Structure of PDB 2xok Chain B Binding Site BS01

Receptor Information
>2xok Chain B (length=483) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
ANLNETGRVLAVGDGIARVFGLNNIQAEELVEFSSGVKGMALNLEPGQVG
IVLFGSDRLVKEGELVKRTGNIVDVPVGPGLLGRVVDALGNPIDGKGPID
AAGRSRAQVKAPGILPRRSVHEPVQTGLKAVDALVPIGRGQRELIIGDRQ
TGKTAVALDTILNQKRWNNGSDESKKLYCVYVAVGQKRSTVAQLVQTLEQ
HDAMKYSIIVAATASEAAPLQYLAPFTAASIGEWFRDNGKHALIVYDDLS
KQAVAYRQLSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSEKEGSGSLT
ALPVIETQGGDVSAYIPTNVISITDGQIFLEAELFYKGIRPAINVGLSVS
RVGSAAQVKALKQVAGSLKLFLAQYREVAAFAQSDLDASTKQTLVRGERL
TQLLKQNQYSPLATEEQVPLIYAGVNGHLDGIELSRIGEFESSFLSYLKS
NHNELLTEIREKGELSKELLASLKSATESFVAT
Ligand information
Ligand IDANP
InChIInChI=1S/C10H17N6O12P3/c11-8-5-9(13-2-12-8)16(3-14-5)10-7(18)6(17)4(27-10)1-26-31(24,25)28-30(22,23)15-29(19,20)21/h2-4,6-7,10,17-18H,1H2,(H,24,25)(H2,11,12,13)(H4,15,19,20,21,22,23)/t4-,6-,7-,10-/m1/s1
InChIKeyPVKSNHVPLWYQGJ-KQYNXXCUSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.7.0c1nc(c2c(n1)n(cn2)C3C(C(C(O3)COP(=O)(O)OP(=O)(NP(=O)(O)O)O)O)O)N
CACTVS 3.370Nc1ncnc2n(cnc12)[CH]3O[CH](CO[P](O)(=O)O[P](O)(=O)N[P](O)(O)=O)[CH](O)[CH]3O
CACTVS 3.370Nc1ncnc2n(cnc12)[C@@H]3O[C@H](CO[P](O)(=O)O[P](O)(=O)N[P](O)(O)=O)[C@@H](O)[C@H]3O
ACDLabs 12.01O=P(O)(O)NP(=O)(O)OP(=O)(O)OCC3OC(n2cnc1c(ncnc12)N)C(O)C3O
OpenEye OEToolkits 1.7.0c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)CO[P@](=O)(O)O[P@@](=O)(NP(=O)(O)O)O)O)O)N
FormulaC10 H17 N6 O12 P3
NamePHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER
ChEMBLCHEMBL1230989
DrugBank
ZINCZINC000008660410
PDB chain2xok Chain B Residue 600 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB2xok Molecular architecture of the rotary motor in ATP synthase.
Resolution3.01 Å
Binding residue
(original residue number in PDB)		R173 Q174 T175 G176 K177 T178 A179 R364 Q434
Binding residue
(residue number reindexed from 1)		R149 Q150 T151 G152 K153 T154 A155 R340 Q408
Annotation score3
Enzymatic activity
Catalytic site (original residue number in PDB) K177 Q210 K211 R375
Catalytic site (residue number reindexed from 1) K153 Q186 K187 R351
Enzyme Commision number ?
Gene Ontology
Molecular Function
GO:0005524 ATP binding
GO:0016887 ATP hydrolysis activity
GO:0032559 adenyl ribonucleotide binding
GO:0043531 ADP binding
GO:0046933 proton-transporting ATP synthase activity, rotational mechanism
Biological Process
GO:0006754 ATP biosynthetic process
GO:0015986 proton motive force-driven ATP synthesis
GO:0046034 ATP metabolic process
GO:1902600 proton transmembrane transport
Cellular Component
GO:0005739 mitochondrion
GO:0005743 mitochondrial inner membrane
GO:0005758 mitochondrial intermembrane space
GO:0005829 cytosol
GO:0016020 membrane
GO:0042645 mitochondrial nucleoid
GO:0045261 proton-transporting ATP synthase complex, catalytic core F(1)
GO:0045267 proton-transporting ATP synthase, catalytic core

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:2xok, PDBe:2xok, PDBj:2xok
PDBsum2xok
PubMed10576729
UniProtP07251|ATPA_YEAST ATP synthase subunit alpha, mitochondrial (Gene Name=ATP1)

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