Structure of PDB 3w3a Chain E

Receptor sequence
>3w3aE (length=457) Species: 300852 (Thermus thermophilus HB8) [Search protein sequence]
EYTGITYISGPLLFVENAKDLAYGAIVDIKDGTGRVRGGQVIEVSEEYAV
IQVFEETTGLDLATTSVSLVEDVARLGVSKEMLGRRFNGIGKPIDGLPPI
TPEKRLPITGLPLNPVARRKPEQFIQTGISTIDVMNTLVRGQKLPIFSGS
GLPANEIAAQIARQATVRPDLSGEGEKEEPFAVVFAAMGITQRELSYFIQ
EFERTGALSRSVLFLNKADDPTIERILTPRMALTVAEYLAFEHDYHVLVI
LTDMTNYCEALREIGAAREEIPGRRGYPGYMYTDLATIYERAGVVEGKKG
SVTQIPILSMPDDDRTHPIPDLTGYITEGQIQLSRELHRKGIYPPIDPLP
SLSRLMNNGVGKGKTREDHKQVSDQLYSAYANGVDIRKLVAIIGEDALTE
NDRRYLQFADAFERFFINQGQQNRSIEESLQIAWALLSMLPQGELKRISK
DHIGKYY
3D structure
PDB3w3a Origin of Asymmetry at the Intersubunit Interfaces of V1-ATPase from Thermusthermophilus
ChainE
Resolution3.9 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) A160 I196 T197 R360
Catalytic site (residue number reindexed from 1) A154 I190 T191 R354
Enzyme Commision number 3.6.3.14: Transferred entry: 7.1.2.2.
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 E R360 N363 R354 N357
Gene Ontology
Molecular Function
GO:0005515 protein binding
GO:0005524 ATP binding
GO:0046933 proton-transporting ATP synthase activity, rotational mechanism
Biological Process
GO:0006754 ATP biosynthetic process
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:3w3a, PDBe:3w3a, PDBj:3w3a
PDBsum3w3a
PubMed23639357
UniProtQ56404|VATB_THET8 V-type ATP synthase beta chain (Gene Name=atpB)

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