Structure of PDB 6res Chain Z

Receptor sequence
>6resZ (length=542) Species: 37502 (Polytomella sp. Pringsheim 198.80) [Search protein sequence]
PAIDAGYVSQVIGPVVDVRFDGELPSILSSLEVEGHSVRLVLEVAQHMGD
NTVRCIAMDSTDGLVRGQKVVDTGSPIKVPVGRGTLGRIMNVIGEPVDEQ
GPIDAADIWSIHREAPEFTEQSTEQEILVTGIKVVDLLAPYQRGGKIGLF
GGAGVGKTVLIMELINNVAKAHGGFSVFAGVGERTREGNDLYREMIESGV
IKLGAERGNSKCTLVYGQMNEPPGARARVALTGLTVAEYFRDIEGQDVLL
FVDNIFRFTQANSEVSALLGRIPSAVGYQPTLATDLGGLQERITTTTKGS
ITSVQAVYVPADDLTDPAPATTFAHLDATTVLSRSIAELGIYPAVDPLDS
TSRMLNPNVIGAEHYNVARGVQKVLQDYKNLQDIIAILGMDELSEEDKLT
VARARKIQRFLSQPFQVAEVFTGTPGKYVDLADTISGFQGVLTGKYDDLP
EMAFYMVGDIKEVKEKADKMAKDIASRKEADNKKVSEELKDIPSLDKLVS
EIKEVVIEEDDGLEEDFKAEALSSETVVLNEEGKSVPLPKKN
3D structure
PDB6res Rotary substates of mitochondrial ATP synthase reveal the basis of flexible F 1 -F o coupling.
ChainZ
Resolution4.3 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) K157 E183 R184 R353
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 ADP Z A185 G186 V187 G188 K189 T190 V191 Y374 F447 A153 G154 V155 G156 K157 T158 V159 Y342 F415
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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Cellular Component
External links
PDB RCSB:6res, PDBe:6res, PDBj:6res
PDBsum6res
PubMed31221832
UniProtA0ZW41

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