Structure of PDB 7tap Chain F

Receptor sequence
>7tapF (length=159) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence]
MTELCPVYAPFFGAIGCASAIIFTSLGAAYGTAKSGVGICATCVLRPDLL
FKNIVPVIMAGIIAIYGLVVSVLVCYSLGQKQALYTGFIQLGAGLSVGLS
GLAAGFAIGIVGDAGVRGSSQQPRLFVGMILILIFAEVLGLYGLIVALLL
NSRATQDVV
3D structure
PDB7tap Cryo-EM of the Yeast V O Complex Reveals Distinct Binding Sites for Macrolide V-ATPase Inhibitors.
ChainF
Resolution2.8 Å
3D
structure
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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 KJL F I58 G61 I62 I65 Y66 E137 I58 G61 I62 I65 Y66 E137
BS02 KJL F F135 V138 Y142 F135 V138 Y142
Gene Ontology
Molecular Function
GO:0015078 proton transmembrane transporter activity
GO:0046961 proton-transporting ATPase activity, rotational mechanism
Biological Process
GO:0006623 protein targeting to vacuole
GO:0006878 intracellular copper ion homeostasis
GO:0006879 intracellular iron ion homeostasis
GO:0006897 endocytosis
GO:0007033 vacuole organization
GO:0007035 vacuolar acidification
GO:0048388 endosomal lumen acidification
GO:0061795 Golgi lumen acidification
GO:1902600 proton transmembrane transport
Cellular Component
GO:0000139 Golgi membrane
GO:0000220 vacuolar proton-transporting V-type ATPase, V0 domain
GO:0000329 fungal-type vacuole membrane
GO:0005773 vacuole
GO:0005774 vacuolar membrane
GO:0016020 membrane
GO:0016471 vacuolar proton-transporting V-type ATPase complex
GO:0033176 proton-transporting V-type ATPase complex
GO:0033177 proton-transporting two-sector ATPase complex, proton-transporting domain
GO:0033179 proton-transporting V-type ATPase, V0 domain

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:7tap, PDBe:7tap, PDBj:7tap
PDBsum7tap
PubMed35148071
UniProtP25515|VATL1_YEAST V-type proton ATPase subunit c (Gene Name=VMA3)

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