Structure of PDB 7p3w Chain C

Receptor sequence

>7p3wC (length=509) Species: 400667 (Acinetobacter baumannii ATCC 17978)

PSEISALIKQRIGDLDTSATAKNEGTIVMVSDGIVRIHGLADAMYGEMIE
FDGGLFGMALNLEQDSVGAVVLGNYLSLQEGQKARCTGRVLEVPVGPELL
GRVVDALGNPIDGKGPIDAKLTDAVEKVAPGVIWRQSVDQPVQTGYKSVD
TMIPVGRGQRELIIGDRQTGKTAMAIDAIIAQKNSGIKCVYVAIGQKQST
IANVVRKLEETGAMAYTTVVAAAAADPAAMQYLAPYSGCTMGEYFRDRGE
DALIIYDDLSKQAVAYRQISLLLRRPPGREAYPGDVFYLHSRLLERASRV
SAEYVEKFTNGAVTGKTGSLTALPIIETQAGDVSAFVPTNVISITDGQIF
LETSLFNAGIRPAVNAGISVSRVGGSAQTKIIKKLSGGIRTALAQYRELA
AFAQFASDLDEATRKQLEHGQRVTELMKQKQYAPYSIADQAVSVYASNEG
YMADVEVKKIVDFDAALIAYFRSEYAPLMKQIDETGDYNKDIEAAIKAGI
ESFKATQTY

3D structure

• PDB: 7p3w Structure of ATP synthase from ESKAPE pathogen Acinetobacter baumannii.
• Chain: C
• Resolution: 4.3 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	C	Q173 T174 G175 T177 R366 Q434 K435 Q436	Q168 T169 G170 T172 R361 Q429 K430 Q431

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:7p3w, PDBe:7p3w, PDBj:7p3w
• PDBsum: 7p3w
• PubMed: 35171679
• UniProt: A3M142|ATPA_ACIBT ATP synthase subunit alpha (Gene Name=atpA)