Structure of PDB 1w0j Chain C Binding Site BS01

Receptor Information
>1w0j Chain C (length=498) Species: 9913 (Bos taurus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
EERILGADTSVDLEETGRVLSIGDGIARVHGLRNVQAEEMVEFSSGLKGM
SLNLEPDNVGVVVFGNDKLIKEGDIVKRTGAIVDVPVGEELLGRVVDALG
NAIDGKGPIGSKARRRVGLKAPGIIPRISVREPMQTGIKAVDSLVPIGRG
QRELIIGDRQTGKTSIAIDTIINQKRFNDGTDEKKKLYCIYVAIGQKRST
VAQLVKRLTDADAMKYTIVVSATASDAAPLQYLAPYSGCSMGEYFRDNGK
HALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKM
NDAFGGGSLTALPVIETQAGDVSAYIPTNVISITDGQIFLETELFYKGIR
PAINVGLSVSRVGSAAQTRAMKQVAGTMKLELAQYREVAAFAQFGSDLDA
ATQQLLSRGVRLTELLKQGQYSPMAIEEQVAVIYAGVRGYLDKLEPSKIT
KFENAFLSHVISQHQALLGKIRTDGKISEESDAKLKEIVTNFLAGFEA
Ligand information
Ligand IDADP
InChIInChI=1S/C10H15N5O10P2/c11-8-5-9(13-2-12-8)15(3-14-5)10-7(17)6(16)4(24-10)1-23-27(21,22)25-26(18,19)20/h2-4,6-7,10,16-17H,1H2,(H,21,22)(H2,11,12,13)(H2,18,19,20)/t4-,6-,7-,10-/m1/s1
InChIKeyXTWYTFMLZFPYCI-KQYNXXCUSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)CO[P@](=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)[CH](O)[CH]3O
ACDLabs 10.04O=P(O)(O)OP(=O)(O)OCC3OC(n2cnc1c(ncnc12)N)C(O)C3O
CACTVS 3.341Nc1ncnc2n(cnc12)[C@@H]3O[C@H](CO[P@@](O)(=O)O[P](O)(O)=O)[C@@H](O)[C@H]3O
OpenEye OEToolkits 1.5.0c1nc(c2c(n1)n(cn2)C3C(C(C(O3)COP(=O)(O)OP(=O)(O)O)O)O)N
FormulaC10 H15 N5 O10 P2
NameADENOSINE-5'-DIPHOSPHATE
ChEMBLCHEMBL14830
DrugBankDB16833
ZINCZINC000012360703
PDB chain1w0j Chain C Residue 1511 [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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PDB1w0j The Structure of Bovine F1-ATPase Inhibited by Adp and Beryllium Fluoride
Resolution2.2 Å
Binding residue
(original residue number in PDB)		Q172 G174 K175 T176 S177 F357 R362 Q432
Binding residue
(residue number reindexed from 1)		Q160 G162 K163 T164 S165 F345 R350 Q420
Annotation score5
Enzymatic activity
Catalytic site (original residue number in PDB) K175 Q208 K209 R373
Catalytic site (residue number reindexed from 1) K163 Q196 K197 R361
Enzyme Commision number 3.6.3.14: Transferred entry: 7.1.2.2.
Gene Ontology
Molecular Function
GO:0005515 protein binding
GO:0005524 ATP binding
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:0005737 cytoplasm
GO:0005739 mitochondrion
GO:0005743 mitochondrial inner membrane
GO:0005886 plasma membrane
GO:0045259 proton-transporting ATP synthase complex
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
View graph for
Cellular Component
External links
PDB RCSB:1w0j, PDBe:1w0j, PDBj:1w0j
PDBsum1w0j
PubMed15229653
UniProtP19483|ATPA_BOVIN ATP synthase subunit alpha, mitochondrial (Gene Name=ATP5F1A)

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