Structure of PDB 5xz2 Chain B Binding Site BS01

Receptor Information
>5xz2 Chain B (length=192) Species: 7955 (Danio rerio) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
ADKIKNAKIVFVVGGPGSGKGTQCEKIVAKYGYTHLSSGDLLRAEVASGS
ERGKQLQAIMQKGELVPLDTVLDMIKDAMIAKADVSKGYLIDGYPREVKQ
GEEFEKKIGAPALLLYIDAKGETMVKRLMKRGETSGRADDNEETIKKRLD
LYYKATEPVIAFYEQRGIVRKINSELPVDEVFAIVEKAIDEL
Ligand information
Ligand IDAP5
InChIInChI=1S/C20H29N10O22P5/c21-15-9-17(25-3-23-15)29(5-27-9)19-13(33)11(31)7(47-19)1-45-53(35,36)49-55(39,40)51-57(43,44)52-56(41,42)50-54(37,38)46-2-8-12(32)14(34)20(48-8)30-6-28-10-16(22)24-4-26-18(10)30/h3-8,11-14,19-20,31-34H,1-2H2,(H,35,36)(H,37,38)(H,39,40)(H,41,42)(H,43,44)(H2,21,23,25)(H2,22,24,26)/t7-,8-,11-,12-,13-,14-,19-,20-/m1/s1
InChIKeyOIMACDRJUANHTJ-XPWFQUROSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0c1nc(c2c(n1)n(cn2)C3C(C(C(O3)COP(=O)(O)OP(=O)(O)OP(=O)(O)OP(=O)(O)OP(=O)(O)OCC4C(C(C(O4)n5cnc6c5ncnc6N)O)O)O)O)N
CACTVS 3.341Nc1ncnc2n(cnc12)[C@@H]3O[C@H](CO[P@@](O)(=O)O[P@@](O)(=O)O[P@](O)(=O)O[P@](O)(=O)O[P@](O)(=O)OC[C@H]4O[C@H]([C@H](O)[C@@H]4O)n5cnc6c(N)ncnc56)[C@@H](O)[C@H]3O
OpenEye OEToolkits 1.5.0c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)CO[P@](=O)(O)O[P@](=O)(O)OP(=O)(O)O[P@@](=O)(O)O[P@@](=O)(O)OC[C@@H]4[C@H]([C@H]([C@@H](O4)n5cnc6c5ncnc6N)O)O)O)O)N
CACTVS 3.341Nc1ncnc2n(cnc12)[CH]3O[CH](CO[P](O)(=O)O[P](O)(=O)O[P](O)(=O)O[P](O)(=O)O[P](O)(=O)OC[CH]4O[CH]([CH](O)[CH]4O)n5cnc6c(N)ncnc56)[CH](O)[CH]3O
FormulaC20 H29 N10 O22 P5
NameBIS(ADENOSINE)-5'-PENTAPHOSPHATE
ChEMBLCHEMBL437508
DrugBankDB01717
ZINCZINC000096085195
PDB chain5xz2 Chain B Residue 201 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB5xz2 Structural analyses of adenylate kinases from Antarctic and tropical fishes for understanding cold adaptation of enzymes
Resolution1.75 Å
Binding residue
(original residue number in PDB)		G18 S19 G20 K21 G22 T23 S39 G40 L43 R44 M61 E65 L66 V67 G94 Y95 R97 Q101 R128 R132 R138 R149 L177 V179
Binding residue
(residue number reindexed from 1)		G17 S18 G19 K20 G21 T22 S38 G39 L42 R43 M60 E64 L65 V66 G93 Y94 R96 Q100 R127 R131 R137 R148 L176 V178
Annotation score4
Enzymatic activity
Catalytic site (original residue number in PDB) K21 R97 R132 R138 R149
Catalytic site (residue number reindexed from 1) K20 R96 R131 R137 R148
Enzyme Commision number 2.7.4.10: nucleoside-triphosphate--adenylate kinase.
2.7.4.3: adenylate kinase.
2.7.4.6: nucleoside-diphosphate kinase.
Gene Ontology
Molecular Function
GO:0004017 adenylate kinase activity
GO:0004550 nucleoside diphosphate kinase activity
GO:0005524 ATP binding
GO:0016301 kinase activity
GO:0019205 nucleobase-containing compound kinase activity
Biological Process
GO:0006139 nucleobase-containing compound metabolic process
GO:0006172 ADP biosynthetic process
GO:0009142 nucleoside triphosphate biosynthetic process
GO:0016310 phosphorylation
GO:0046033 AMP metabolic process
GO:0046034 ATP metabolic process
GO:0046940 nucleoside monophosphate phosphorylation
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:5xz2, PDBe:5xz2, PDBj:5xz2
PDBsum5xz2
PubMed29167503
UniProtQ68EH2

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