Structure of PDB 6oqr Chain F Binding Site BS02

Receptor Information
>6oqr Chain F (length=458) Species: 562 (Escherichia coli) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
TGKIVQVIGAVVDVEFPQDAVPRVYDALEVQNGNERLVLEVQQQLGGGIV
RTIAMGSSDGLRRGLDVKDLEHPIEVPVGKATLGRIMNVLGEPVDMKGEI
GEEERWAIHRAAPSYEELSNSQELLETGIKVIDLMAPFAKGGKVGLFGGA
GVGKTVNMMELIRNIAIEHSGYSVFAGVGERTREGNDFYHEMTDSNVIDK
VSLVYGQMNEPPGNRLRVALTGLTMAEKFRDEGRDVLLFVDNIYRYTLAG
TEVSALLGRMPSAVGYQPTLAEEMGVLQERITSTKTGSITSVQAVYVPAD
DLTDPSPATTFAHLDATVVLSRQIASLGIYPAVDPLDSTSRQLDPLVVGQ
EHYDTARGVQSILQRYQELKDIIAILGMDELSEEDKLVVARARKIQRFLS
QPFFVAEVFTGSPGKYVSLKDTIRGFKGIMEGEYDHLPEQAFYMVGSIEE
AVEKAKKL
Ligand information
Ligand IDMG
InChIInChI=1S/Mg/q+2
InChIKeyJLVVSXFLKOJNIY-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Mg+2]
CACTVS 3.341[Mg++]
FormulaMg
NameMAGNESIUM ION
ChEMBL
DrugBankDB01378
ZINC
PDB chain6oqr Chain F Residue 501 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB6oqr Cryo-EM structures provide insight into how E. coli F1FoATP synthase accommodates symmetry mismatch.
Resolution3.1 Å
Binding residue
(original residue number in PDB)		T156 E181
Binding residue
(residue number reindexed from 1)		T155 E180
Annotation score1
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.
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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