Structure of PDB 5lqz Chain C

Receptor sequence
>5lqzC (length=503) Species: 870730 (Ogataea angusta) [Search protein sequence]
PTEVSSILESKIRGVSDEANLDETGRVLSVGDGIARVFGLNNCQAEELVE
FASGVKGMALNLEPGQVGIVLFGSDREVKEGEIVKRTGKIVDVPIGPGML
GRVVDALGNPIDGKGPIEATGYAIAQLKAPGILPRRSVFEPMQTGLKAVD
ALVPIGRGQRELIIGDRQTGKTAVALDTILNQKRWNDGNDESKKLYCVYV
AVGQKRSTVAQLVQTLEQNDAMKYSIVVAATASEAAPLQYLAPFTACAIA
EWFRDNGKHALIVYDDLSKQAVAYRQLSLLLRRPPGREAYPGDVFYLHSR
LLERAAKMSDANGGGSLTALPVIETQGGDVSAYIPTNVISITDGQIFLEA
ELFYKGIRPAINVGLSVSRVGSAAQVKAMKQVAGSLKLFLAQYREVAAFA
QFGSDLDASTKQTLSRGERLTQLLKQKQYSPQASEEQVPVIYAGVNGFLD
NIPIERIPEFEEQFIAYLKANEGDILEAIRTKGELSSELLDKLKSATETF
VAT
3D structure
PDB5lqz Structure of the mitochondrial ATP synthase fromPichia angustadetermined by electron cryo-microscopy.
ChainC
Resolution7.0 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 R167 Q168 G170 K171 T172 A173 R358 K427 Q428
Gene Ontology
Molecular Function
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:0016020 membrane
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:5lqz, PDBe:5lqz, PDBj:5lqz
PDBsum5lqz
PubMed27791192
UniProtW1Q6W1

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