Structure of PDB 6xbw Chain C

Receptor sequence
>6xbwC (length=597) Species: 9913 (Bos taurus) [Search protein sequence]
STFGYVHGVSGPVVTACDMAGAAMYELVRVGHSELVGEIIRLEGDMATIQ
VYEETSGVSVGDPVLRTGKPLSVELGPGIMGAIFDGIQRPLSDISSQTQS
IYIPRGVNVSALSRDVKWDFTPCKNLRVGSHITGGDIYGIVNENSLIKHK
IMLPPRNRGTVTYIAPPGNYDTSDVVLELEFEGIKEKFSMVQVWPVRQVR
PVTEKLPANHPLLTGQRVLDALFPCVQGGTTAIPGAFGCGKTVISQSLSK
YSNSDVIIYVGCGERGNEMSEVLRDFPELTMEVDGKVESIMKRTALVANT
SNMPVAAREASIYTGITLSEYFRDMGYHVSMMADSTSRWAEALREISGRL
AEMPADSGYPAYLGARLASFYERAGRVKCLGNPEREGSVSIVGAVSPPGG
DFSDPVTSATLGIVQVFWGLDKKLAQRKHFPSVNWLISYSKYMRALDEYY
DKHFTEFVPLRTKAKEILQEEEDLAEIVQLVGKASLAETDKITLEVAKLI
KDDFLQQNGYTPYDRFCPFYKTVGMLSNMIAFYDMARRAVETTAQSDNKI
TWSIIREHMGEILYKLSSMKFKDPVKDGEAKIKADYAQLLEDMQNAF
3D structure
PDB6xbw Cryo-EM structures of intact V-ATPase from bovine brain.
ChainC
Resolution3.37 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K256 E279 R280 K456
Catalytic site (residue number reindexed from 1) K241 E264 R265 K441
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 MG C T257 E283 T242 E268
BS02 ADP C G253 G255 K256 T257 V258 F445 N523 G524 Y525 G238 G240 K241 T242 V243 F430 N508 G509 Y510
Gene Ontology
Molecular Function
GO:0005524 ATP binding
GO:0016887 ATP hydrolysis activity
GO:0046933 proton-transporting ATP synthase activity, rotational mechanism
GO:0046961 proton-transporting ATPase activity, rotational mechanism
Biological Process
GO:0006879 intracellular iron ion homeostasis
GO:0015986 proton motive force-driven ATP synthesis
GO:0036295 cellular response to increased oxygen levels
GO:0045851 pH reduction
GO:0046034 ATP metabolic process
GO:1902600 proton transmembrane transport
Cellular Component
GO:0000221 vacuolar proton-transporting V-type ATPase, V1 domain
GO:0005737 cytoplasm
GO:0005764 lysosome
GO:0005829 cytosol
GO:0005886 plasma membrane
GO:0016020 membrane
GO:0030133 transport vesicle
GO:0030665 clathrin-coated vesicle membrane
GO:0031410 cytoplasmic vesicle
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:6xbw, PDBe:6xbw, PDBj:6xbw
PDBsum6xbw
PubMed32764564
UniProtP31404|VATA_BOVIN V-type proton ATPase catalytic subunit A (Gene Name=ATP6V1A)

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