Structure of PDB 5t4o Chain F

Receptor sequence
>5t4oF (length=466) Species: 562 (Escherichia coli) [Search protein sequence]
HHHHHGMATGKIVQVIGAVVDVEFPQDAVPRVYDALEVQNGNERLVLEVQ
QQLGGGIVRTIAMGSSDGLRRGLDVKDLEHPIEVPVGKATLGRIMNVLGE
PVDMKGEIGEEERWAIHRAAPSYEELSNSQELLETGIKVIDLMAPFAKGG
KVGLFGGAGVGKTVNMMELIRNIAIEHSGYSVFAGVGERTREGNDFYHEM
TDSNVIDKVSLVYGQMNEPPGNRLRVALTGLTMAEKFRDEGRDVLLFVDN
IYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERITSTKTGSITSV
QAVYVPADDLTDPSPATTFAHLDATVVLSRQIASLGIYPAVDPLDSTSRQ
LDPLVVGQEHYDTARGVQSILQRYQELKDIIAILGMDELSEEDKLVVARA
RKIQRFLSQPFFVAEVFTGSPGKYVSLKDTIRGFKGIMEGEYDHLPEQAF
YMVGSIEEAVEKAKKL
3D structure
PDB5t4o Cryo-EM structures of the autoinhibitedE. coliATP synthase in three rotational states.
ChainF
Resolution6.9 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) K162 E188 R189 R349
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 A151 G152 V153 G154 K155 T156 V157 Y331 A158 G159 V160 G161 K162 T163 V164 Y338
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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Cellular Component
External links
PDB RCSB:5t4o, PDBe:5t4o, PDBj:5t4o
PDBsum5t4o
PubMed28001127
UniProtP0ABB4|ATPB_ECOLI ATP synthase subunit beta (Gene Name=atpD)

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