Structure of PDB 2wpd Chain A Binding Site BS01

Receptor Information
>2wpd Chain A (length=485) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
NLNETGRVLAVGDGIARVFGLNNIQAEELVEFSSGVKGMALNLEPGQVGI
VLFGSDRLVKEGELVKRTGNIVDVPVGPGLLGRVVDALGNPIDGKGPIDA
AGRSRAQVKAPGILPRRSVHEPVQTGLKAVDALVPIGRGQRELIIGDRQT
GKTAVALDTILNQKRWNNGSDESKKLYCVYVAVGQKRSTVAQLVQTLEQH
DAMKYSIIVAATASEAAPLQYLAPFTAASIGEWFRDNGKHALIVYDDLSK
QAVAYRQLSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSEKEGSGSLTA
LPVIETQGGDVSAYIPTNVISITDGQIFLEAELFYKGIRPAINVGLSVSR
VGSAAQVKALKQVAGSLKLFLAQYREVAAFAQFGSDLDASTKQTLVRGER
LTQLLKQNQYSPLATEEQVPLIYAGVNGHLDGIELSRIGEFESSFLSYLK
SNHNELLTEIREKGELSKELLASLKSATESFVATF
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 chain2wpd Chain A Residue 600 [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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PDB2wpd Crystal Structure of the Mg.Adp-Inhibited State of the Yeast F1C10-ATP Synthase.
Resolution3.432 Å
Binding residue
(original residue number in PDB)		Q174 G176 K177 T178 A179 Q434
Binding residue
(residue number reindexed from 1)		Q149 G151 K152 T153 A154 Q409
Annotation score5
Enzymatic activity
Catalytic site (original residue number in PDB) K177 Q210 K211 R375
Catalytic site (residue number reindexed from 1) K152 Q185 K186 R350
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:2wpd, PDBe:2wpd, PDBj:2wpd
PDBsum2wpd
PubMed20610387
UniProtP07251|ATPA_YEAST ATP synthase subunit alpha, mitochondrial (Gene Name=ATP1)

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