Structure of PDB 7p3n Chain B

Receptor sequence

>7p3nB (length=514) Species: 400667 (Acinetobacter baumannii ATCC 17978)

MQQLNPSEISALIKQRIGDLDTSATAKNEGTIVMVSDGIVRIHGLADAMY
GEMIEFDGGLFGMALNLEQDSVGAVVLGNYLSLQEGQKARCTGRVLEVPV
GPELLGRVVDALGNPIDGKGPIDAKLTDAVEKVAPGVIWRQSVDQPVQTG
YKSVDTMIPVGRGQRELIIGDRQTGKTAMAIDAIIAQKNSGIKCVYVAIG
QKQSTIANVVRKLEETGAMAYTTVVAAAAADPAAMQYLAPYSGCTMGEYF
RDRGEDALIIYDDLSKQAVAYRQISLLLRRPPGREAYPGDVFYLHSRLLE
RASRVSAEYVEKFTNGAVTGKTGSLTALPIIETQAGDVSAFVPTNVISIT
DGQIFLETSLFNAGIRPAVNAGISVSRVGGSAQTKIIKKLSGGIRTALAQ
YRELAAFAQFASDLDEATRKQLEHGQRVTELMKQKQYAPYSIADQAVSVY
ASNEGYMADVEVKKIVDFDAALIAYFRSEYAPLMKQIDETGDYNKDIEAA
IKAGIESFKATQTY

3D structure

• PDB: 7p3n Structure of ATP synthase from ESKAPE pathogen Acinetobacter baumannii.
• Chain: B
• Resolution: 4.6 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	B	Q173 T174 G175 K176 A178 R366 Q436	Q173 T174 G175 K176 A178 R366 Q436

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:7p3n, PDBe:7p3n, PDBj:7p3n
• PDBsum: 7p3n
• PubMed: 35171679
• UniProt: A3M142|ATPA_ACIBT ATP synthase subunit alpha (Gene Name=atpA)