Structure of PDB 8dbv Chain D

Receptor sequence

>8dbvD (length=460) Species: 562 (Escherichia coli)

MATGKIVQVIGAVVDVEFPQDAVPRVYDALEVQNGNERLVLEVQQQLGGG
IVRTIAMGSSDGLRRGLDVKDLEHPIEVPVGKATLGRIMNVLGEPVDMKG
EIGEEERWAIHRAAPSYEELSNSQELLETGIKVIDLMAPFAKGGKVGLFG
GAGVGKTVNMMELIRNIAIEHSGYSVFAGVGERTREGNDFYHEMTDSNVI
DKVSLVYGQMNEPPGNRLRVALTGLTMAEKFRDEGRDVLLFVDNIYRYTL
AGTEVSALLGRMPSAVGYQPTLAEEMGVLQERITSTKTGSITSVQAVYVP
ADDLTDPSPATTFAHLDATVVLSRQIASLGIYPAVDPLDSTSRQLDPLVV
GQEHYDTARGVQSILQRYQELKDIIAILGMDELSEEDKLVVARARKIQRF
LSQPFFVAEVFTGSPGKYVSLKDTIRGFKGIMEGEYDHLPEQAFYMVGSI
EEAVEKAKKL

3D structure

• PDB: 8dbv Changes within the central stalk of E. coli F 1 F o ATP synthase observed after addition of ATP.
• Chain: D
• Resolution: 3.7 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	ADP	D	G152 V153 G154 K155 T156 Y331 A407	G153 V154 G155 K156 T157 Y332 A408

Gene Ontology

Molecular Function

• GO:0005515 protein binding
• 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:0042777 proton motive force-driven plasma membrane ATP synthesis
• GO:0046034 ATP metabolic process
• GO:1902600 proton transmembrane transport

Cellular Component

• GO:0005886 plasma membrane
• GO:0016020 membrane
• GO:0045259 proton-transporting ATP synthase complex
• GO:0045261 proton-transporting ATP synthase complex, catalytic core F(1)

External links

• PDB: RCSB:8dbv, PDBe:8dbv, PDBj:8dbv
• PDBsum: 8dbv
• PubMed: 36631659
• UniProt: P0ABB4|ATPB_ECOLI ATP synthase subunit beta (Gene Name=atpD)