Structure of PDB 6oqt Chain A

Receptor sequence
>6oqtA (length=508) Species: 562 (Escherichia coli) [Search protein sequence]
NSTEISELIKQRIAQFNVVSEAHNEGTIVSVSDGVIRIHGLADCMQGEMI
SLPGNRYAIALNLERDSVGAVVMGPYADLAEGMKVKCTGRILEVPVGRGL
LGRVVNTLGAPIDGKGPLDHDGFSAVEAIAPGVIERQSVDQPVQTGYKAV
DSMIPIGRGQRELIIGDRQTGKTALAIDAIINQRDSGIKCIYVAIGQKAS
TISNVVRKLEEHGALANTIVVVATASESAALQYLAPYAGCAMGEYFRDRG
EDALIIYDDLSKQAVAYRQISLLLRRPPGREAFPGDVFYLHSRLLERAAR
VNAEYVEAFTKGEVKGKTGSLTALPIIETQAGDVSAFVPTNVISITDGQI
FLETNLFNAGIRPAVNPGISVSRVGGAAQTKIMKKLSGGIRTALAQYREL
AAFSQFASDLDDATRKQLDHGQKVTELLKQKQYAPMSVAQQSLVLFAAER
GYLADVELSKIGSFEAALLAYVDRDHAPLMQEINQTGGYNDEIEGKLKGI
LDSFKATQ
3D structure
PDB6oqt Cryo-EM structures provide insight into how E. coli F1FoATP synthase accommodates symmetry mismatch.
ChainA
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) K175 Q200 K201 R376
Catalytic site (residue number reindexed from 1) K172 Q197 K198 R373
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 ATP A Q172 T173 G174 K175 T176 A177 R365 Q435 Q169 T170 G171 K172 T173 A174 R362 Q432
Gene Ontology
Molecular Function
GO:0005515 protein binding
GO:0005524 ATP binding
GO:0032559 adenyl ribonucleotide binding
GO:0043531 ADP binding
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:6oqt, PDBe:6oqt, PDBj:6oqt
PDBsum6oqt
PubMed32457314
UniProtP0ABB0|ATPA_ECOLI ATP synthase subunit alpha (Gene Name=atpA)

[Back to BioLiP]