Structure of PDB 7tmo Chain E

Receptor sequence
>7tmoE (length=590) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence]
YGAIYSVSGPVVIAENMIGCAMYELVKVGHDNLVGEVIRIDGDKATIQVY
EETAGLTVGDPVLRTGKPLSVELGPGLMETIYDGIQRPLKAIKEESQSIY
IPRGIDTPALDRTIKWQFTPGKFQVGDHISGGDIYGSVFENSLISSHKIL
LPPRSRGTITWIAPAGEYTLDEKILEVEFDGKKSDFTLYHTWPVRVPRPV
TEKLSADYPLLTGQRVLDALFPCVQGGTTCIPGAFGCGKTVISQSLSKYS
NSDAIIYVGCGERGNEMAEVLMEFPELYTEMSGTKEPIMKRTTLVANTSN
MPVAAREASIYTGITLAEYFRDQGKNVSMIADSSSRWAEALREISGRLGE
MPADQGFPAYLGAKLASFYERAGKAVALGSPDRTGSVSIVAAVSPAGGDF
SDPVTTATLGITQVFWGLDKKLAQRKHFPSINTSVSYSKYTNVLNKFYDS
NYPEFPVLRDRMKEILSNAEELEQVVQLVGKSALSDSDKITLDVATLIKE
DFLQQNGYSTYDAFCPIWKTFDMMRAFISYHDEAQKAVANGANWSKLADS
TGDVKHAVSSSKFFEPSRGEKEVHGEFEKLLSTMQERFAE
3D structure
PDB7tmo Coordinated conformational changes in the V 1 complex during V-ATPase reversible dissociation.
ChainE
Resolution3.3 Å
3D
structure
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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 ADP E F258 G259 G261 K262 T263 V264 F451 N529 G530 F235 G236 G238 K239 T240 V241 F428 N506 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

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:7tmo, PDBe:7tmo, PDBj:7tmo
PDBsum7tmo
PubMed35469063
UniProtP17255|VATA_YEAST V-type proton ATPase catalytic subunit A (Gene Name=VMA1)

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