Structure of PDB 7xkr Chain F

Receptor sequence

>7xkrF (length=471) Species: 2334 (Bacillus sp. PS3)

MTRGRVIQVMGPVVDVKFENGHLPAIYNALKIQHKARNENEVDIDLTLEV
ALHLGDDTVRTIAMASTDGLIRGMEVIDTGAPISVPVGEVTLGRVFNVLG
EPIDLEGDIPADARRDPIHRPAPKFEELATEVEILETGIKVVDLLAPYIK
GGKIGLFGGAGVGKTVLIQELIHNIAQEHGGISVFAGVGERTREGNDLYH
EMKDSGVISKTAMVFGQMNEPPGARMRVALTGLTMAEYFRDEQGQDVLLF
IDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQERITSTAKGSI
TSIQAIYVPADDYTDPAPATTFSHLDATTNLERKLAEMGIYPAVDPLAST
SRALAPEIVGEEHYQVARKVQQTLQRYKELQDIIAILGMDELSDEDKLVV
HRARRIQFFLSQNFHVAEQFTGQPGSYVPVKETVRGFKEILEGKYDHLPE
DAFRLVGRIEEVVEKAKAMGV

3D structure

• PDB: 7xkr Structural basis of unisite catalysis of bacterial F 0 F 1 -ATPase.
• Chain: F
• Resolution: 2.6 Å

Enzymatic activity

• 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	G161 V162 G163 K164 T165 V166 Y341	G161 V162 G163 K164 T165 V166 Y341

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:0046034 ATP metabolic process
• GO:1902600 proton transmembrane transport

Cellular Component

• GO:0005886 plasma membrane
• GO:0045259 proton-transporting ATP synthase complex
• GO:0045261 proton-transporting ATP synthase complex, catalytic core F(1)

External links

• PDB: RCSB:7xkr, PDBe:7xkr, PDBj:7xkr
• PDBsum: 7xkr
• PubMed: 36741449
• UniProt: P07677|ATPB_BACP3 ATP synthase subunit beta (Gene Name=atpD)