Structure of PDB 6rdq Chain V

Receptor sequence
>6rdqV (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
PDB6rdq Rotary substates of mitochondrial ATP synthase reveal the basis of flexible F 1 -F o coupling.
ChainV
Resolution4.0 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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 Q228 G230 K231 T232 A233 R418 Q488 Q186 G188 K189 T190 A191 R376 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)

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:6rdq, PDBe:6rdq, PDBj:6rdq
PDBsum6rdq
PubMed31221832
UniProtA0ZW40

[Back to BioLiP]