Structure of PDB 7l1s Chain A

Receptor sequence

>7l1sA (length=474) Species: 2334 (Bacillus sp. PS3)

SDVGTVIQVGDGIARAHGLDNVMSGELVEFANGVMGMALNLEENNVGIVI
LGPYTGIKEGDEVRRTGRIMEVPVGEALIGRVVNPLGQPVDGLGPVETTE
TRPIESRAPGVMDRRSVHEPLQTGIKAIDALVPIGRGQRELIIGDRQTGK
TSVAIDTIINQKDQNMISIYVAIGQKESTVRTVVETLRKHGALDYTIVVT
ASASQPAPLLFLAPYAGVAMGEYFMYKGKHVLVVYDDLSKQAAAYRELSL
LLRRPPGREAYPGDIFYLHSRLLERAAKLSDAKGGGSLTALPFVETQAGD
ISAYIPTNVISITDGQIFLQSDLFFSGVRPAINAGLSVSRVGGAAQIKAM
KKVAGTLRLDLAAYRELEAFAQFGSDLDKATQAKLARGARTVEVLKQDLH
QPIPVEKQVLIIYALTRGFLDDIPVEDVRRFEKEFYLFLDQNGQHLLEHI
RTTKDLPNEDDLNKAIEAFKKTFV

3D structure

• PDB: 7l1s The six steps of the complete F 1 -ATPase rotary catalytic cycle.
• Chain: A
• Resolution: 3.6 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	ATP	A	R171 Q172 T173 G174 K175 T176 S177 F349	R146 Q147 T148 G149 K150 T151 S152 F324

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:7l1s, PDBe:7l1s, PDBj:7l1s
• PDBsum: 7l1s
• PubMed: 34344897
• UniProt: A0A0M3VGF9