Structure of PDB 5lqx Chain C

Receptor sequence
>5lqxC (length=498) Species: 870730,871575 [Search protein sequence]
SILESKIRGVSDEANLDETGRVLSVGDGIARVFGLNNCQAEELVEFASGV
KGMALNLEPGQVGIVLFGSDREVKEGEIVKRTGKIVDVPIGPGMLGRVVD
ALGNPIDGKGPIEATGYAIAQLKAPGILPRRSVFEPMQTGLKAVDALVPI
GRGQRELIIGDRQTGKTAVALDTILNQKRWNDGNDESKKLYCVYVAVGQK
RSTVAQLVQTLEQNDAMKYSIVVAATASEAAPLQYLAPFTACAIAEWFRD
NGKHALIVYDDLSKQAVAYRQLSLLLRRPPGREAYPGDVFYLHSRLLERA
AKMSDANGGGSLTALPVIETQGGDVSAYIPTNVISITDGQIFLEAELFYK
GIRPAINVGLSVSRVGSAAQVKAMKQVAGSLKLFLAQYREVAAFAQFGSD
LDASTKQTLSRGERLTQLLKQKQYSPQASEEQVPVIYAGVNGFLDNIPIE
RIPEFEEQFIAYLKANEGDILEAIRTKGELSSELLDKLKSATETFVAT
3D structure
PDB5lqx Structure of the mitochondrial ATP synthase fromPichia angustadetermined by electron cryo-microscopy.
ChainC
Resolution7.9 Å
3D
structure
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Enzymatic activity
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 ADP C R173 Q174 G176 K177 T178 A179 R364 K433 Q434 R162 Q163 G165 K166 T167 A168 R353 K422 Q423
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:5lqx, PDBe:5lqx, PDBj:5lqx
PDBsum5lqx
PubMed27791192
UniProtC0HK51|ATPA_PICAN ATP synthase subunit alpha, mitochondrial (Gene Name=ATP1);
W1Q6W1

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