Structure of PDB 6r0w Chain E

Receptor sequence
>6r0wE (length=462) Species: 300852 (Thermus thermophilus HB8) [Search protein sequence]
LLKKEYTGITYISGPLLFVENAKDLAYGAIVDIKDGTGRVRGGQVIEVSE
EYAVIQVFEETTGLDLATTSVSLVEDVARLGVSKEMLGRRFNGIGKPIDG
LPPITPEKRLPITGLPLNPVARRKPEQFIQTGISTIDVMNTLVRGQKLPI
FSGSGLPANEIAAQIARQATVRPDLSGEGEKEEPFAVVFAAMGITQRELS
YFIQEFERTGALSRSVLFLNKADDPTIERILTPRMALTVAEYLAFEHDYH
VLVILTDMTNYCEALREIGAAREEIPGRRGYPGYMYTDLATIYERAGVVE
GKKGSVTQIPILSMPDDDRTHPIPDLTGYITEGQIQLSRELHRKGIYPPI
DPLPSLSRLMNNGVGKGKTREDHKQVSDQLYSAYANGVDIRKLVAIIGED
ALTENDRRYLQFADAFERFFINQGQQNRSIEESLQIAWALLSMLPQGELK
RISKDHIGKYYG
3D structure
PDB6r0w Structure and conformational plasticity of the intact Thermus thermophilus V/A-type ATPase.
ChainE
Resolution3.6 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) A158 I194 T195 R358
Enzyme Commision number ?
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 R274 E275 R272 E273
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:6r0w, PDBe:6r0w, PDBj:6r0w
PDBsum6r0w
PubMed31439765
UniProtQ56404|VATB_THET8 V-type ATP synthase beta chain (Gene Name=atpB)

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