Structure of PDB 6afv Chain A

Receptor sequence
>6afvA (length=740) Species: 3916 (Vigna radiata var. radiata) [Search protein sequence]
GAAILPDLGTEILIPVCAVIGIAFALFQWLLVSKVKLSAVDHNVVVKCAE
IQNAISEGATSFLFTEYKYVGIFMVAFAILIFLFLGSVEGFSTSPQACSY
DKTKTCKPALATAIFSTVSFLLGGVTSLVSGFLGMKIATYANARTTLEAR
KGVGKAFITAFRSGAVMGFLLAANGLLVLYIAINLFKIYYGDDWGGLFEA
ITGYGLGGSSMALFGRVGGGIYTKAADVGADLVGKVERNIPEDDPRNPAV
IADNVGDNVGDIAGMGSDLFGSYAESSCAALVVASISSFGLNHELTAMLY
PLIVSSVGILVCLLTTLFATDFFEIKAVKEIEPALKKQLVISTVLMTIGV
AVVSFVALPTSFTIFNFGVQKDVKSWQLFLCVAVGLWAGLIIGFVTEYYT
SNAYSPVQDVADSCRTGAATNVIFGLALGYKSVIIPIFAIAISIFVSFTF
AAMYGIAVAALGMLSTIATGLAIDAYGPISDNAGGIAEMAGMSHRIRERT
DALDAAGNTTAAIGKGFAIGSAALVSLAKFGAFVSRASITTVDVLTPKVF
IGLIVGAMLPYWFSAMTMKSVGSAALKMVEEVRRQFNTIPGLMEGTAKPD
YATCVKISTDASIKEMIPPGALVMLTPLVVGILFGVETLSGVLAGSLVSG
VQIAISASNTGGAWDNAKKYIEAGASEHARSLGPKGSDCHKAAVIGDTIG
DPLKDTSGPSLNILIKLMAVESLVFAPFFATHGGLLFKIF
3D structure
PDB6afv Roles of the Hydrophobic Gate and Exit Channel in Vigna radiata Pyrophosphatase Ion Translocation.
ChainA
Resolution2.701 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 7.1.3.1: H(+)-exporting diphosphatase.
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 PO4 A K250 D287 D731 K224 D261 D705
BS02 PO4 A D253 D507 D227 D481
BS03 MG A D253 D257 D227 D231
BS04 MG A D253 D727 D227 D701
Gene Ontology
Molecular Function
GO:0004427 inorganic diphosphate phosphatase activity
GO:0009678 diphosphate hydrolysis-driven proton transmembrane transporter activity
GO:0046872 metal ion binding
Biological Process
GO:1902600 proton transmembrane transport
Cellular Component
GO:0005773 vacuole
GO:0005774 vacuolar membrane
GO:0016020 membrane

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:6afv, PDBe:6afv, PDBj:6afv
PDBsum6afv
PubMed30878480
UniProtP21616|AVP_VIGRR Pyrophosphate-energized vacuolar membrane proton pump

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