Structure of PDB 6vq7 Chain B

Receptor sequence
>6vq7B (length=600) Species: 10116 (Rattus norvegicus) [Search protein sequence]
TFGYVHGVSGPVVTACDMAGAAMYELVRVGHSELVGEIIRLEGDMATIQV
YEETSGVSVGDPVLRTGKPLSVELGPGIMGAIFDGIQRPLSDISSQTQSI
YIPRGVNVSALSRDIKWEFIPSKNLRVGSHITGGDIYGIVNENSLIKHKI
MLPPRSRGSVTYIAPPGNYDASDVVLELEFEGVKEKLSMVQVWPVRQVRP
VTEKLPANHPLLTGQRVLDALFPCVQGGTTAIPGAFGCGKTVISQSLSKY
SNSDVIIYVGCGERGNEMSEVLRDFPELTMEVDGKVESIMKRTALVANTS
NMPVAAREASIYTGITLSEYFRDMGYHVSMMADSTSRWAEALREISGRLA
EMPADSGYPAYLGARLASFYERAGRVKCLGNPEREGSVSIVGAVSPPGGD
FSDPVTSATLGIVQVFWGLDKKLAQRKHFPSVNWLISYSKYMRALDEYYD
KHFTEFVPLRTKAKEILQEEEDLAEIVQLVGKASLAETDKITLEVAKLIK
DDFLQQNGYTPYDRFCPFYKTVGMLSNMISFYDMARRAVETTAQSDNKIT
WSIIREHMGEILYKLSSMKFKDPVKDGEAKIKADYAQLLEDMQNAFRSLE
3D structure
PDB6vq7 Structure of V-ATPase from the mammalian brain.
ChainB
Resolution4.0 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) K256 E279 R280 K456
Catalytic site (residue number reindexed from 1) K240 E263 R264 K440
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 ADP B F252 G253 C254 G255 K256 T257 V258 F445 G524 Y525 F236 G237 C238 G239 K240 T241 V242 F429 G508 Y509
Gene Ontology
Molecular Function
GO:0005515 protein binding
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:0046034 ATP metabolic process
GO:0097401 synaptic vesicle lumen acidification
GO:1902600 proton transmembrane transport
Cellular Component
GO:0000221 vacuolar proton-transporting V-type ATPase, V1 domain
GO:0005654 nucleoplasm
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0005886 plasma membrane
GO:0005902 microvillus
GO:0016020 membrane
GO:0016324 apical plasma membrane
GO:0030133 transport vesicle
GO:0030141 secretory granule
GO:0030665 clathrin-coated vesicle membrane
GO:0033176 proton-transporting V-type ATPase complex
GO:0033180 proton-transporting V-type ATPase, V1 domain
GO:0043231 intracellular membrane-bounded organelle
GO:0098850 extrinsic component of synaptic vesicle membrane
GO:1904949 ATPase complex

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:6vq7, PDBe:6vq7, PDBj:6vq7
PDBsum6vq7
PubMed32165585
UniProtD4A133

[Back to BioLiP]