Structure of PDB 3vr3 Chain F

Receptor sequence
>3vr3F (length=451) Species: 1354 (Enterococcus hirae) [Search protein sequence]
EYRTIKEVVGPLMAVEKVSGVKYEELIEVRMQNGEIRRGQVLEVQEDKAM
VQIFEGTSGINLKNSSVRFLGHPLQLGVSEDMIGRVFDGLGRPKDNGPEI
LPEKYLDINGEVINPIARDYPDEFIQTGISAIDHLNTLVRGQKLPVFSGS
GLPHKELAAQIARQATVLDSSDDFAVVFAAIGITFEEAEFFMEDFRQTGA
IDRSVMFMNLANDPAIERIATPRMALTAAEYLAYEKGMHVLVIMTDMTNY
AEALREISAARREVPGRRGYPGYLYTNLATLFERAGRIRGLKGSVTQIPI
LTMPEDDKTHPIPDLTGYITEGQIILTRELYKSGIQPPIDVLPSLSRLKD
KGTGAGKTREDHAATMNQLFAAYAQGKQAKELAVVLGESALSDIDKIYAK
FAERFENEYVNQGFYTNRTITETLDLGWELLAMLPRTELKRIKDDLLDKY
L
3D structure
PDB3vr3 Rotation mechanism of Enterococcus hirae V(1)-ATPase based on asymmetric crystal structures
ChainF
Resolution3.4 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H157 I186 T187 R350
Catalytic site (residue number reindexed from 1) H154 I183 T184 R347
Enzyme Commision number 3.6.3.15: Transferred entry: 7.2.2.1.
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 ANP F Y321 R350 Y318 R347
Gene Ontology
Molecular Function
GO:0005515 protein binding
GO:0005524 ATP binding
GO:0046933 proton-transporting ATP synthase activity, rotational mechanism
Biological Process
GO:0006814 sodium ion transport
GO:0042777 proton motive force-driven plasma membrane ATP synthesis
GO:0046034 ATP metabolic process
GO:1902600 proton transmembrane transport

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Molecular Function
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Biological Process
External links
PDB RCSB:3vr3, PDBe:3vr3, PDBj:3vr3
PDBsum3vr3
PubMed23334411
UniProtQ08637|NTPB_ENTHA V-type sodium ATPase subunit B (Gene Name=ntpB)

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