Structure of PDB 6oqr Chain F

Receptor sequence
>6oqrF (length=458) Species: 562 (Escherichia coli) [Search protein sequence]
TGKIVQVIGAVVDVEFPQDAVPRVYDALEVQNGNERLVLEVQQQLGGGIV
RTIAMGSSDGLRRGLDVKDLEHPIEVPVGKATLGRIMNVLGEPVDMKGEI
GEEERWAIHRAAPSYEELSNSQELLETGIKVIDLMAPFAKGGKVGLFGGA
GVGKTVNMMELIRNIAIEHSGYSVFAGVGERTREGNDFYHEMTDSNVIDK
VSLVYGQMNEPPGNRLRVALTGLTMAEKFRDEGRDVLLFVDNIYRYTLAG
TEVSALLGRMPSAVGYQPTLAEEMGVLQERITSTKTGSITSVQAVYVPAD
DLTDPSPATTFAHLDATVVLSRQIASLGIYPAVDPLDSTSRQLDPLVVGQ
EHYDTARGVQSILQRYQELKDIIAILGMDELSEEDKLVVARARKIQRFLS
QPFFVAEVFTGSPGKYVSLKDTIRGFKGIMEGEYDHLPEQAFYMVGSIEE
AVEKAKKL
3D structure
PDB6oqr 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
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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 E181 T155 E180
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)

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:6oqr, PDBe:6oqr, PDBj:6oqr
PDBsum6oqr
PubMed32457314
UniProtP0ABB4|ATPB_ECOLI ATP synthase subunit beta (Gene Name=atpD)

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