Structure of PDB 7val Chain C

Receptor sequence

>7valC (length=578) Species: 300852 (Thermus thermophilus HB8)

MIQGVIQKIAGPAVIAKGMLGARMYDICKVGEEGLVGEIIRLDGDTAFVQ
VYEDTSGLKVGEPVVSTGLPLAVELGPGMLNGIYDGIQRPLERIREKTGI
YITRGVVVHALDREKKWAWTPMVKPGDEVRGGMVLGTVPEFGFTHKILVP
PDVRGRVKEVKPAGEYTVEEPVVVLEDGTELKMYHTWPVRRARPVQRKLD
PNTPFLTGMRILDVLFPVAMGGTAAIPGPFGAGKSVTQQSLAKWSNADVV
VYVGCGERGNEMTDVLVEFPELTDPKTGGPLMHRTVLIANTSNMPVAARE
ASIYVGVTIAEYFRDQGFSVALMADSTSRWAEALREISSRLEEMPAEEGY
PPYLAARLAAFYERAGKVITLGGEEGAVTIVGAVSPPGGDMSEPVTQSTL
RIVGAFWRLDASLAFRRHFPAINWNGSYSLFTSALDPWYRENVAEDYPEL
RDAISELLQREAGLQEIVQLVGPDALQDAERLVIEVGRIIREDFLQQNAY
HEVDAYCSMKKAYGIMKMILAFYKEAEAAIKRGVSIDEILQLPVLERIGR
ARYVSEEEFPAYFEEAMKEIQGAFKALA

3D structure

• PDB: 7val Structural snapshots of V/A-ATPase reveal the rotary catalytic mechanism of rotary ATPases.
• Chain: C
• Resolution: 3.1 Å

Enzymatic activity

• 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	C	G233 K234 S235 V236 R258 F419 A499	G233 K234 S235 V236 R258 F419 A499

Gene Ontology

Molecular Function

• GO:0005515 protein binding
• GO:0005524 ATP binding
• 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:0042777 proton motive force-driven plasma membrane ATP synthesis
• GO:0046034 ATP metabolic process
• GO:1902600 proton transmembrane transport

Cellular Component

• GO:0045259 proton-transporting ATP synthase complex

External links

• PDB: RCSB:7val, PDBe:7val, PDBj:7val
• PDBsum: 7val
• PubMed: 35260556
• UniProt: Q56403|VATA_THET8 V-type ATP synthase alpha chain (Gene Name=atpA)