Structure of PDB 4b2q Chain B Binding Site BS01

Receptor Information
>4b2q Chain B (length=485) 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
RVGSAAQVKALKQVAGSLKLFLAQYREVAAFAQFGSDLDASTKQTLVRGE
RLTQLLKQNQYSPLATEEQVPLIYAGVNGHLDGIELSRIGEFESSFLSYL
KSNHNELLTEIREKGELSKELLASLKSATESFVAT
Ligand information
Ligand IDATP
InChIInChI=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
InChIKeyZKHQWZAMYRWXGA-KQYNXXCUSA-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)O)O)O)N
CACTVS 3.341Nc1ncnc2n(cnc12)[CH]3O[CH](CO[P](O)(=O)O[P](O)(=O)O[P](O)(O)=O)[CH](O)[CH]3O
ACDLabs 10.04O=P(O)(O)OP(=O)(O)OP(=O)(O)OCC3OC(n2cnc1c(ncnc12)N)C(O)C3O
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)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)[C@@H](O)[C@H]3O
FormulaC10 H16 N5 O13 P3
NameADENOSINE-5'-TRIPHOSPHATE
ChEMBLCHEMBL14249
DrugBankDB00171
ZINCZINC000004261765
PDB chain4b2q Chain B Residue 1510 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB4b2q Structure of the Yeast F1Fo-ATP Synthase Dimer and its Role in Shaping the Mitochondrial Cristae.
Resolution37.0 Å
Binding residue
(original residue number in PDB)		Q174 G176 K177 T178 A179 R364 Q434
Binding residue
(residue number reindexed from 1)		Q150 G152 K153 T154 A155 R340 Q410
Annotation score5
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:0032559 adenyl ribonucleotide binding
GO:0046933 proton-transporting ATP synthase activity, rotational mechanism
Biological Process
GO:0015986 proton motive force-driven ATP synthesis
GO:0046034 ATP metabolic process
GO:1902600 proton transmembrane transport
Cellular Component
GO:0045261 proton-transporting ATP synthase complex, catalytic core F(1)

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:4b2q, PDBe:4b2q, PDBj:4b2q
PDBsum4b2q
PubMed22864911
UniProtP07251|ATPA_YEAST ATP synthase subunit alpha, mitochondrial (Gene Name=ATP1)

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