Target Pathogen

Overview

Basic information about this protein and its source genome.

Accession: PA5560
Assembly: Pseudomonas aeruginosa PAO1, complete genome
Gene: atpB PA5560
Status: annotated
Amino acids: 289
Structure source: AlphaFold

GO

GO:0005886 The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins. GO:0045259 A proton-transporting two-sector ATPase complex that catalyzes the phosphorylation of ADP to ATP during oxidative phosphorylation. The complex comprises a membrane sector (F0) that carries out proton transport and a cytoplasmic compartment sector (F1) that catalyzes ATP synthesis by a rotational mechanism; the extramembrane sector (containing 3 a and 3 b subunits) is connected via the d-subunit to the membrane sector by several smaller subunits. Within this complex, the g and e subunits and the 9-12 c subunits rotate by consecutive 120 degree angles and perform parts of ATP synthesis. This movement is driven by the hydrogen ion electrochemical potential gradient. GO:0046933 Enables the synthesis of ATP from ADP and phosphate by the transfer of protons from one side of a membrane to the other by a rotational mechanism driven by a gradient according to the reaction: ADP + phosphate + 5 H+(out) => ATP + H2O + 4 H+(in). GO:0042777 The chemical reactions and pathways resulting in the formation of ATP driven by transport of protons across a plasma membrane to generate an electrochemical gradient (proton-motive force). GO:0015986 The chemical reactions and pathways resulting in the formation of ATP driven by transport of protons across a membrane to generate an electrochemical gradient (proton-motive force). GO:0015078 Enables the transfer of a proton from one side of a membrane to the other.

Target profile

Computed evidence for target prioritization.

Human off-target: No hit
Gut microbiome off-target: hit
Essential (DEG): Y
Localization: CytoplasmicMembrane

Selected Druggability evidence

Selected Druggability is the FPocket score chosen for ranking using the curated structure priority. The 3D viewer may show a different loaded structure, so its visible pockets can differ.

FPocket 0.851

Structure –

Pocket –

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

7 GO

Gene Ontology (GO)

7

GO:0005886 The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.
GO:0045259 A proton-transporting two-sector ATPase complex that catalyzes the phosphorylation of ADP to ATP during oxidative phosphorylation. The complex comprises a membrane sector (F0) that carries out proton transport and a cytoplasmic compartment sector (F1) that catalyzes ATP synthesis by a rotational mechanism; the extramembrane sector (containing 3 a and 3 b subunits) is connected via the d-subunit to the membrane sector by several smaller subunits. Within this complex, the g and e subunits and the 9-12 c subunits rotate by consecutive 120 degree angles and perform parts of ATP synthesis. This movement is driven by the hydrogen ion electrochemical potential gradient.
GO:0046933 Enables the synthesis of ATP from ADP and phosphate by the transfer of protons from one side of a membrane to the other by a rotational mechanism driven by a gradient according to the reaction: ADP + phosphate + 5 H+(out) => ATP + H2O + 4 H+(in).
GO:0042777 The chemical reactions and pathways resulting in the formation of ATP driven by transport of protons across a plasma membrane to generate an electrochemical gradient (proton-motive force).
GO:0015986 The chemical reactions and pathways resulting in the formation of ATP driven by transport of protons across a membrane to generate an electrochemical gradient (proton-motive force).
GO:0015078 Enables the transfer of a proton from one side of a membrane to the other.
GO:0045263 OBSOLETE. All non-F1 subunits of a hydrogen-transporting ATP synthase, including integral and peripheral membrane proteins.

Sequence Features

Domain/signature hits from InterPro and related databases.

35 records

Show feature table

Start	End	DB	Term	Name
261	283	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
255	260	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
51	282	Pfam	PF00119	ATP synthase A chain
51	282	InterPro	IPR000568	ATP synthase, F0 complex, subunit A
154	171	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
41	283	NCBIfam	TIGR01131	F0F1 ATP synthase subunit A
41	283	InterPro	IPR000568	ATP synthase, F0 complex, subunit A
193	212	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
284	289	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
41	63	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
103	121	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
103	125	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
10	288	Hamap	MF_01393	ATP synthase subunit a [atpB].
10	288	InterPro	IPR000568	ATP synthase, F0 complex, subunit A
36	289	PANTHER	PTHR42823	ATP SYNTHASE SUBUNIT A, CHLOROPLASTIC
36	289	InterPro	IPR045082	ATP synthase, F0 complex, subunit A, bacterial/chloroplast
213	231	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
232	254	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
68	102	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
217	226	ProSitePatterns	PS00449	ATP synthase a subunit signature.
217	226	InterPro	IPR023011	ATP synthase, F0 complex, subunit A, active site
172	191	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
98	288	FunFam	G3DSA:1.20.120.220:FF:000002	ATP synthase subunit a
105	282	CDD	cd00310	ATP-synt_Fo_a_6
232	254	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
49	67	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
122	153	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
259	281	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
158	180	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
99	282	SUPERFAMILY	SSF81336	F1F0 ATP synthase subunit A
99	282	InterPro	IPR035908	ATP synthase, F0 complex, subunit A superfamily
192	212	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
98	288	Gene3D	G3DSA:1.20.120.220	ATP synthase, F0 complex, subunit A
98	288	InterPro	IPR035908	ATP synthase, F0 complex, subunit A superfamily
1	48	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.

3D Structure

Selected loaded structure. Experimental PDB entries may cover only a portion of the sequence; predicted models typically cover the full protein.

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Structural evidence

0 + 1

Experimental PDB entries and predicted models. Click Switch to display a different structure in the viewer.

Entry	Method	Resolution	Chain	Coverage	Links	Status
AlphaFold PA5560	AlphaFold	—	—	full sequence	—	Viewing

Pocket details FPocket · P2Rank — toggle visibility and zoom from here, or open full viewer

Pockets (FPOCKET)

Showing top-ranked FPocket candidates by druggability. Druggability is color-coded: high (0.7 or higher), medium (0.4 to 0.69), low (below 0.4).

FPOCKET	Sticks	Spheres	Surfaces	Druggability	Labels	Zoom	Positions
1				0.851
2				0.481

Ligand evidence

Ligands grouped by evidence source. PDB ligands keep the source crystal visible, and loaded crystals can be opened directly in the structure viewer.

1 records

Highest-confidence structural evidence: ligands co-crystallized with this exact protein. If the source PDB is loaded in TPW, use Open crystal to inspect it in the structure viewer.

No PDB structure with a co-crystallized ligand found for this exact protein.

Structural evidence inferred from similar proteins. The source crystal indicates where the ligand was observed; the UniProt column identifies the homologous protein carrying that ligand.

Ligand	Source crystal	UniProt (homolog)	MW · LogP · TPSA	Lipinski	PAINS	SMILES
BQ1	7JGC	A0R206	555.5 Da LogP 7.13 TPSA 45.6	2 viol.	✓ Clean	`CN(C)CC[C@@](c1cccc2c1cccc2)([C@H](c3ccccc3)c4c…`

Experimental bioactivity from ChEMBL measured directly on this protein. Score = pchembl (−log Ki/IC₅₀; higher = more potent).

No ChEMBL bioactivity data found for this exact protein.

Bioactivity inferred from similar proteins in ChEMBL. Score = pchembl (−log Ki/IC₅₀; higher = more potent).

No ChEMBL hits found through similar proteins.

Proposed virtual-screening candidates from ZINC. Score = Tanimoto similarity to a known binder (0–1; higher = more similar).

No virtual-screening candidates for this protein.

PDB and ChEMBL records on this protein are shown in full. ChEMBL records from similar proteins are capped at the top 100 per protein (by pchembl) and ZINC at the top 50 (Tanimoto ≥ 0.5). ADME columns are descriptor-based screening flags, not experimental toxicity results.

PA5560