Structure of PDB 7l1q Chain B

Receptor sequence

>7l1qB (length=475) Species: 2334 (Bacillus sp. PS3)

DVGTVIQVGDGIARAHGLDNVMSGELVEFANGVMGMALNLEENNVGIVIL
GPYTGIKEGDEVRRTGRIMEVPVGEALIGRVVNPLGQPVDGLGPVETTET
RPIESRAPGVMDRRSVHEPLQTGIKAIDALVPIGRGQRELIIGDRQTGKT
SVAIDTIINQKDQNMISIYVAIGQKESTVRTVVETLRKHGALDYTIVVTA
SASQPAPLLFLAPYAGVAMGEYFMYKGKHVLVVYDDLSKQAAAYRELSLL
LRRPPGREAYPGDIFYLHSRLLERAAKLSDAKGGGSLTALPFVETQAGDI
SAYIPTNVISITDGQIFLQSDLFFSGVRPAINAGLSVSRVGGAAQIKAMK
KVAGTLRLDLAAYRELEAFAQFGSDLDKATQAKLARGARTVEVLKQDLHQ
PIPVEKQVLIIYALTRGFLDDIPVEDVRRFEKEFYLFLDQNGQHLLEHIR
TTKDLPNEDDLNKAIEAFKKTFVVS

3D structure

• PDB: 7l1q The six steps of the complete F 1 -ATPase rotary catalytic cycle.
• Chain: B
• Resolution: 3.4 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	B	Q172 T173 G174 K175 T176 S177 L424	Q146 T147 G148 K149 T150 S151 L398
BS02	ATP	B	V363 R365	V337 R339

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:7l1q, PDBe:7l1q, PDBj:7l1q
• PDBsum: 7l1q
• PubMed: 34344897
• UniProt: A0A0M3VGF9