISKQAEVSSIPEHLTNCVRPDVRVSPGFSQNCLAYKNDKQMSYGFLFPPYLSSSPEAKYDAFLVTNMVPMYPAFKRVWTYFQRVLVKKYASERNGVNVISGPIFDYNYNGLRDIEDEIKQYVEGSSIPVPTHYYSIITSCLDFTQPADKCDGPLSVSSFILPHRPDNDESCNSSEDESKWVEELMKMHTARVRDIEHLTGLDFYRKTSRSYSEILTLKTYLHTYESEISRENLYFQ
Oligomeric state: Monomer
Stoichiometry: A1
Experimental method: X-RAY DIFFRACTION
Refinement resolution (Å): 1.997
R work: 0.1637
R free: 0.2018
Crystallization method: VAPOR DIFFUSION, HANGING DROP
Crystallization pH: 7.5
Crystallization temperature (K): 293
Crystal growth procedure: PEG3350, calcium chloride, tris
Matthews coefficient: 2.65
Solvent content (%): 53.56
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: 2016-04-06
Crystal structure of the KH2 domain of human RNA-binding E3 ubiquitin-protein ligase MEX-3C (PDB entry 5WWZ)
Macromolecule: RNA-binding E3 ubiquitin-protein ligase MEX3C
Type: Protein, polypeptide(L)
Source organism: Homo sapiens
EC number: 2.3.2.27
Sequence length: 86 residues
Sequence: MGHHHHHHMSPNLPGQTTVQVRVPYRVVGLVVGPKGATIKRIQQQTHTYIVTPSRDKEPVFEVTGMPENVDRAREEIEMHIAMRTG
Oligomeric state: Monomer
Stoichiometry: A1
Experimental method: X-RAY DIFFRACTION
Refinement resolution (Å): 2.5
R work: 0.2263
R free: 0.2698
Average B factor: 56.6324
Crystallization method: VAPOR DIFFUSION, SITTING DROP
Crystallization temperature (K): 277
Crystal growth procedure: 1.6M Ammonium sulfate
Matthews coefficient: 2.5
Solvent content (%): 50.83
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: 2017-08-23
Human Fatty Acid Synthase Psi/KR Tri-Domain with NADPH and Compound 22 (PDB entry 6NNA)
Macromolecule: Fatty acid synthase,Fatty acid synthase
Type: Protein, polypeptide(L)
Source organism: Homo sapiens
EC number: 2.3.1.85
Sequence length: 660 residues
Sequence: QQVPILEKFCFTPHTEEGCLSERAALQEELQLCKGLVQALQTKVTQQGLKMVVPGLDGAQIPRDPSQQELPRLLSAACRLQLNGNLQLELAQVLAQERPKLPEDPLLSGLLDSPALKACLDTAVENMPSLKMKVVEVLAGHGHLYSRIPGLLSPHPLLQLSYTATDRHPQALEAAQAELQQHDVAQGQWDPADPAPSALGSADLLVCNCAVAALGDPASALSNMVAALREGGFLLLHTLLRGHPLGDIVAFLTSTEPQYGQGILSQDAWESLFSRVSLRLVGLKKSFYGSTLFLCRRPTPQDSPIFLPVDDTSFRWVESLKGILADEDSARPVWLKAINCATSGVVGLVNCLRREPGGNRLRCVLLSNLSSTSHVPEVDPGSAELQKVLQGDLVMNVYRDGAWGAFRHFLLEEDKGSKTFCPAHKSYIIAGGLGGFGLELAQWLIQRGVQKLVLTSRSGIRTGYQAKQVRRWRRQGVQVQVSTSNISSLEGARGLIAEAAQLGPVGGVFNLAVVLRDGLLENQTPEFFQDVCKPKYSGTLNLDRVTREACPELDYFVVFSSVSCGRGNAGQSNYGFANSAMERICEKRRHEGLPGLAVQWGAIGDVGILVETMSTNDTIVSGTLPQRMASCLEVLDLFLNQPHMVLSSFVLAEKHHHHHH
Oligomeric state: Monomer
Stoichiometry: A1
Experimental method: X-RAY DIFFRACTION
Refinement resolution (Å): 2.26
R work: 0.2008
R free: 0.2508
Average B factor: 34.873
Crystallization method: VAPOR DIFFUSION, HANGING DROP
Crystallization pH: 7.6
Crystallization temperature (K): 291
Crystal growth procedure: 0.19 M ammonium sulfate, 5 mM sodium cacodylate,pH7.6 and 27 % w/v PEG 3350
Matthews coefficient: 2.26
Solvent content (%): 45.48
Ligand: NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE (NDP)
Ligand formula: C21 H30 N7 O17 P3
Ligand molecular weight: 745.421
Ligand SMILES: c1nc(c2c(n1)n(cn2)C3C(C(C(O3)COP(=O)(O)OP(=O)(O)OCC4C(C(C(O4)N5C=CCC(=C5)C(=O)N)O)O)O)OP(=O)(O)O)N
Ligand InChI: InChI=1S/C21H30N7O17P3/c22-17-12-19(25-7-24-17)28(8-26-12)21-16(44-46(33,34)35)14(30)11(43-21)6-41-48(38,39)45-47(36,37)40-5-10-13(29)15(31)20(42-10)27-3-1-2-9(4-27)18(23)32/h1,3-4,7-8,10-11,13-16,20-21,29-31H,2,5-6H2,(H2,23,32)(H,36,37)(H,38,39)(H2,22,24,25)(H2,33,34,35)/t10-,11-,13-,14-,15-,16-,20-,21-/m1/s1
Release date: 2019-02-20
Human LMPTP in complex with inhibitor (PDB entry 7KH8)
Macromolecule: Low molecular weight phosphotyrosine protein phosphatase
Type: Protein, polypeptide(L)
Source organism: Homo sapiens
EC number: 3.1.3.48
Sequence length: 157 residues
Sequence: GHGATKSVLFVCLGNICRSPIAEAVFRKLVTDQNISENWRVDSAATSGYEIGNPPDYRGQSCMKRHGIPMSHVARQITKEDFATFDYILCMDESNLRDLNRKSNQVKTCKAKIELLGSYDPQKQLIIEDPYYGNDSDFETVYQQCVRCCRAFLEKAH
Oligomeric state: Monomer
Stoichiometry: A1
Experimental method: X-RAY DIFFRACTION
Refinement resolution (Å): 1.3
R work: 0.1254
R free: 0.1608
Average B factor: 18.557
Crystallization method: VAPOR DIFFUSION, SITTING DROP
Crystallization pH: 5
Crystallization temperature (K): 293
Crystal growth procedure: PEG 3350, Potassium Nitrate, Bis-Tris
Matthews coefficient: 2.16
Solvent content (%): 42.98
Ligand: 3-[(2,6-dichlorophenyl)methyl]-8-(2-methylphenyl)-3H-purin-6-amine (WE7)
Ligand formula: C19 H15 Cl2 N5
Ligand molecular weight: 384.262
Ligand SMILES: Cc1ccccc1c2nc-3c(ncn(c3n2)Cc4c(cccc4Cl)Cl)N
Ligand InChI: InChI=1S/C19H15Cl2N5/c1-11-5-2-3-6-12(11)18-24-16-17(22)23-10-26(19(16)25-18)9-13-14(20)7-4-8-15(13)21/h2-8,10H,9,22H2,1H3
Release date: 2021-05-19
Crystal Structure of FHA domain of human APLF in complex with XRCC1 bisphospho peptide (PDB entry 5W7X)
Macromolecule: Aprataxin and PNK-like factor
Type: Protein, polypeptide(L)
Source organism: Homo sapiens
EC number: 4.2.99.18
Sequence length: 108 residues
Sequence: SFTMSGGFELQPRDGGPRVALAPGETVIGRGPLLGITDKRVSRRHAILEVAGGQLRIKPIHTNPCFYQSSEKSQLLPLKPNLWCYLNPGDSFSLLVDKYIFRILSIPS
Oligomeric state: Hetero 2-mer
Stoichiometry: A1, B1
Experimental method: X-RAY DIFFRACTION
Refinement resolution (Å): 2.005
R work: 0.1922
R free: 0.2291
Crystallization method: VAPOR DIFFUSION, SITTING DROP
Crystallization pH: 8.5
Crystallization temperature (K): 293
Crystal growth procedure: 0.6mM XRCC1 bisphosphopeptide
0.6mM APLF
0.5M lithium chloride
0.1M Tris 
28% PEG 6000
Matthews coefficient: 2.05
Solvent content (%): 40.01
Release date: 2018-05-02
Anti-FIXa Fab in complex with human des-(Gla-EGF1) FIXa (PDB entry 8OL9)
Macromolecule: Light chain of FIXa binding Fab
Type: Protein, polypeptide(L)
Source organism: Homo sapiens
Sequence length: 214 residues
Sequence: DIQMTQSPSTLSASAGDRVTISCRASQSISSWLAWYQQKPGKAPKLLIYKASSLESGVPSRFSGSGSGTEFTLTISSLQPDDFATYYCQEYNSYIRTFGQGTKVEIKRTVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDSKDSTYSLSSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC
Oligomeric state: Hetero 4-mer
Stoichiometry: A1, B1, C1, D1
Experimental method: X-RAY DIFFRACTION
Refinement resolution (Å): 2.6
R work: 0.2666
R free: 0.3233
Average B factor: 61.15
Crystallization method: VAPOR DIFFUSION, SITTING DROP
Crystallization pH: 5.6
Crystallization temperature (K): 291
Crystal growth procedure: 0.5 M ammonium sulphate, 0.1 M sodium citrate, pH 5.6, !.0 M lithium sulphate
Matthews coefficient: 3.42
Solvent content (%): 63.99
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: 2023-07-19
Human Carbonic Anhydrase II native 13 atm CO2 (PDB entry 6KM5)
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): 1.151
R work: 0.1028
R free: 0.1288
Average B factor: 16.179
Crystallization method: VAPOR DIFFUSION, HANGING DROP
Crystallization pH: 7.8
Crystallization temperature (K): 293
Crystal growth procedure: 1.3 M sodium citrate, 100 mM Tris-HCl
Matthews coefficient: 2.08
Solvent content (%): 40.79
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: 2020-08-05
Selective pharmacological inhibition of the CREB binding protein bromodomain regulates inflammatory cytokines in macrophages and RGS4 in neurons (PDB entry 5CGP)
Macromolecule: CREB-binding protein
Type: Protein, polypeptide(L)
Source organism: Homo sapiens
EC number: 2.3.1.48
Sequence length: 119 residues
Sequence: SMRKKIFKPEELRQALMPTLEALYRQDPESLPFRQPVDPQLLGIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRKTSRVYKFCSKLAEVFEQEIDPVMQSLG
Oligomeric state: Monomer
Stoichiometry: A1
Experimental method: X-RAY DIFFRACTION
Refinement resolution (Å): 1.96
R work: 0.2092
R free: 0.2493
Average B factor: 17.15
Crystallization method: VAPOR DIFFUSION, HANGING DROP
Crystallization temperature (K): 293
Crystal growth procedure: 15-20% PEG 8000, 0.2M CaAcetate, 0.1 M cacodylate ph 6-7
Matthews coefficient: 2.14
Solvent content (%): 42.4
Ligand: 5-(3,5-dimethyl-1,2-oxazol-4-yl)-2-[2-(4-methoxyphenyl)ethyl]-1-[2-(morpholin-4-yl)ethyl]-1H-benzimidazole (53W)
Ligand formula: C27 H32 N4 O3
Ligand molecular weight: 460.568
Ligand SMILES: Cc1c(c(on1)C)c2ccc3c(c2)nc(n3CCN4CCOCC4)CCc5ccc(cc5)OC
Ligand InChI: InChI=1S/C27H32N4O3/c1-19-27(20(2)34-29-19)22-7-10-25-24(18-22)28-26(11-6-21-4-8-23(32-3)9-5-21)31(25)13-12-30-14-16-33-17-15-30/h4-5,7-10,18H,6,11-17H2,1-3H3
Release date: 2016-04-20
Crystal structure of TOPBP1 BRCT0,1,2 in complex with a RAD9 phosphopeptide (PDB entry 6HM5)
Macromolecule: DNA topoisomerase II binding protein 1
Type: Protein, polypeptide(L)
Source organism: Gallus gallus
Sequence length: 290 residues
Sequence: RMKGSKEVFLVKFVKSSGSSEYFLKALESIKEFQSEEHLQILEEEAALNIKENDKSLYICDPFTGVVFNHLKKLGCRIVGPQVVLYCMQSQRCVPRAEYPVYNMTMADVTISCTTLDKDVREEVHKYVQMMGGRVYRDLNMSVTHLIAGEVGSKKYLVAASLKKPVLLPSWVKTLWDKSQQRMMRYTDVNMEDYACPVFLGCTICVTGLSSSDRKEVQRLTAEHGGQYSGQLKMNECTHLIVQEPKGQKYECAKKWNVHCVPVQWFSDSIEKGFCQDETMYKIESGSKLS
Oligomeric state: Hetero 2-mer
Stoichiometry: A1, B1
Experimental method: X-RAY DIFFRACTION
Refinement resolution (Å): 2.33003812226
R work: 0.201270613267
R free: 0.241491216096
Average B factor: 51.5979895974
Crystallization method: VAPOR DIFFUSION, SITTING DROP
Crystallization temperature (K): 287.15
Crystal growth procedure: 100 mM bicine/Trizma base pH 8.5, 300 mM diethyleneglycol, 300 mM triethyleneglycol, 300 mM tetraethyleneglycol, 300 mM pentaethyleneglycol, 10% w/v PEG 20000 and 20% v/v PEG MME 550
Matthews coefficient: 2.21
Solvent content (%): 44.31
Release date: 2018-10-17