Structure of PDB 6oqw Chain F

Receptor sequence
>6oqwF (length=458) Species: 741093 (Escherichia coli Xuzhou21) [Search protein sequence]
TGKIVQVIGAVVDVEFPQDAVPRVYDALEVQNGNERLVLEVQQQLGGGIV
RTIAMGSSDGLRRGLDVKDLEHPIEVPVGKATLGRIMNVLGEPVDMKGEI
GEEERWAIHRAAPSYEELSNSQELLETGIKVIDLMAPFAKGGKVGLFGGA
GVGKTVNMMELIRNIAIEHSGYSVFAGVGERTREGNDFYHEMTDSNVIDK
VSLVYGQMNEPPGNRLRVALTGLTMAEKFRDEGRDVLLFVDNIYRYTLAG
TEVSALLGRMPSAVGYQPTLAEEMGVLQERITSTKTGSITSVQAVYVPAD
DLTDPSPATTFAHLDATVVLSRQIASLGIYPAVDPLDSTSRQLDPLVVGQ
EHYDTARGVQSILQRYQELKDIIAILGMDELSEEDKLVVARARKIQRFLS
QPFFVAEVFTGSPGKYVSLKDTIRGFKGIMEGEYDHLPEQAFYMVGSIEE
AVEKAKKL
3D structure
PDB6oqw Cryo-EM structures provide insight into how E. coli F1FoATP synthase accommodates symmetry mismatch.
ChainF
Resolution3.1 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) K155 E181 R182 R342
Catalytic site (residue number reindexed from 1) K154 E180 R181 R341
Enzyme Commision number 7.1.2.2: H(+)-transporting two-sector ATPase.
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 G152 G154 K155 T156 V157 Y331 A407 F410 G151 G153 K154 T155 V156 Y330 A406 F409
BS02 MG F T156 E185 T155 E184
Gene Ontology
Molecular Function
GO:0005515 protein binding
GO:0005524 ATP binding
GO:0016887 ATP hydrolysis activity
GO:0046933 proton-transporting ATP synthase activity, rotational mechanism
GO:0046961 proton-transporting ATPase activity, rotational mechanism
Biological Process
GO:0006754 ATP biosynthetic process
GO:0015986 proton motive force-driven ATP synthesis
GO:0042777 proton motive force-driven plasma membrane ATP synthesis
GO:0046034 ATP metabolic process
GO:1902600 proton transmembrane transport
Cellular Component
GO:0005886 plasma membrane
GO:0016020 membrane
GO:0045259 proton-transporting ATP synthase complex
GO:0045261 proton-transporting ATP synthase complex, catalytic core F(1)

View graph for
Molecular Function

View graph for
Biological Process

View graph for
Cellular Component
External links
PDB RCSB:6oqw, PDBe:6oqw, PDBj:6oqw
PDBsum6oqw
PubMed32457314
UniProtP0ABB4|ATPB_ECOLI ATP synthase subunit beta (Gene Name=atpD)

[Back to BioLiP]