Structure of PDB 6r10 Chain F

Receptor sequence
>6r10F (length=460) Species: 300852 (Thermus thermophilus HB8) [Search protein sequence]
KKEYTGITYISGPLLFVENAKDLAYGAIVDIKDGTGRVRGGQVIEVSEEY
AVIQVFEETTGLDLATTSVSLVEDVARLGVSKEMLGRRFNGIGKPIDGLP
PITPEKRLPITGLPLNPVARRKPEQFIQTGISTIDVMNTLVRGQKLPIFS
GSGLPANEIAAQIARQATVRPDLSGEGEKEEPFAVVFAAMGITQRELSYF
IQEFERTGALSRSVLFLNKADDPTIERILTPRMALTVAEYLAFEHDYHVL
VILTDMTNYCEALREIGAAREEIPGRRGYPGYMYTDLATIYERAGVVEGK
KGSVTQIPILSMPDDDRTHPIPDLTGYITEGQIQLSRELHRKGIYPPIDP
LPSLSRLMNNGVGKGKTREDHKQVSDQLYSAYANGVDIRKLVAIIGEDAL
TENDRRYLQFADAFERFFINQGQQNRSIEESLQIAWALLSMLPQGELKRI
SKDHIGKYYG
3D structure
PDB6r10 Structure and conformational plasticity of the intact Thermus thermophilus V/A-type ATPase.
ChainF
Resolution4.3 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) 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 F F20 E49 R274 E275 F16 E45 R270 E271
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:6r10, PDBe:6r10, PDBj:6r10
PDBsum6r10
PubMed31439765
UniProtQ56404|VATB_THET8 V-type ATP synthase beta chain (Gene Name=atpB)

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