Protein profile

PA0849

thioredoxin reductase

Genome: NC_002516.2

Gene: PA0849 trxB2 Structure source: AlphaFold UniProt Q9I592

Export view

Amino acids 316

Annotations 6

Features 27

PDB binders 4

Druggability 0.4

Overview

Basic information about this protein and its source genome.

Accession: PA0849
Assembly: Pseudomonas aeruginosa PAO1, complete genome
Gene: PA0849 trxB2
Status: annotated
Amino acids: 316
Structure source: AlphaFold

1.8.1.9

GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. GO:0004791 Catalysis of the reaction: thioredoxin-dithiol + NADP+ = thioredoxin-disulfide + H+ + NADPH. GO:0045454 Any process that maintains the redox environment of a cell or compartment within a cell. GO:0019430 Any process, acting at the cellular level, involved in removing superoxide radicals (O2-) from a cell or organism, e.g. by conversion to dioxygen (O2) and hydrogen peroxide (H2O2). 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 (%): 31.973
Human E-value: 1.77e-06
Gut microbiome off-target: hit
Essential (DEG): Y
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 0.4

Structure –

Pocket –

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 5 GO

Enzyme Commission (EC)

1.8.1.9

Gene Ontology (GO)

GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
GO:0004791 Catalysis of the reaction: thioredoxin-dithiol + NADP+ = thioredoxin-disulfide + H+ + NADPH.
GO:0045454 Any process that maintains the redox environment of a cell or compartment within a cell.
GO:0019430 Any process, acting at the cellular level, involved in removing superoxide radicals (O2-) from a cell or organism, e.g. by conversion to dioxygen (O2) and hydrogen peroxide (H2O2).
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.

27 records

Show feature table

Start	End	DB	Term	Name
119	244	Gene3D	G3DSA:3.50.50.60	-
119	244	InterPro	IPR036188	FAD/NAD(P)-binding domain superfamily
2	313	SUPERFAMILY	SSF51905	FAD/NAD(P)-binding domain
2	313	InterPro	IPR036188	FAD/NAD(P)-binding domain superfamily
8	314	PANTHER	PTHR48105	THIOREDOXIN REDUCTASE 1-RELATED-RELATED
9	313	NCBIfam	TIGR01292	thioredoxin-disulfide reductase
9	313	InterPro	IPR005982	Thioredoxin reductase
10	313	Gene3D	G3DSA:3.50.50.60	-
10	313	InterPro	IPR036188	FAD/NAD(P)-binding domain superfamily
9	300	Pfam	PF07992	Pyridine nucleotide-disulphide oxidoreductase
9	300	InterPro	IPR023753	FAD/NAD(P)-binding domain
137	157	ProSitePatterns	PS00573	Pyridine nucleotide-disulphide oxidoreductases class-II active site.
137	157	InterPro	IPR008255	Pyridine nucleotide-disulphide oxidoreductase, class-II, active site
107	125	PRINTS	PR00368	FAD-dependent pyridine nucleotide reductase signature
149	167	PRINTS	PR00368	FAD-dependent pyridine nucleotide reductase signature
10	29	PRINTS	PR00368	FAD-dependent pyridine nucleotide reductase signature
236	252	PRINTS	PR00368	FAD-dependent pyridine nucleotide reductase signature
266	288	PRINTS	PR00368	FAD-dependent pyridine nucleotide reductase signature
9	31	PRINTS	PR00469	Pyridine nucleotide disulphide reductase class-II signature
276	294	PRINTS	PR00469	Pyridine nucleotide disulphide reductase class-II signature
130	142	PRINTS	PR00469	Pyridine nucleotide disulphide reductase class-II signature
108	116	PRINTS	PR00469	Pyridine nucleotide disulphide reductase class-II signature
200	216	PRINTS	PR00469	Pyridine nucleotide disulphide reductase class-II signature
238	259	PRINTS	PR00469	Pyridine nucleotide disulphide reductase class-II signature
42	57	PRINTS	PR00469	Pyridine nucleotide disulphide reductase class-II signature
145	169	PRINTS	PR00469	Pyridine nucleotide disulphide reductase class-II signature
63	73	PRINTS	PR00469	Pyridine nucleotide disulphide reductase class-II signature

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...

Legend High Medium Low

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 PA0849	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
3				0.4

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.

70 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
3AA	1F6M	P0A9P4	716.4 Da LogP -2.42 TPSA 347.7	3 viol.	✓ Clean	`c1cc(c[n+](c1)[C@H]2[C@@H]([C@@H]([C@H](O2)CO[P…`
FDA	4JNQ	Q8YID2	787.6 Da LogP -1.75 TPSA 363.3	3 viol.	✓ Clean	`Cc1cc2c(cc1C)N(C3=C(N2)C(=O)NC(=O)N3)C[C@@H]([C…`
MLI	6BPY	A0A229Y1X4	102.0 Da LogP -3.12 TPSA 80.3	✓ Ro5	✓ Clean	`C(C(=O)[O-])C(=O)[O-]`
MLT	6BPY	A0A229Y1X4	134.1 Da LogP -1.09 TPSA 94.8	✓ Ro5	✓ Clean	`C([C@H](C(=O)O)O)C(=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).

Ligand	UniProt (homolog)	pchembl	MW · LogP · TPSA	Lipinski	PAINS	SMILES
CHEMBL2035464	P0A9P4	8.00	478.3 Da LogP 2.69 TPSA 44.0	✓ Ro5	✓ Clean	`O=c1c2ccccc2[se]n1CCCCCCn1[se]c2ccccc2c1=O`
CHEMBL2035461	P0A9P4	7.40	436.2 Da LogP 1.52 TPSA 44.0	✓ Ro5	✓ Clean	`O=c1c2ccccc2[se]n1CCCn1[se]c2ccccc2c1=O`
CHEMBL2035460	P0A9P4	7.30	422.2 Da LogP 1.13 TPSA 44.0	✓ Ro5	✓ Clean	`O=c1c2ccccc2[se]n1CCn1[se]c2ccccc2c1=O`
CHEMBL3655713	P0A9P4	6.60	322.7 Da LogP 3.01 TPSA 22.0	✓ Ro5	✓ Clean	`Cc1cc(Cl)ccc1-n1[se]c2ccccc2c1=O`
CHEMBL3655720	P0A9P4	6.60	320.2 Da LogP 1.35 TPSA 78.0	✓ Ro5	✓ Clean	`O=c1c2ccccc2[se]n1-c1ncccc1[N+](=O)[O-]`
CHEMBL51085	P0A9P4	6.52	274.2 Da LogP 2.05 TPSA 22.0	✓ Ro5	✓ Clean	`O=c1c2ccccc2[se]n1-c1ccccc1`
CHEMBL3926452	C4LW95	6.41	361.4 Da LogP 4.48 TPSA 58.7	✓ Ro5	✓ Clean	`O=C1/C(=C/c2ccccn2)S/C(=N\c2ccccc2)N1Cc1ccco1`
CHEMBL5395264	P0A9P4	6.30	476.3 Da LogP 3.86 TPSA 35.6	✓ Ro5	✓ Clean	`Cc1nn(CC[Se][Se]CCn2nc(C)c3ccccc32)c2ccccc12`
CHEMBL3655712	P0A9P4	6.26	308.6 Da LogP 2.70 TPSA 22.0	✓ Ro5	✓ Clean	`O=c1c2ccccc2[se]n1-c1ccc(Cl)cc1`
CHEMBL3913125	C4LW95	6.17	420.5 Da LogP 5.10 TPSA 64.3	1 viol.	✓ Clean	`COc1ccc(/C=C2\S/C(=N\c3ccccc3)N(Cc3ccco3)C2=O)c…`
CHEMBL3968421	C4LW95	6.16	420.5 Da LogP 5.10 TPSA 64.3	1 viol.	✓ Clean	`COc1ccc(OC)c(/C=C2\S/C(=N\c3ccccc3)N(Cc3ccco3)C…`
CHEMBL5397149	P0A9P4	6.16	538.3 Da LogP 3.06 TPSA 121.9	1 viol.	✓ Clean	`O=[N+]([O-])c1ccc2c(cnn2CC[Se][Se]CCn2ncc3cc([N…`
CHEMBL5416840	P0A9P4	6.16	473.2 Da LogP 3.48 TPSA 35.6	✓ Ro5	✓ Clean	`Cc1nn(CC[Se][Se]CCn2nc(C)c(Cl)c2C)c(C)c1Cl`
CHEMBL5440854	P0A9P4	6.16	506.3 Da LogP 1.74 TPSA 74.8	1 viol.	✓ Clean	`O=C1c2ccccc2C(=O)N1CC[Se][Se]CCN1C(=O)c2ccccc2C…`
CHEMBL3976958	C4LW95	6.14	376.4 Da LogP 4.79 TPSA 66.0	✓ Ro5	✓ Clean	`O=C1/C(=C/c2ccc(O)cc2)S/C(=N\c2ccccc2)N1Cc1ccco1`
CHEMBL3655716	P0A9P4	6.00	198.1 Da LogP 0.59 TPSA 32.9	✓ Ro5	✓ Clean	`O=c1[nH][se]c2ccccc12`

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
ZINC18246980	1.000	376.4 Da LogP 4.79 TPSA 66.0	✓ Ro5	✓ Clean	`O=C1/C(=C\c2ccc(O)cc2)S/C(=N/c2ccccc2)N1Cc1ccco1`
ZINC2293355652	1.000	376.4 Da LogP 4.79 TPSA 66.0	✓ Ro5	✓ Clean	`O=C1C(=Cc2ccc(O)cc2)SC(=Nc2ccccc2)N1Cc1ccco1`
ZINC15013521	0.852	406.5 Da LogP 4.80 TPSA 75.3	✓ Ro5	✓ Clean	`COc1cc(/C=C2/S/C(=N/c3ccccc3)N(Cc3ccco3)C2=O)cc…`
ZINC9261465	0.818	478.5 Da LogP 4.64 TPSA 90.6	✓ Ro5	✓ Clean	`COC(=O)COc1ccc(/C=C2/S/C(=N\c3ccccc3)N(Cc3ccco3…`
ZINC4660313	0.780	368.5 Da LogP 4.33 TPSA 51.1	✓ Ro5	✓ Clean	`CCN1C(=O)/C(=C\c2cc(OC)ccc2OC)S/C1=N\c1ccccc1`
ZINC100314562	0.769	434.5 Da LogP 4.82 TPSA 73.5	✓ Ro5	✓ Clean	`COc1cc2c(cc1/C=C1/S/C(=N\c3ccccc3)N(Cc3ccco3)C1…`
ZINC17719664	0.769	434.5 Da LogP 4.82 TPSA 73.5	✓ Ro5	✓ Clean	`COc1cc2c(cc1/C=C1/S/C(=N/c3ccccc3)N(Cc3ccco3)C1…`
ZINC245309458	0.769	434.5 Da LogP 4.82 TPSA 73.5	✓ Ro5	✓ Clean	`COc1cc2c(cc1/C=C1/SC(=Nc3ccccc3)N(Cc3ccco3)C1=O…`
ZINC13546520	0.759	405.4 Da LogP 4.99 TPSA 88.9	✓ Ro5	✓ Clean	`O=C1/C(=C/c2ccc([N+](=O)[O-])cc2)S/C(=N\c2ccccc…`
ZINC4664355	0.759	368.5 Da LogP 4.33 TPSA 51.1	✓ Ro5	✓ Clean	`CCN1C(=O)/C(=C\c2ccc(OC)c(OC)c2)S/C1=N/c1ccccc1`
ZINC13880821	0.750	418.5 Da LogP 4.87 TPSA 72.1	✓ Ro5	✓ Clean	`COC(=O)c1ccc(/C=C2\S/C(=N\c3ccccc3)N(Cc3ccco3)C…`
ZINC49582222	0.750	207.2 Da LogP 0.94 TPSA 81.2	✓ Ro5	✓ Clean	`O=[N+]([O-])c1ccc2c(cnn2CCO)c1`
ZINC4526109	0.741	350.4 Da LogP 4.68 TPSA 59.0	✓ Ro5	✓ Clean	`O=C1/C(=C/c2ccco2)S/C(=N\c2ccccc2)N1Cc1ccco1`
ZINC1014076	0.738	382.5 Da LogP 4.72 TPSA 51.1	✓ Ro5	✓ Clean	`CCCN1C(=O)/C(=C/c2cc(OC)ccc2OC)S/C1=N\c1ccccc1`
ZINC4664262	0.738	382.5 Da LogP 4.72 TPSA 51.1	✓ Ro5	✓ Clean	`CCCN1C(=O)/C(=C\c2cc(OC)ccc2OC)S/C1=N/c1ccccc1`
ZINC18246975	0.733	445.5 Da LogP 4.92 TPSA 58.3	✓ Ro5	Alert	`O=C1/C(=C\c2ccc(N3CCOCC3)cc2)S/C(=N/c2ccccc2)N1…`
ZINC8816280	0.729	477.5 Da LogP 4.35 TPSA 107.4	✓ Ro5	✓ Clean	`CCOc1cc(/C=C2\S/C(=N\c3ccccc3)N(Cc3ccco3)C2=O)c…`
ZINC2777124	0.714	398.5 Da LogP 3.95 TPSA 60.4	✓ Ro5	✓ Clean	`COCCN1C(=O)/C(=C/c2cc(OC)ccc2OC)S/C1=N\c1ccccc1`
ZINC5660821	0.714	398.5 Da LogP 3.95 TPSA 60.4	✓ Ro5	✓ Clean	`COCCN1C(=O)/C(=C\c2cc(OC)ccc2OC)S/C1=N\c1ccccc1`
ZINC1184606	0.710	361.4 Da LogP 3.70 TPSA 51.9	✓ Ro5	Alert	`COc1ccc(OC)c(/C=C2/SC(=S)N(Cc3ccco3)C2=O)c1`
ZINC13534752	0.710	361.4 Da LogP 3.70 TPSA 51.9	✓ Ro5	Alert	`COc1ccc(OC)c(/C=C2\SC(=S)N(Cc3ccco3)C2=O)c1`
ZINC175473	0.708	320.3 Da LogP 1.58 TPSA 74.8	✓ Ro5	✓ Clean	`O=C1c2ccccc2C(=O)N1CCN1C(=O)c2ccccc2C1=O`
ZINC13739257	0.705	361.4 Da LogP 3.70 TPSA 51.9	✓ Ro5	Alert	`COc1ccc(/C=C2\SC(=S)N(Cc3ccco3)C2=O)cc1OC`
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`
ZINC1065235	0.696	302.4 Da LogP 3.08 TPSA 46.3	✓ Ro5	Alert	`O=C1/C(=C\c2ccccn2)SC(=S)N1Cc1ccco1`
ZINC1065238	0.696	302.4 Da LogP 3.08 TPSA 46.3	✓ Ro5	Alert	`O=C1/C(=C/c2ccccn2)SC(=S)N1Cc1ccco1`
ZINC2141838	0.694	398.5 Da LogP 3.95 TPSA 60.4	✓ Ro5	✓ Clean	`COCCN1C(=O)/C(=C/c2ccc(OC)c(OC)c2)S/C1=N\c1cccc…`
ZINC5879640	0.694	398.5 Da LogP 3.95 TPSA 60.4	✓ Ro5	✓ Clean	`COCCN1C(=O)/C(=C\c2ccc(OC)c(OC)c2)S/C1=N\c1cccc…`
ZINC1187854	0.673	317.4 Da LogP 3.39 TPSA 53.7	✓ Ro5	Alert	`O=C1/C(=C/c2ccc(O)cc2)SC(=S)N1Cc1ccco1`
ZINC12436467	0.673	317.4 Da LogP 3.39 TPSA 53.7	✓ Ro5	Alert	`O=C1/C(=C\c2ccc(O)cc2)SC(=S)N1Cc1ccco1`
ZINC4660314	0.672	354.4 Da LogP 3.94 TPSA 51.1	✓ Ro5	✓ Clean	`COc1ccc(OC)c(/C=C2/S/C(=N\c3ccccc3)N(C)C2=O)c1`
ZINC96592063	0.672	354.4 Da LogP 3.94 TPSA 51.1	✓ Ro5	✓ Clean	`COc1ccc(OC)c(/C=C2/S/C(=N/c3ccccc3)N(C)C2=O)c1`
ZINC4491584	0.667	383.5 Da LogP 3.78 TPSA 54.4	✓ Ro5	✓ Clean	`COc1ccc(OC)c(/C=C2/S/C(=N\c3ccccc3)N(N(C)C)C2=O…`
ZINC4664352	0.667	368.5 Da LogP 4.33 TPSA 51.1	✓ Ro5	✓ Clean	`CCN1C(=O)/C(=C\c2ccc(OC)cc2OC)S/C1=N/c1ccccc1`
ZINC71773889	0.667	206.1 Da LogP -1.77 TPSA 132.1	✓ Ro5	✓ Clean	`O=C(C[C@H](O)C(=O)O)C[C@H](O)C(=O)O`
ZINC71773890	0.667	206.1 Da LogP -1.77 TPSA 132.1	✓ Ro5	✓ Clean	`O=C(C[C@H](O)C(=O)O)C[C@@H](O)C(=O)O`
ZINC71773891	0.667	206.1 Da LogP -1.77 TPSA 132.1	✓ Ro5	✓ Clean	`O=C(C[C@@H](O)C(=O)O)C[C@@H](O)C(=O)O`
ZINC101695107	0.662	412.5 Da LogP 4.34 TPSA 60.4	✓ Ro5	✓ Clean	`CCOCCN1C(=O)/C(=C/c2ccc(OC)c(OC)c2)S/C1=N/c1ccc…`
ZINC4466315	0.661	336.4 Da LogP 4.18 TPSA 52.9	✓ Ro5	✓ Clean	`C=CCN1C(=O)/C(=C\c2ccc(O)cc2)S/C1=N/c1ccccc1`
ZINC4672070	0.656	382.5 Da LogP 4.64 TPSA 51.1	✓ Ro5	✓ Clean	`CCN1C(=O)/C(=C\c2cc(OC)ccc2OC)S/C1=N\c1ccc(C)cc1`
ZINC1719027	0.654	348.4 Da LogP 2.36 TPSA 74.8	✓ Ro5	✓ Clean	`O=C1c2ccccc2C(=O)N1CCCCN1C(=O)c2ccccc2C1=O`
ZINC398642	0.654	334.3 Da LogP 1.97 TPSA 74.8	✓ Ro5	✓ Clean	`O=C1c2ccccc2C(=O)N1CCCN1C(=O)c2ccccc2C1=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`
ZINC4660312	0.651	352.5 Da LogP 4.63 TPSA 41.9	✓ Ro5	✓ Clean	`CCN1C(=O)/C(=C\c2ccc(C)c(OC)c2)S/C1=N\c1ccccc1`
ZINC96610654	0.651	352.5 Da LogP 4.63 TPSA 41.9	✓ Ro5	✓ Clean	`CCN1C(=O)/C(=C\c2ccc(C)c(OC)c2)S/C1=N/c1ccccc1`
ZINC4682460	0.650	342.4 Da LogP 3.10 TPSA 72.1	✓ Ro5	✓ Clean	`COC(=O)/C=C1/S/C(=N\c2ccccc2)N(Cc2ccco2)C1=O`
ZINC9957365	0.647	474.5 Da LogP 4.96 TPSA 88.4	✓ Ro5	✓ Clean	`COc1cc(/C=C2\S/C(=N\c3ccccc3)N(Cc3ccccc3)C2=O)c…`
ZINC8698499	0.636	253.3 Da LogP 2.99 TPSA 61.0	✓ Ro5	✓ Clean	`O=[N+]([O-])c1ccc2c(cnn2Cc2ccccc2)c1`

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.