Structure of PDB 2ck3 Chain C Binding Site BS03

Receptor Information
>2ck3 Chain C (length=490) Species: 9913 (Bos taurus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
TSVDLEETGRVLSIGDGIARVHGLRNVQAEEMVEFSSGLKGMSLNLEPDN
VGVVVFGNDKLIKEGDIVKRTGAIVDVPVGEELLGRVVDALGNAIDGKGP
IGSKARRRVGLKAPGIIPRISVREPMQTGIKAVDSLVPIGRGQRELIIGD
RQTGKTSIAIDTIINQKRFNDGTDEKKKLYCIYVAIGQKRSTVAQLVKRL
TDADAMKYTIVVSATASDAAPLQYLAPYSGCSMGEYFRDNGKHALIIYDD
LSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMNDAFGGGS
LTALPVIETQAGDVSAYIPTNVISITDGQIFLETELFYKGIRPAINVGLS
VSRVGSAAQTRAMKQVAGTMKLELAQYREVAAFAQFGSDLDAATQQLLSR
GVRLTELLKQGQYSPMAIEEQVAVIYAGVRGYLDKLEPSKITKFENAFLS
HVISQHQALLGKIRTDGKISEESDAKLKEIVTNFLAGFEA
Ligand information
Ligand IDAZI
InChIInChI=1S/N3/c1-3-2/q-1
InChIKeyIVRMZWNICZWHMI-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
CACTVS 3.341
OpenEye OEToolkits 1.5.0		[N-]=[N+]=[N-]
FormulaN3
NameAZIDE ION
ChEMBLCHEMBL79455
DrugBank
ZINC
PDB chain2ck3 Chain D Residue 1092 [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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PDB2ck3 How Azide Inhibits ATP Hydrolysis by the F-Atpases.
Resolution1.95 Å
Binding residue
(original residue number in PDB)		S344 R373
Binding residue
(residue number reindexed from 1)		S324 R353
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) K175 Q208 K209 R373
Catalytic site (residue number reindexed from 1) K155 Q188 K189 R353
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
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Cellular Component
External links
PDB RCSB:2ck3, PDBe:2ck3, PDBj:2ck3
PDBsum2ck3
PubMed16728506
UniProtP19483|ATPA_BOVIN ATP synthase subunit alpha, mitochondrial (Gene Name=ATP5F1A)

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