Structure of PDB 4b2q Chain B

Receptor sequence
>4b2qB (length=485) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence]
ANLNETGRVLAVGDGIARVFGLNNIQAEELVEFSSGVKGMALNLEPGQVG
IVLFGSDRLVKEGELVKRTGNIVDVPVGPGLLGRVVDALGNPIDGKGPID
AAGRSRAQVKAPGILPRRSVHEPVQTGLKAVDALVPIGRGQRELIIGDRQ
TGKTAVALDTILNQKRWNNGSDESKKLYCVYVAVGQKRSTVAQLVQTLEQ
HDAMKYSIIVAATASEAAPLQYLAPFTAASIGEWFRDNGKHALIVYDDLS
KQAVAYRQLSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSEKEGSGSLT
ALPVIETQGGDVSAYIPTNVISITDGQIFLEAELFYKGIRPAINVGLSVS
RVGSAAQVKALKQVAGSLKLFLAQYREVAAFAQFGSDLDASTKQTLVRGE
RLTQLLKQNQYSPLATEEQVPLIYAGVNGHLDGIELSRIGEFESSFLSYL
KSNHNELLTEIREKGELSKELLASLKSATESFVAT
3D structure
PDB4b2q Structure of the Yeast F1Fo-ATP Synthase Dimer and its Role in Shaping the Mitochondrial Cristae.
ChainB
Resolution37.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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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 ?
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 ATP B Q174 G176 K177 T178 A179 R364 Q434 Q150 G152 K153 T154 A155 R340 Q410
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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