Structure of PDB 7xkq Chain A

Receptor sequence

>7xkqA (length=478) Species: 2334 (Bacillus sp. PS3)

QVSDVGTVIQVGDGIARAHGLDNVMSGELVEFANGVMGMALNLEENNVGI
VILGPYTGIKEGDEVRRTGRIMEVPVGEALIGRVVNPLGQPVDGLGPVET
TETRPIESPAPGVMDRRSVHEPLQTGIKAIDALVPIGRGQRELIIGDRQT
GKTSVAIDTIINQKDQNMISIYVAIGQKESTVRTVVETLRKHGALDYTIV
VTASASQPAPLLFLAPYAGVAMGEYFMYKGKHVLVVYDDLSKQAAAYREL
SLLLRRPPGREAYPGDIFYLHSRLLERAAKLSDAKGGGSLTALPFVETQA
GDISAYIPTNVISITDGQIFLQSDLFFSGVRPAINAGLSVSRVGGAAQIK
AMKKVAGTLRLDLAAYRELEAFAQFGSDLDKATQAKLARGARTVEVLKQD
LHQPIPVEKQVLIIYALTRGFLDDIPVEDVRRFEKEFYLFLDQNGQHLLE
HIRTTKDLPNEDDLNKAIEAFKKTFVVS

3D structure

• PDB: 7xkq Structural basis of unisite catalysis of bacterial F 0 F 1 -ATPase.
• Chain: A
• Resolution: 3.3 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	ATP	A	Q172 G174 K175 T176 S177 F349 R354 L424	Q149 G151 K152 T153 S154 F326 R331 L401

Gene Ontology

Molecular Function

• 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: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:7xkq, PDBe:7xkq, PDBj:7xkq
• PDBsum: 7xkq
• PubMed: 36741449
• UniProt: A0A0M3VGF9