Structure of PDB 7tmo Chain A

Receptor sequence

>7tmoA (length=592) Species: 4932 (Saccharomyces cerevisiae)

YGAIYSVSGPVVIAENMIGCAMYELVKVGHDNLVGEVIRIDGDKATIQVY
EETAGLTVGDPVLRTGKPLSVELGPGLMETIYDGIQRPLKAIKEESQSIY
IPRGIDTPALDRTIKWQFTPGKFQVGDHISGGDIYGSVFENSLISSHKIL
LPPRSRGTITWIAPAGEYTLDEKILEVEFDGKKSDFTLYHTWPVRVPRPV
TEKLSADYPLLTGQRVLDALFPCVQGGTTCIPGAFGCGKTVISQSLSKYS
NSDAIIYVGCGERGNEMAEVLMEFPELYTEMSGTKEPIMKRTTLVANTSN
MPVAAREASIYTGITLAEYFRDQGKNVSMIADSSSRWAEALREISGRLGE
MPADQGFPAYLGAKLASFYERAGKAVALGSPDRTGSVSIVAAVSPAGGDF
SDPVTTATLGITQVFWGLDKKLAQRKHFPSINTSVSYSKYTNVLNKFYDS
NYPEFPVLRDRMKEILSNAEELEQVVQLVGKSALSDSDKITLDVATLIKE
DFLQQNGYSTYDAFCPIWKTFDMMRAFISYHDEAQKAVANGANWSKLADS
TGDVKHAVSSSKFFEPSRGEKEVHGEFEKLLSTMQERFAEST

3D structure

• PDB: 7tmo Coordinated conformational changes in the V 1 complex during V-ATPase reversible dissociation.
• Chain: A
• Resolution: 3.3 Å

Enzymatic activity

• Enzyme Commision number: 3.1.-.-
  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	A	G259 G261 K262 T263 V264 R286 F451 G530	G236 G238 K239 T240 V241 R263 F428 G507

Gene Ontology

Molecular Function

• GO:0005524 ATP binding
• GO:0016887 ATP hydrolysis activity
• GO:0046961 proton-transporting ATPase activity, rotational mechanism

Biological Process

• GO:0046034 ATP metabolic process
• GO:1902600 proton transmembrane transport

Cellular Component

• GO:0033180 proton-transporting V-type ATPase, V1 domain

External links

• PDB: RCSB:7tmo, PDBe:7tmo, PDBj:7tmo
• PDBsum: 7tmo
• PubMed: 35469063
• UniProt: P17255|VATA_YEAST V-type proton ATPase catalytic subunit A (Gene Name=VMA1)