Structure of PDB 7p3n Chain E

Receptor sequence
>7p3nE (length=463) Species: 400667 (Acinetobacter baumannii ATCC 17978) [Search protein sequence]
SSGRIIQIIGAVIDVEFERTSVPKIYDALQVDGTETTLEVQQQLGDGVVR
TIAMGSTEGLKRGLTVTSTNAPISVPVGTATLGRIMDVLGRPIDEAGPVA
TEERLPIHRQAPSYAEQAASTDLLETGIKVIDLLCPFAKGGKVGLFGGAG
VGKTVNMMELINNIAKAHSGLSVFAGVGERTREGNDFYHEMKDSNVLDKV
AMVYGQMNEPPGNRLRVALTGLTMAEYFRDEKDENGKGRDVLLFVDNIYR
YTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERITSTKSGSITSIQAV
YVPADDLTDPSPATTFAHLDATVVLSRDIASSGIYPAIDPLDSTSRQLDP
LVVGQEHYEIARAVQNVLQRYKELKDIIAILGMDELAEEDKLVVYRARKI
QRFFSQPFHVAEVFTGAPGKLVPLKETIRGFKGLLAGEYDHIPEQAFYMV
GGIDEVIAKAEKL
3D structure
PDB7p3n Structure of ATP synthase from ESKAPE pathogen Acinetobacter baumannii.
ChainE
Resolution4.6 Å
3D
structure
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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 ADP E G151 G153 K154 T155 V156 Y336 F415 G150 G152 K153 T154 V155 Y335 F414
Gene Ontology
Molecular Function
GO:0005524 ATP binding
GO:0016887 ATP hydrolysis activity
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)

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Biological Process
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Cellular Component
External links
PDB RCSB:7p3n, PDBe:7p3n, PDBj:7p3n
PDBsum7p3n
PubMed35171679
UniProtA3M144|ATPB_ACIBT ATP synthase subunit beta (Gene Name=atpD)

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