Target Pathogen

Overview

Basic information about this protein and its source genome.

Accession: PA1552
Assembly: Pseudomonas aeruginosa PAO1, complete genome
Gene: PA1552 ccoP1
Status: annotated
Amino acids: 318
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:0004129 Catalysis of the reaction: 4 Fe(II)-[cytochrome c] + O2 + 8 H+(in) = 4 Fe(III)-[cytochrome c] + 2 H2O + 4 H+(out). GO:0020037 Binding to a heme, a compound composed of iron complexed in a porphyrin (tetrapyrrole) ring. GO:0005506 Binding to an iron (Fe) ion. GO:0016491 Catalysis of an oxidation-reduction (redox) reaction, a reversible chemical reaction in which the oxidation state of an atom or atoms within a molecule is altered. One substrate acts as a hydrogen or electron donor and becomes oxidized, while the other acts as hydrogen or electron acceptor and becomes reduced. GO:0006119 The phosphorylation of ADP to ATP that accompanies the oxidation of a metabolite through the operation of the respiratory chain. Oxidation of compounds establishes a proton gradient across the membrane, providing the energy for ATP synthesis.

Target profile

Computed evidence for target prioritization.

Human off-target: No hit
Gut microbiome off-target: hit
Essential (DEG): N
Localization: Unknown

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 0.767

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:0004129 Catalysis of the reaction: 4 Fe(II)-[cytochrome c] + O2 + 8 H+(in) = 4 Fe(III)-[cytochrome c] + 2 H2O + 4 H+(out).
GO:0020037 Binding to a heme, a compound composed of iron complexed in a porphyrin (tetrapyrrole) ring.
GO:0005506 Binding to an iron (Fe) ion.
GO:0016491 Catalysis of an oxidation-reduction (redox) reaction, a reversible chemical reaction in which the oxidation state of an atom or atoms within a molecule is altered. One substrate acts as a hydrogen or electron donor and becomes oxidized, while the other acts as hydrogen or electron acceptor and becomes reduced.
GO:0006119 The phosphorylation of ADP to ATP that accompanies the oxidation of a metabolite through the operation of the respiratory chain. Oxidation of compounds establishes a proton gradient across the membrane, providing the energy for ATP synthesis.
GO:0009055 A molecular function representing the directed movement of electrons from one molecular entity to another, typically mediated by electron carriers or acceptors, resulting in the transfer of energy and/or the reduction-oxidation (redox) transformation of chemical species. This activity is fundamental to various biological processes, including cellular respiration and photosynthesis, as well as numerous enzymatic reactions involved in metabolic pathways.

Sequence Features

Domain/signature hits from InterPro and related databases.

38 records

Show feature table

Start	End	DB	Term	Name
26	56	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
77	318	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
33	314	NCBIfam	TIGR00782	cytochrome-c oxidase, cbb3-type subunit III
33	314	InterPro	IPR004678	Cytochrome c oxidase cbb3-type, subunit III
139	218	ProSiteProfiles	PS51007	Cytochrome c family profile.
139	218	InterPro	IPR009056	Cytochrome c-like domain
219	318	Gene3D	G3DSA:1.10.760.10	-
219	318	InterPro	IPR036909	Cytochrome c-like domain superfamily
38	311	PANTHER	PTHR33751	CBB3-TYPE CYTOCHROME C OXIDASE SUBUNIT FIXP
1	314	PIRSF	PIRSF000006	Cbb3-Cox_fixP
1	314	InterPro	IPR004678	Cytochrome c oxidase cbb3-type, subunit III
221	317	FunFam	G3DSA:1.10.760.10:FF:000015	Cbb3-type cytochrome c oxidase subunit
57	79	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
57	76	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
7	25	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
4	26	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
1	93	Gene3D	G3DSA:6.10.280.130	-
1	93	InterPro	IPR038414	Cbb3-type cytochrome c oxidase subunit CcoP, N-terminal domain superfamily
104	220	FunFam	G3DSA:1.10.760.10:FF:000013	Cbb3-type cytochrome c oxidase subunit
1	6	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
229	307	Pfam	PF13442	Cytochrome C oxidase, cbb3-type, subunit III
229	307	InterPro	IPR009056	Cytochrome c-like domain
140	214	Pfam	PF13442	Cytochrome C oxidase, cbb3-type, subunit III
140	214	InterPro	IPR009056	Cytochrome c-like domain
192	214	PRINTS	PR00605	Class IC cytochrome C signature
192	214	InterPro	IPR008168	Cytochrome c, class IC
150	161	PRINTS	PR00605	Class IC cytochrome C signature
150	161	InterPro	IPR008168	Cytochrome c, class IC
37	83	Pfam	PF14715	N-terminal domain of cytochrome oxidase-cbb3, FixP
37	83	InterPro	IPR032858	Cbb3-type cytochrome c oxidase subunit CcoP, N-terminal
55	219	SUPERFAMILY	SSF46626	Cytochrome c
55	219	InterPro	IPR036909	Cytochrome c-like domain superfamily
225	313	SUPERFAMILY	SSF46626	Cytochrome c
225	313	InterPro	IPR036909	Cytochrome c-like domain superfamily
105	218	Gene3D	G3DSA:1.10.760.10	-
105	218	InterPro	IPR036909	Cytochrome c-like domain superfamily
229	311	ProSiteProfiles	PS51007	Cytochrome c family profile.
229	311	InterPro	IPR009056	Cytochrome c-like domain

3D Structure

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

Loading 3D structure...

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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 PA1552	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
2				0.767
1				0.619

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.

2 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
FC6	3MK7	D9IA45	212.0 Da LogP 0.10 TPSA 142.7	✓ Ro5	✓ Clean	`C(#N)[Fe](C#N)(C#N)(C#N)(C#N)C#N`
PEO	3MK7	D9IA45	34.0 Da LogP 0.02 TPSA 40.5	✓ Ro5	✓ Clean	`OO`

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.

PA1552