Protein profile

PA0023

oxygen-dependent quinone oxidoreductase

Genome: NC_002516.2

Gene: qor PA0023 Structure source: AlphaFold UniProt P43903

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Amino acids 325

Annotations 7

Features 18

PDB binders 8

Druggability 0.755

Overview

Basic information about this protein and its source genome.

Accession: PA0023
Assembly: Pseudomonas aeruginosa PAO1, complete genome
Gene: qor PA0023
Status: annotated
Amino acids: 325
Structure source: AlphaFold

1.6.5.5

GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. GO:0035925 Binding to a region containing frequent adenine and uridine bases within the 3' untranslated region of a mRNA molecule or in pre-mRNA intron. The ARE-binding element consensus is UUAUUUAUU. ARE-binding proteins control the stability and/or translation of mRNAs. GO:0070402 Binding to the reduced form, NADPH, of nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions. GO:0003960 Catalysis of the reaction: 2 a quinone + NADPH + H+ = 2 a 1,4-benzosemiquinone + NADP+. GO:0008270 Binding to a zinc ion (Zn). 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: hit
Human identity (%): 52.632
Human E-value: 1.1e-06
Gut microbiome off-target: hit
Essential (DEG): N
Localization: Cytoplasmic

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 0.755

Structure –

Pocket –

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 6 GO

Enzyme Commission (EC)

1.6.5.5

Gene Ontology (GO)

GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
GO:0035925 Binding to a region containing frequent adenine and uridine bases within the 3' untranslated region of a mRNA molecule or in pre-mRNA intron. The ARE-binding element consensus is UUAUUUAUU. ARE-binding proteins control the stability and/or translation of mRNAs.
GO:0070402 Binding to the reduced form, NADPH, of nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions.
GO:0003960 Catalysis of the reaction: 2 a quinone + NADPH + H+ = 2 a 1,4-benzosemiquinone + NADP+.
GO:0008270 Binding to a zinc ion (Zn).
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.

18 records

Show feature table

Start	End	DB	Term	Name
4	325	PANTHER	PTHR48106	QUINONE OXIDOREDUCTASE PIG3-RELATED
124	269	FunFam	G3DSA:3.40.50.720:FF:000053	Quinone oxidoreductase 1
141	162	ProSitePatterns	PS01162	Quinone oxidoreductase / zeta-crystallin signature.
141	162	InterPro	IPR002364	Quinone oxidoreductase/zeta-crystallin, conserved site
11	319	Gene3D	G3DSA:3.90.180.10	-
29	87	Pfam	PF08240	Alcohol dehydrogenase GroES-like domain
29	87	InterPro	IPR013154	Alcohol dehydrogenase-like, N-terminal
8	142	SUPERFAMILY	SSF50129	GroES-like
8	142	InterPro	IPR011032	GroES-like superfamily
3	325	CDD	cd05286	QOR2
3	325	InterPro	IPR047618	Quinone oxidoreductase-like
112	267	SUPERFAMILY	SSF51735	NAD(P)-binding Rossmann-fold domains
112	267	InterPro	IPR036291	NAD(P)-binding domain superfamily
124	269	Gene3D	G3DSA:3.40.50.720	-
11	323	SMART	SM00829	PKS_ER_names_mod
11	323	InterPro	IPR020843	Polyketide synthase, enoylreductase domain
152	268	Pfam	PF00107	Zinc-binding dehydrogenase
152	268	InterPro	IPR013149	Alcohol dehydrogenase-like, C-terminal

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 PA0023	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				0.755

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.

58 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
8ID	4W6Z	P00330	790.3 Da LogP -2.41 TPSA 318.3	3 viol.	✓ Clean	`c1cc(c[n+](c1)[C@H]2[C@@H]([C@@H]([C@H](O2)CO[P…`
BMD	3PII	P42328	87.1 Da LogP 0.27 TPSA 43.1	✓ Ro5	✓ Clean	`CCCC(=O)N`
DIF	2WEK	Q8N4Q0	296.2 Da LogP 4.36 TPSA 49.3	✓ Ro5	✓ Clean	`c1ccc(c(c1)CC(=O)O)Nc2c(cccc2Cl)Cl`
ETF	4W6Z	P00330	100.0 Da LogP 0.54 TPSA 20.2	✓ Ro5	✓ Clean	`C(C(F)(F)F)O`
FU2	3S2F	Q46UZ9	96.1 Da LogP 1.09 TPSA 30.2	✓ Ro5	✓ Clean	`c1cc(oc1)C=O`
ISP	3S2F	Q46UZ9	140.1 Da LogP 0.50 TPSA 66.8	✓ Ro5	✓ Clean	`CC(C)OP(=O)(O)O`
PFN	2X7H	Q8N4Q0-2	242.3 Da LogP 3.67 TPSA 46.5	✓ Ro5	✓ Clean	`C[C@H](c1cccc(c1)Oc2ccccc2)C(=O)O`
X1H	2X1H	Q8N4Q0	376.4 Da LogP 5.22 TPSA 66.8	1 viol.	✓ Clean	`COc1ccc(cc1)C(=O)c2c3ccc(cc3sc2c4ccc(cc4)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
ZINC12501520	1.000	458.5 Da LogP -0.88 TPSA 123.5	1 viol.	✓ Clean	`OCCOCCOCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC1281	1.000	296.2 Da LogP 4.36 TPSA 49.3	✓ Ro5	✓ Clean	`O=C(O)Cc1ccccc1Nc1c(Cl)cccc1Cl`
ZINC301	1.000	242.3 Da LogP 3.67 TPSA 46.5	✓ Ro5	✓ Clean	`C[C@H](C(=O)O)c1cccc(Oc2ccccc2)c1`
ZINC3874716	1.000	414.5 Da LogP -0.90 TPSA 114.3	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC402909	1.000	242.3 Da LogP 3.67 TPSA 46.5	✓ Ro5	✓ Clean	`C[C@@H](C(=O)O)c1cccc(Oc2ccccc2)c1`
ZINC4283769	1.000	238.3 Da LogP -0.96 TPSA 77.4	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCO`
ZINC4521548	1.000	282.3 Da LogP -0.95 TPSA 86.6	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCOCCO`
ZINC5178829	1.000	326.4 Da LogP -0.93 TPSA 95.8	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCOCCOCCO`
ZINC5178830	1.000	370.4 Da LogP -0.91 TPSA 105.1	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC2506700	0.800	340.6 Da LogP 4.47 TPSA 49.3	✓ Ro5	✓ Clean	`O=C(O)Cc1ccccc1Nc1c(Cl)cccc1Br`
ZINC26395789	0.800	279.7 Da LogP 3.85 TPSA 49.3	✓ Ro5	✓ Clean	`O=C(O)Cc1ccccc1Nc1c(F)cccc1Cl`
ZINC33998501	0.795	362.4 Da LogP 4.92 TPSA 77.8	✓ Ro5	✓ Clean	`O=C(c1ccc(O)cc1)c1c(-c2ccc(O)cc2)sc2cc(O)ccc12`
ZINC2383046	0.743	312.2 Da LogP 4.07 TPSA 69.6	✓ Ro5	✓ Clean	`O=C(O)Cc1ccccc1Nc1c(Cl)cc(O)cc1Cl`
ZINC32167079	0.743	256.3 Da LogP 3.76 TPSA 35.5	✓ Ro5	✓ Clean	`COC(=O)[C@@H](C)c1cccc(Oc2ccccc2)c1`
ZINC32167081	0.743	256.3 Da LogP 3.76 TPSA 35.5	✓ Ro5	✓ Clean	`COC(=O)[C@H](C)c1cccc(Oc2ccccc2)c1`
ZINC3805798	0.737	354.2 Da LogP 3.91 TPSA 75.6	✓ Ro5	✓ Clean	`O=C(O)COC(=O)Cc1ccccc1Nc1c(Cl)cccc1Cl`
ZINC13558626	0.722	310.2 Da LogP 4.45 TPSA 38.3	✓ Ro5	✓ Clean	`COC(=O)Cc1ccccc1Nc1c(Cl)cccc1Cl`
ZINC32165764	0.719	242.3 Da LogP 3.67 TPSA 46.5	✓ Ro5	✓ Clean	`C[C@@H](C(=O)O)c1ccc(Oc2ccccc2)cc1`
ZINC32165766	0.719	242.3 Da LogP 3.67 TPSA 46.5	✓ Ro5	✓ Clean	`C[C@H](C(=O)O)c1ccc(Oc2ccccc2)cc1`
ZINC39330321	0.703	323.2 Da LogP 4.37 TPSA 32.3	✓ Ro5	✓ Clean	`CN(C)C(=O)Cc1ccccc1Nc1c(Cl)cccc1Cl`
ZINC6095281	0.703	312.2 Da LogP 4.07 TPSA 69.6	✓ Ro5	✓ Clean	`O=C(O)Cc1ccccc1Nc1c(Cl)ccc(O)c1Cl`
ZINC44699349	0.700	412.2 Da LogP 3.45 TPSA 101.9	✓ Ro5	✓ Clean	`O=C(O)COC(=O)COC(=O)Cc1ccccc1Nc1c(Cl)cccc1Cl`
ZINC44699432	0.700	470.3 Da LogP 2.99 TPSA 128.2	✓ Ro5	✓ Clean	`O=C(O)COC(=O)COC(=O)COC(=O)Cc1ccccc1Nc1c(Cl)ccc…`
ZINC2506699	0.697	268.1 Da LogP 4.23 TPSA 32.3	✓ Ro5	✓ Clean	`OCc1ccccc1Nc1c(Cl)cccc1Cl`
ZINC22060327	0.694	312.2 Da LogP 4.07 TPSA 69.6	✓ Ro5	✓ Clean	`O=C(O)Cc1cc(O)ccc1Nc1c(Cl)cccc1Cl`
ZINC238950253	0.694	744.4 Da LogP -2.90 TPSA 364.8	3 viol.	✓ Clean	`NC(=O)c1ccc[n+]([C@@H]2O[C@H](CO[P@](=O)(O)O[P@…`
ZINC238950256	0.694	744.4 Da LogP -2.90 TPSA 364.8	3 viol.	✓ Clean	`NC(=O)c1ccc[n+]([C@@H]2O[C@H](CO[P@](=O)(O)O[P@…`
ZINC238950259	0.694	744.4 Da LogP -2.90 TPSA 364.8	3 viol.	✓ Clean	`NC(=O)c1ccc[n+]([C@@H]2O[C@H](CO[P@](=O)(O)O[P@…`
ZINC238950261	0.694	744.4 Da LogP -2.90 TPSA 364.8	3 viol.	✓ Clean	`NC(=O)c1ccc[n+]([C@@H]2O[C@H](CO[P@](=O)(O)O[P@…`
ZINC115086873	0.688	209.2 Da LogP -1.08 TPSA 83.2	✓ Ro5	✓ Clean	`NOCCOCCOCCOCCO`
ZINC137432264	0.688	457.6 Da LogP -0.91 TPSA 129.3	1 viol.	✓ Clean	`NCCOCCOCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC146143823	0.688	237.3 Da LogP -1.00 TPSA 83.2	✓ Ro5	✓ Clean	`NCCOCCOCCOCCOCCO`
ZINC1542984442	0.688	413.5 Da LogP -0.93 TPSA 120.1	✓ Ro5	✓ Clean	`NCCOCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC1565503710	0.688	254.3 Da LogP -0.03 TPSA 57.2	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCS`
ZINC1580161	0.688	208.3 Da LogP -0.33 TPSA 57.2	✓ Ro5	✓ Clean	`COCCOCCOCCOCCO`
ZINC16052118	0.688	340.4 Da LogP -0.28 TPSA 84.8	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCO`
ZINC16052257	0.688	384.5 Da LogP -0.26 TPSA 94.1	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC1857792028	0.688	430.6 Da LogP 0.04 TPSA 94.1	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCOCCOCCOCCOCCS`
ZINC1857792057	0.688	474.6 Da LogP 0.06 TPSA 103.3	1 viol.	✓ Clean	`OCCOCCOCCOCCOCCOCCOCCOCCOCCOCCS`
ZINC230494776	0.688	325.4 Da LogP -0.96 TPSA 101.6	✓ Ro5	✓ Clean	`NCCOCCOCCOCCOCCOCCOCCO`
ZINC34317654	0.688	472.6 Da LogP -0.23 TPSA 112.5	1 viol.	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC38917157	0.688	210.3 Da LogP -0.04 TPSA 47.9	✓ Ro5	✓ Clean	`OCCOCCOCCOCCS`
ZINC44076059	0.688	428.5 Da LogP -0.24 TPSA 103.3	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC5210101	0.688	252.3 Da LogP -0.31 TPSA 66.4	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCO`
ZINC5650743	0.688	222.3 Da LogP 0.07 TPSA 57.2	✓ Ro5	✓ Clean	`CCOCCOCCOCCOCCO`
ZINC6403917	0.688	354.4 Da LogP 0.11 TPSA 84.8	✓ Ro5	✓ Clean	`CCOCCOCCOCCOCCOCCOCCOCCO`
ZINC77271182	0.688	281.3 Da LogP -0.98 TPSA 92.4	✓ Ro5	✓ Clean	`NCCOCCOCCOCCOCCOCCO`
ZINC83253921	0.688	369.5 Da LogP -0.95 TPSA 110.9	✓ Ro5	✓ Clean	`NCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC90741446	0.688	386.5 Da LogP 0.02 TPSA 84.8	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCOCCOCCOCCS`
ZINC90741447	0.688	298.4 Da LogP -0.01 TPSA 66.4	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCOCCS`

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.