Structure of PDB 7vat Chain E

Receptor sequence
>7vatE (length=468) Species: 300852 (Thermus thermophilus HB8) [Search protein sequence]
LLKKEYTGITYISGPLLFVENAKDLAYGAIVDIKDGTGRVRGGQVIEVSE
EYAVIQVFEETTGLDLATTSVSLVEDVARLGVSKEMLGRRFNGIGKPIDG
LPPITPEKRLPITGLPLNPVARRKPEQFIQTGISTIDVMNTLVRGQKLPI
FSGSGLPANEIAAQIARQATVRPDLSGEGEKEEPFAVVFAAMGITQRELS
YFIQEFERTGALSRSVLFLNKADDPTIERILTPRMALTVAEYLAFEHDYH
VLVILTDMTNYCEALREIGAAREEIPGRRGYPGYMYTDLATIYERAGVVE
GKKGSVTQIPILSMPDDDRTHPIPDLTGYITEGQIQLSRELHRKGIYPPI
DPLPSLSRLMNNGVGKGKTREDHKQVSDQLYSAYANGVDIRKLVAIIGED
ALTENDRRYLQFADAFERFFINQGQQNRSIEESLQIAWALLSMLPQGELK
RISKDHIGKYYGQKLEEI
3D structure
PDB7vat Structural snapshots of V/A-ATPase reveal the rotary catalytic mechanism of rotary ATPases.
ChainE
Resolution3.2 Å
3D
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
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 E Y331 R360 Y329 R358
Gene Ontology
Molecular Function
GO:0005515 protein binding
GO:0005524 ATP binding
GO:0046933 proton-transporting ATP synthase activity, rotational mechanism
Biological Process
GO:0006754 ATP biosynthetic process
GO:0042777 proton motive force-driven plasma membrane ATP synthesis
GO:0046034 ATP metabolic process
GO:1902600 proton transmembrane transport

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:7vat, PDBe:7vat, PDBj:7vat
PDBsum7vat
PubMed35260556
UniProtQ56404|VATB_THET8 V-type ATP synthase beta chain (Gene Name=atpB)

[Back to BioLiP]