Structure of PDB 6ref Chain Y

Receptor sequence
>6refY (length=521) Species: 37502 (Polytomella sp. Pringsheim 198.80) [Search protein sequence]
DAGYVSQVIGPVVDVRFDGELPSILSSLEVEGHSVRLVLEVAQHMGDNTV
RCIAMDSTDGLVRGQKVVDTGSPIKVPVGRGTLGRIMNVIGEPVDEQGPI
DAADIWSIHREAPEFTEQSTEQEILVTGIKVVDLLAPYQRGGKIGLFGGA
GVGKTVLIMELINNVAKAHGGFSVFAGVGERTREGNDLYREMIESGVIKL
GAERGNSKCTLVYGQMNEPPGARARVALTGLTVAEYFRDIEGQDVLLFVD
NIFRFTQANSEVSALLGRIPSAVGYQPTLATDLGGLQERITTTTKGSITS
VQAVYVPADDLTDPAPATTFAHLDATTVLSRSIAELGIYPAVDPLDSTSR
MLNPNVIGAEHYNVARGVQKVLQDYKNLQDIIAILGMDELSEEDKLTVAR
ARKIQRFLSQPFQVAEVFTGTPGKYVDLADTISGFQGVLTGKYDDLPEMA
FYMVGDIKEVKEKADKMAKDIASRKEADNKKVSEELKDIPSLDKLVSEIK
EVVIEEDDGLEEDFKAEALSS
3D structure
PDB6ref Rotary substates of mitochondrial ATP synthase reveal the basis of flexible F 1 -F o coupling.
ChainY
Resolution3.3 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K189 E215 R216 R385
Catalytic site (residue number reindexed from 1) K154 E180 R181 R350
Enzyme Commision number 7.1.2.2: H(+)-transporting two-sector ATPase.
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 Y R385 N388 R350 N353
Gene Ontology
Molecular Function
GO:0005524 ATP binding
GO:0016787 hydrolase activity
GO:0016887 ATP hydrolysis activity
GO:0046933 proton-transporting ATP synthase activity, rotational mechanism
GO:0046961 proton-transporting ATPase activity, rotational mechanism
Biological Process
GO:0006754 ATP biosynthetic process
GO:0015986 proton motive force-driven ATP synthesis
GO:0042776 proton motive force-driven mitochondrial ATP synthesis
GO:0046034 ATP metabolic process
GO:1902600 proton transmembrane transport
Cellular Component
GO:0005739 mitochondrion
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:6ref, PDBe:6ref, PDBj:6ref
PDBsum6ref
PubMed31221832
UniProtA0ZW41

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