Structure of PDB 5t4q Chain B

Receptor sequence
>5t4qB (length=510) Species: 562 (Escherichia coli) [Search protein sequence]
QLNSTEISELIKQRIAQFNVVSEAHNEGTIVSVSDGVIRIHGLADAMQGE
MISLPGNRYAIALNLERDSVGAVVMGPYADLAEGMKVKATGRILEVPVGR
GLLGRVVNTLGAPIDGKGPLDHDGFSAVEAIAPGVIERQSVDQPVQTGYK
AVDSMIPIGRGQRELIIGDRQTGKTALAIDAIINQRDSGIKAIYVAIGQK
ASTISNVVRKLEEHGALANTIVVVATASESAALQYLAPYAGAAMGEYFRD
RGEDALIIYDDLSKQAVAYRQISLLLRRPPGREAFPGDVFYLHSRLLERA
ARVNAEYVEAFTKGEVKGKTGSLTALPIIETQAGDVSAFVPTNVISITDG
QIFLETNLFNAGIRPAVNPGISVSRVGGAAQTKIMKKLSGGIRTALAQYR
ELAAFSQFASDLDDATRNQLDHGQKVTELLKQKQYAPMSVAQQSLVLFAA
ERGYLADVELSKIGSFEAALLAYVDRDHAPLMQEINQTGGYNDEIEGKLK
GILDSFKATQ
3D structure
PDB5t4q Cryo-EM structures of the autoinhibitedE. coliATP synthase in three rotational states.
ChainB
Resolution8.53 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K175 Q200 K201 R376
Catalytic site (residue number reindexed from 1) K174 Q199 K200 R375
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 B R171 Q172 T173 K175 T176 L178 Q435 R170 Q171 T172 K174 T175 L177 Q434
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)

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Cellular Component
External links
PDB RCSB:5t4q, PDBe:5t4q, PDBj:5t4q
PDBsum5t4q
PubMed28001127
UniProtP0ABB0|ATPA_ECOLI ATP synthase subunit alpha (Gene Name=atpA)

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