Structure of PDB 6rea Chain V

Receptor sequence
>6reaV (length=520) Species: 37502 (Polytomella sp. Pringsheim 198.80) [Search protein sequence]
KALDELRKPKFSSKYLIQHVSQKLIPAVKEWEKSYQPPVIHLGRVLSVGD
GIARVYGLKSVQAGELVCFDSGVKGMALNLQADHVGVVVFGNDSVIHQGD
LVYRTGQIVNVPIGPGTLGRVTDGLGQPIDGKGPLTNVRSSLVEVKAPGI
IARQSVREPLFTGVKAVDALVPIGRGQRELIIGDRQTGKTAVAIDAIIHQ
KNCNEQVPKAQRVYCVYVAVGQKRSTVAQLVKLFTQTGAMRYTIMVSATA
SDAAPLQFLAPYSGCAMAEYFRDTGKHGLIIYDDLSKQSVAYRQMSLLLR
RPPGREAFPGDVFYLHSRLLERAAKLSKELGGGSLTAFPVIETQAGDVSA
YIATNVISITDGQIFLETELFYKGIRPALNVGLSVSRVGSAAQFPGMKQV
AGTLKLELAQYREVAAFAQFGSDLDAATQYVLERGARLTEMLKQKQFAPI
PIERQTVAVYAATKGFLDKVRVQDIVAAEEAVISQVNPAVFKILKANGKI
TPALDAHLKAELRKVKLPGA
3D structure
PDB6rea Rotary substates of mitochondrial ATP synthase reveal the basis of flexible F 1 -F o coupling.
ChainV
Resolution3.6 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K231 Q264 K265 R429
Catalytic site (residue number reindexed from 1) K189 Q222 K223 R387
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 V R227 Q228 G230 K231 T232 A233 R418 Q486 K487 Q488 R185 Q186 G188 K189 T190 A191 R376 Q444 K445 Q446
Gene Ontology
Molecular Function
GO:0005524 ATP binding
GO:0016787 hydrolase activity
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:0005739 mitochondrion
GO:0005743 mitochondrial inner 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:6rea, PDBe:6rea, PDBj:6rea
PDBsum6rea
PubMed31221832
UniProtA0ZW40

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