Structure of PDB 1aky Chain A Binding Site BS01

Receptor Information
>1aky Chain A (length=218) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
ESIRMVLIGPPGAGKGTQAPNLQERFHAAHLATGDMLRSQIAKGTQLGLE
AKKIMDQGGLVSDDIMVNMIKDELTNNPACKNGFILDGFPRTIPQAEKLD
QMLKEQGTPLEKAIELKVDDELLVARITGRLIHPASGRSYHKIFNPPKED
MKDDVTGEALVQRSDDNADALKKRLAAYHAQTEPIVDFYKKTGIWAGVDA
SQPPATVWADILNKLGKN
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 chain1aky Chain A Residue 301 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB1aky High-resolution structures of adenylate kinase from yeast ligated with inhibitor Ap5A, showing the pathway of phosphoryl transfer.
Resolution1.63 Å
Binding residue
(original residue number in PDB)		G14 G16 K17 G18 T19 T35 R40 M57 G61 V63 M68 G90 R93 Q97 R128 R132 S141 Y142 H143 R165 R176 P206
Binding residue
(residue number reindexed from 1)		G12 G14 K15 G16 T17 T33 R38 M55 G59 V61 M66 G88 R91 Q95 R126 R130 S139 Y140 H141 R163 R174 P204
Annotation score4
Enzymatic activity
Catalytic site (original residue number in PDB) K17 R93 R132 R165 R176
Catalytic site (residue number reindexed from 1) K15 R91 R130 R163 R174
Enzyme Commision number 2.7.4.3: adenylate kinase.
Gene Ontology
Molecular Function
GO:0003688 DNA replication origin binding
GO:0004017 adenylate kinase activity
GO:0005524 ATP binding
GO:0016301 kinase activity
GO:0016776 phosphotransferase activity, phosphate group as acceptor
GO:0019205 nucleobase-containing compound kinase activity
Biological Process
GO:0006139 nucleobase-containing compound metabolic process
GO:0006172 ADP biosynthetic process
GO:0006270 DNA replication initiation
GO:0009117 nucleotide metabolic process
GO:0016310 phosphorylation
GO:0036388 pre-replicative complex assembly
GO:0046033 AMP metabolic process
GO:0046034 ATP metabolic process
GO:0046940 nucleoside monophosphate phosphorylation
Cellular Component
GO:0005737 cytoplasm
GO:0005739 mitochondrion
GO:0005758 mitochondrial intermembrane space
GO:0005829 cytosol

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:1aky, PDBe:1aky, PDBj:1aky
PDBsum1aky
PubMed7670369
UniProtP07170|KAD2_YEAST Adenylate kinase (Gene Name=ADK1)

[Back to BioLiP]