Structure of PDB 6r0y Chain D

Receptor sequence
>6r0yD (length=461) Species: 300852 (Thermus thermophilus HB8) [Search protein sequence]
KKEYTGITYISGPLLFVENAKDLAYGAIVDIKDGTGRVRGGQVIEVSEEY
AVIQVFEETTGLDLATTSVSLVEDVARLGVSKEMLGRRFNGIGKPIDGLP
PITPEKRLPITGLPLNPVARRKPEQFIQTGISTIDVMNTLVRGQKLPIFS
GSGLPANEIAAQIARQATVRPDLSGEGEKEEPFAVVFAAMGITQRELSYF
IQEFERTGALSRSVLFLNKADDPTIERILTPRMALTVAEYLAFEHDYHVL
VILTDMTNYCEALREIGAAREEIPGRRGYPGYMYTDLATIYERAGVVEGK
KGSVTQIPILSMPDDDRTHPIPDLTGYITEGQIQLSRELHRKGIYPPIDP
LPSLSRLMNNGVGKGKTREDHKQVSDQLYSAYANGVDIRKLVAIIGEDAL
TENDRRYLQFADAFERFFINQGQQNRSIEESLQIAWALLSMLPQGELKRI
SKDHIGKYYGQ
3D structure
PDB6r0y Structure and conformational plasticity of the intact Thermus thermophilus V/A-type ATPase.
ChainD
Resolution3.9 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) A160 I196 T197 R360
Catalytic site (residue number reindexed from 1) A156 I192 T193 R356
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 D F20 V56 R274 F16 V52 R270
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

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:6r0y, PDBe:6r0y, PDBj:6r0y
PDBsum6r0y
PubMed31439765
UniProtQ56404|VATB_THET8 V-type ATP synthase beta chain (Gene Name=atpB)

[Back to BioLiP]