Protein profile

PA2065

copper resistance protein A

Genome: NC_002516.2

Gene: pcoA PA2065 Structure source: AlphaFold UniProt Q9I250

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Amino acids 632

Annotations 3

Features 41

PDB binders 5

Druggability 0.858

Overview

Basic information about this protein and its source genome.

Accession: PA2065
Assembly: Pseudomonas aeruginosa PAO1, complete genome
Gene: pcoA PA2065
Status: annotated
Amino acids: 632
Structure source: AlphaFold

GO:0042597 The region between the inner (cytoplasmic) and outer membrane (Gram-negative Bacteria) or cytoplasmic membrane and cell wall (Fungi and Gram-positive Bacteria). GO:0005507 Binding to a copper (Cu) 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.

Target profile

Computed evidence for target prioritization.

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

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 0.858

Structure –

Pocket –

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

3 GO

Gene Ontology (GO)

GO:0042597 The region between the inner (cytoplasmic) and outer membrane (Gram-negative Bacteria) or cytoplasmic membrane and cell wall (Fungi and Gram-positive Bacteria).
GO:0005507 Binding to a copper (Cu) 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.

Sequence Features

Domain/signature hits from InterPro and related databases.

41 records

Show feature table

Start	End	DB	Term	Name
1	12	Phobius	SIGNAL_PEPTIDE_N_REGION	N-terminal region of a signal peptide.
232	345	CDD	cd13874	CuRO_2_CopA
232	345	InterPro	IPR034282	Copper resistance protein CopA, second cupredoxin domain
165	380	SUPERFAMILY	SSF49503	Cupredoxins
165	380	InterPro	IPR008972	Cupredoxin
52	162	Pfam	PF07732	Multicopper oxidase
52	162	InterPro	IPR011707	Multicopper oxidase, N-terminal
500	631	Gene3D	G3DSA:2.60.40.420	-
500	631	InterPro	IPR008972	Cupredoxin
46	159	CDD	cd13848	CuRO_1_CopA
46	159	InterPro	IPR034284	Copper resistance protein, first cupredoxin domain
477	626	SUPERFAMILY	SSF49503	Cupredoxins
477	626	InterPro	IPR008972	Cupredoxin
26	33	Phobius	SIGNAL_PEPTIDE_C_REGION	C-terminal region of a signal peptide.
1	31	ProSiteProfiles	PS51318	Twin arginine translocation (Tat) signal profile.
1	31	InterPro	IPR006311	Twin-arginine translocation pathway, signal sequence
513	626	CDD	cd13896	CuRO_3_CopA
513	626	InterPro	IPR034279	Copper resistance protein, third cupredoxin domain
34	632	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
609	620	ProSitePatterns	PS00080	Multicopper oxidases signature 2.
609	620	InterPro	IPR002355	Multicopper oxidase, copper-binding site
516	629	Pfam	PF07731	Multicopper oxidase
516	629	InterPro	IPR011706	Multicopper oxidase, C-terminal
13	25	Phobius	SIGNAL_PEPTIDE_H_REGION	Hydrophobic region of a signal peptide.
64	621	PANTHER	PTHR11709	MULTI-COPPER OXIDASE
64	621	InterPro	IPR045087	Multicopper oxidase
4	31	NCBIfam	TIGR01409	twin-arginine translocation signal domain
4	31	InterPro	IPR019546	Twin-arginine translocation pathway, signal sequence, bacterial/archaeal
166	369	Gene3D	G3DSA:2.60.40.420	-
166	369	InterPro	IPR008972	Cupredoxin
1	33	Phobius	SIGNAL_PEPTIDE	Signal peptide region
46	184	SUPERFAMILY	SSF49503	Cupredoxins
46	184	InterPro	IPR008972	Cupredoxin
38	160	Gene3D	G3DSA:2.60.40.420	-
38	160	InterPro	IPR008972	Cupredoxin
3	409	NCBIfam	TIGR01480	copper resistance system multicopper oxidase
3	409	InterPro	IPR006376	Copper-resistance protein CopA
604	624	ProSitePatterns	PS00079	Multicopper oxidases signature 1.
604	624	InterPro	IPR033138	Multicopper oxidases, conserved site
171	346	Pfam	PF00394	Multicopper oxidase
171	346	InterPro	IPR001117	Multicopper oxidase, second cupredoxin domain

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 PA2065	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				0.858
1				0.361

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.

55 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
C2O	1KV7	P36649	143.1 Da LogP -0.07 TPSA 9.2	✓ Ro5	✓ Clean	`O([Cu])[Cu]`
CIY	6KLJ	Q2PAJ1	178.2 Da LogP 1.61 TPSA 46.5	✓ Ro5	✓ Clean	`COc1cc(ccc1O)/C=C/C=O`
D2M	3FU7	Q70KY3	306.3 Da LogP 3.22 TPSA 66.4	✓ Ro5	✓ Clean	`COc1cccc(c1Oc2cc(c(c(c2)OC)O)OC)OC`
O	3OD3	P36649	18.0 Da LogP -0.82 TPSA 31.5	✓ Ro5	✓ Clean	`O`
OXY	3ZX1	A0A0H3PBA4	32.0 Da LogP 0.07 TPSA 34.1	✓ Ro5	✓ Clean	`O=O`

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).

Ligand	Tanimoto	MW · LogP · TPSA	Lipinski	PAINS	SMILES
ZINC1532902	0.700	206.2 Da LogP -0.86 TPSA 132.1	✓ Ro5	✓ Clean	`O=C(O)CC[C@@](O)(CC(=O)O)C(=O)O`
ZINC2018106	0.700	206.2 Da LogP -0.86 TPSA 132.1	✓ Ro5	✓ Clean	`O=C(O)CC[C@](O)(CC(=O)O)C(=O)O`
ZINC3593496	0.652	206.2 Da LogP -1.16 TPSA 121.1	✓ Ro5	✓ Clean	`COC(=O)C[C@@](O)(CC(=O)O)C(=O)O`
ZINC3593497	0.652	206.2 Da LogP -1.16 TPSA 121.1	✓ Ro5	✓ Clean	`COC(=O)C[C@](O)(CC(=O)O)C(=O)O`
ZINC13541228	0.647	258.3 Da LogP 2.98 TPSA 69.9	✓ Ro5	✓ Clean	`COc1cc(/C=C/c2cc(O)cc(O)c2)ccc1O`
ZINC2053487767	0.647	258.3 Da LogP 2.98 TPSA 69.9	✓ Ro5	✓ Clean	`COc1cc(C=Cc2cc(O)cc(O)c2)ccc1O`
ZINC120595	0.629	226.3 Da LogP 3.57 TPSA 29.5	✓ Ro5	✓ Clean	`COc1cc(/C=C/c2ccccc2)ccc1O`
ZINC5081027	0.629	226.3 Da LogP 3.57 TPSA 29.5	✓ Ro5	✓ Clean	`COc1cc(/C=C\c2ccccc2)ccc1O`
ZINC14686440	0.625	436.4 Da LogP -2.64 TPSA 247.9	1 viol.	✓ Clean	`O=C(O)C[C@](O)(CC(=O)NCCCCNC(=O)C[C@@](O)(CC(=O…`
ZINC14686442	0.625	436.4 Da LogP -2.64 TPSA 247.9	1 viol.	✓ Clean	`O=C(O)C[C@@](O)(CC(=O)NCCCCNC(=O)C[C@](O)(CC(=O…`
ZINC14686444	0.625	436.4 Da LogP -2.64 TPSA 247.9	1 viol.	✓ Clean	`O=C(O)C[C@@](O)(CC(=O)NCCCCNC(=O)C[C@@](O)(CC(=…`
ZINC12358996	0.622	208.2 Da LogP 1.59 TPSA 55.8	✓ Ro5	✓ Clean	`COC(=O)/C=C\c1ccc(O)c(OC)c1`
ZINC1621053	0.622	208.2 Da LogP 1.59 TPSA 55.8	✓ Ro5	✓ Clean	`COC(=O)/C=C/c1ccc(O)c(OC)c1`
ZINC17255287	0.622	368.4 Da LogP 3.37 TPSA 93.1	✓ Ro5	✓ Clean	`COc1cc(/C=C\C(=O)CC(=O)/C=C/c2ccc(O)c(OC)c2)ccc…`
ZINC1857743026	0.622	368.4 Da LogP 3.37 TPSA 93.1	✓ Ro5	✓ Clean	`COc1cc(C=CC(=O)CC(=O)C=Cc2ccc(O)c(OC)c2)ccc1O`
ZINC1903846672	0.622	208.2 Da LogP 1.59 TPSA 55.8	✓ Ro5	✓ Clean	`COC(=O)C=Cc1ccc(O)c(OC)c1`
ZINC31261437	0.622	368.4 Da LogP 3.37 TPSA 93.1	✓ Ro5	✓ Clean	`COc1cc(/C=C\C(=O)CC(=O)/C=C\c2ccc(O)c(OC)c2)ccc…`
ZINC899824	0.622	368.4 Da LogP 3.37 TPSA 93.1	✓ Ro5	✓ Clean	`COc1cc(/C=C/C(=O)CC(=O)/C=C/c2ccc(O)c(OC)c2)ccc…`
ZINC1591265	0.611	286.3 Da LogP 3.59 TPSA 47.9	✓ Ro5	✓ Clean	`COc1cc(/C=C/c2ccc(O)c(OC)c2)cc(OC)c1`
ZINC5663472	0.611	286.3 Da LogP 3.59 TPSA 47.9	✓ Ro5	✓ Clean	`COc1cc(/C=C\c2ccc(O)c(OC)c2)cc(OC)c1`
ZINC1387051	0.595	234.3 Da LogP 1.96 TPSA 63.6	✓ Ro5	✓ Clean	`COc1cc(C=C(C(C)=O)C(C)=O)ccc1O`
ZINC19943836	0.595	227.3 Da LogP 2.97 TPSA 42.4	✓ Ro5	✓ Clean	`COc1cc(/C=C/c2ccncc2)ccc1O`
ZINC33956762	0.590	234.3 Da LogP 3.03 TPSA 46.5	✓ Ro5	✓ Clean	`COc1cc(/C=C/C(=O)C(C)(C)C)ccc1O`
ZINC1603409	0.579	242.3 Da LogP 2.40 TPSA 33.3	✓ Ro5	✓ Clean	`COc1cc(/C=C/c2cc[n+](C)cc2)ccc1O`
ZINC13398039	0.577	234.2 Da LogP -0.38 TPSA 121.1	✓ Ro5	✓ Clean	`CC(C)OC(=O)C[C@](O)(CC(=O)O)C(=O)O`
ZINC2528012	0.577	234.2 Da LogP -0.38 TPSA 121.1	✓ Ro5	✓ Clean	`CC(C)OC(=O)C[C@@](O)(CC(=O)O)C(=O)O`
ZINC100067274	0.575	368.4 Da LogP 3.85 TPSA 96.2	✓ Ro5	✓ Clean	`COc1cc(/C=C/C(=O)/C=C(O)/C=C/c2ccc(O)c(OC)c2)cc…`
ZINC104896565	0.575	368.4 Da LogP 3.85 TPSA 96.2	✓ Ro5	✓ Clean	`COc1cc(/C=C\C(=O)/C=C(O)/C=C/c2ccc(O)c(OC)c2)cc…`
ZINC184566	0.575	271.3 Da LogP 3.48 TPSA 72.6	✓ Ro5	✓ Clean	`COc1cc(/C=C/c2ccc([N+](=O)[O-])cc2)ccc1O`
ZINC2356428976	0.575	354.4 Da LogP 3.07 TPSA 104.1	✓ Ro5	Alert	`COc1cc(C=CC(=O)CC(=O)C=Cc2ccc(O)c(O)c2)ccc1O`
ZINC34581303	0.575	234.3 Da LogP 1.96 TPSA 63.6	✓ Ro5	✓ Clean	`COc1cc(/C=C/C(=O)CC(C)=O)ccc1O`
ZINC39309887	0.575	222.2 Da LogP 1.98 TPSA 55.8	✓ Ro5	✓ Clean	`COc1cc(/C=C/COC(C)=O)ccc1O`
ZINC5543044	0.575	354.4 Da LogP 3.07 TPSA 104.1	✓ Ro5	Alert	`COc1cc(/C=C/C(=O)CC(=O)/C=C/c2ccc(O)c(O)c2)ccc1O`
ZINC8816263	0.575	227.3 Da LogP 2.97 TPSA 42.4	✓ Ro5	✓ Clean	`COc1cc(/C=C/c2ccccn2)ccc1O`
ZINC100289944	0.564	226.3 Da LogP 1.76 TPSA 66.8	✓ Ro5	✓ Clean	`COc1cc(/C=C(/S)C(=O)O)ccc1O`
ZINC1911962839	0.564	226.3 Da LogP 1.76 TPSA 66.8	✓ Ro5	✓ Clean	`COc1cc(C=C(S)C(=O)O)ccc1O`
ZINC47621	0.564	226.3 Da LogP 1.76 TPSA 66.8	✓ Ro5	✓ Clean	`COc1cc(/C=C(\S)C(=O)O)ccc1O`
ZINC14488535	0.561	222.2 Da LogP 1.98 TPSA 55.8	✓ Ro5	✓ Clean	`CCOC(=O)/C=C\c1ccc(O)c(OC)c1`
ZINC160496	0.561	222.2 Da LogP 1.98 TPSA 55.8	✓ Ro5	✓ Clean	`CCOC(=O)/C=C/c1ccc(O)c(OC)c1`
ZINC1857524314	0.561	222.2 Da LogP 1.98 TPSA 55.8	✓ Ro5	✓ Clean	`CCOC(=O)C=Cc1ccc(O)c(OC)c1`
ZINC1903857764	0.561	338.4 Da LogP 3.36 TPSA 83.8	✓ Ro5	✓ Clean	`COc1cc(C=CC(=O)CC(=O)C=Cc2ccc(O)cc2)ccc1O`
ZINC2001304	0.561	236.3 Da LogP 2.37 TPSA 55.8	✓ Ro5	✓ Clean	`COc1cc(/C=C/C(=O)OC(C)C)ccc1O`
ZINC2042437156	0.561	236.3 Da LogP 2.37 TPSA 55.8	✓ Ro5	✓ Clean	`COc1cc(C=CC(=O)OC(C)C)ccc1O`
ZINC307223328	0.561	276.1 Da LogP 3.05 TPSA 47.9	✓ Ro5	✓ Clean	`COc1cc(/C=C/B2OC(C)(C)C(C)(C)O2)ccc1O`
ZINC31430204	0.561	338.4 Da LogP 3.36 TPSA 83.8	✓ Ro5	✓ Clean	`COc1cc(/C=C\C(=O)CC(=O)/C=C/c2ccc(O)cc2)ccc1O`
ZINC3921800	0.561	254.3 Da LogP 3.30 TPSA 46.5	✓ Ro5	✓ Clean	`COc1cc(/C=C/C(=O)c2ccccc2)ccc1O`
ZINC4252576	0.561	270.3 Da LogP 3.00 TPSA 66.8	✓ Ro5	✓ Clean	`COc1cc(/C=C/C(=O)c2ccccc2O)ccc1O`
ZINC457482	0.561	330.4 Da LogP 4.80 TPSA 46.5	✓ Ro5	✓ Clean	`COc1cc(/C=C/c2ccc(C(=O)c3ccccc3)cc2)ccc1O`
ZINC4934330	0.561	270.3 Da LogP 3.00 TPSA 66.8	✓ Ro5	✓ Clean	`COc1cc(/C=C\C(=O)c2ccccc2O)ccc1O`
ZINC5115722	0.561	338.4 Da LogP 3.36 TPSA 83.8	✓ Ro5	✓ Clean	`COc1cc(/C=C/C(=O)CC(=O)/C=C/c2ccc(O)cc2)ccc1O`

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.