Protein target profile

PA1962

FMN-dependent NADH-azoreductase

Genome: NC_002516.2

Gene: azoR2 PA1962 3D evidence: AlphaFold DB model UniProt Q9I2E2

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Length 202

Pocket druggability 0.713

Ligand records 59

EC / GO 2 / 4

Target summary

Promising target candidate with multiple supporting evidence streams.

5 signals

Strengths

Risks / watch

No major risk signal surfaced in the loaded evidence.

Missing evidence

No metabolic context No SBML/network-derived reaction evidence is loaded for this protein.

How to read this page

PDB: experimentally determined structures from the Protein Data Bank. These are the strongest structural evidence, but may cover only part of the protein.

AlphaFold DB model: a precomputed predicted structure downloaded from AlphaFold Database/UniProt, not an experiment performed here.

ColabFold model: a predicted structure generated for this workspace; interpret it with coverage and confidence.

pLDDT: confidence score for predicted structures. High values support local geometry; low values mean the region should not drive pocket interpretation.

FPocket / P2Rank: software tools that predict possible ligand-binding pockets on a 3D structure. They are useful screening signals, not experimental validation.

Druggability: a pocket-based estimate of whether a small molecule could bind productively. It does not mean a drug already exists.

PDB ligand: a compound observed in an experimental structure. Direct same-protein records are stronger than homolog-transferred records.

ChEMBL: a public database of measured compound bioactivity. Direct entries are stronger than entries transferred from similar proteins.

ZINC: a purchasable-compound database. Here it marks proposed candidates from chemical similarity, not measured binders.

LigQ / LigQ_2: an internal TPW pipeline step that gathers PDB, ChEMBL, and ZINC ligand evidence for each protein.

Off-target: sequence similarity to proteins we prefer not to hit, such as human proteins or beneficial gut microbiome proteins.

DEG: Database of Essential Genes. A match suggests the protein resembles genes known to be essential in other organisms.

Roary / CoreCruncher: pan-genome tools used to decide whether a gene is core across analyzed strains or accessory/strain-specific.

EC / GO: functional annotations: EC describes enzyme reactions; GO describes biological process, molecular function, or cellular component.

KEGG pathway: a curated metabolic route label used here to group reactions imported from the metabolic model.

Chokepoint: a metabolic reaction that is the only producer or consumer of a metabolite in the imported model.

Overview

Basic information about this protein and its source genome.

Accession: PA1962
Assembly: Pseudomonas aeruginosa PAO1, complete genome
Gene: azoR2 PA1962
Status: annotated
Amino acids: 202
3D evidence: AlphaFold DB model

1.6.5.- 1.7.1.17

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. GO:0010181 Binding to flavin mono nucleotide. Flavin mono nucleotide (FMN) is the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes. GO:0016652 Catalysis of an oxidation-reduction (redox) reaction in which NADH or NADPH acts as a hydrogen or electron donor and reduces NAD+ or NADP. GO:0016655 Catalysis of an oxidation-reduction (redox) reaction in which NADH or NADPH acts as a hydrogen or electron donor and reduces a quinone or a similar acceptor molecule.

Target profile

Computed evidence for target prioritization.

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

Selected pocket evidence

The selected pocket score is the FPocket value used for ranking after applying the curated structure priority. It estimates small-molecule pocket quality; it is not experimental binding evidence. The 3D viewer may show a different loaded structure, so visible pockets can differ.

FPocket 0.713

Structure –

Pocket –

Sequence

Primary amino-acid sequence viewer.

MKLLHIDSSILGDASASRQLSAELVQAWRQNEDGLDVTYRDLAADAVAHFSALTLAAGSTPAELRDAALKHEVAVGEEVLEEFLAADVVVIGAPMYNFTISSQLKAWIDRIAVAGKTFRYTENGPVGLAGDKKVVIVSTAGGVHAGQPTGAAHEGYLRTVLGFFGITDIEVVRAEGLAYGEEPRTQAIAAARRQIAGQFAAA

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

2 EC 4 GO

Enzyme Commission (EC)

Gene Ontology (GO)

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.
GO:0010181 Binding to flavin mono nucleotide. Flavin mono nucleotide (FMN) is the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes.
GO:0016652 Catalysis of an oxidation-reduction (redox) reaction in which NADH or NADPH acts as a hydrogen or electron donor and reduces NAD+ or NADP.
GO:0016655 Catalysis of an oxidation-reduction (redox) reaction in which NADH or NADPH acts as a hydrogen or electron donor and reduces a quinone or a similar acceptor molecule.

Sequence Features

Domain/signature hits from InterPro and related databases.

10 records

Show feature table

Start	End	DB	Term	Name
1	201	Gene3D	G3DSA:3.40.50.360	-
1	201	InterPro	IPR029039	Flavoprotein-like superfamily
1	202	FunFam	G3DSA:3.40.50.360:FF:000049	FMN-dependent NADH-azoreductase
1	195	PANTHER	PTHR43741	FMN-DEPENDENT NADH-AZOREDUCTASE 1
1	199	Hamap	MF_01216	FMN dependent NADH:quinone oxidoreductase [azoR].
1	199	InterPro	IPR023048	NADH:quinone oxidoreductase, FMN-dependent
1	196	Pfam	PF02525	Flavodoxin-like fold
1	196	InterPro	IPR003680	Flavodoxin-like fold
1	199	SUPERFAMILY	SSF52218	Flavoproteins
1	199	InterPro	IPR029039	Flavoprotein-like superfamily

3D Structure

Selected loaded structure. Experimental PDB entries may cover only a portion of the sequence; AlphaFold DB and ColabFold models typically cover the full protein but remain computational predictions.

Loading 3D structure...

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Structural evidence

0 + 1

Experimental PDB entries plus predicted AlphaFold DB or ColabFold models. Click Switch to display a different loaded structure in the viewer.

Entry	Method	Resolution	Chain	Coverage	Links	Status
AlphaFold DB PA1962	AlphaFold DB	—	—	full sequence	—	Viewing

Pocket details Inspect a specific pocket, or open the full viewer

Binding pockets · FPocket

Druggability: high ≥ 0.7 · medium 0.4–0.69 · low < 0.4

Site 1 FPocket #1

0.713

Show in viewer

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.

59 records

Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 59 via homologs

Structural ligands 9 0 loaded crystals

Bioactive compounds 0 50 ZINC proposed compounds

Drug-like & clean 31 22 PAINS alerts

Best available ligand signal

12P PDB via homolog 546.7 Da · LogP -0.85 · TPSA 142.0 Open detail RCSB PDB

Detail RCSB PDB 12P PDB via homolog

Detail RCSB PDB AQN PDB via homolog

Detail RCSB PDB CBD PDB via homolog

Detail RCSB PDB DTC PDB via homolog

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
12P RCSB PDB	4C0W	Q88IY3	546.7 Da LogP -0.85 TPSA 142.0	2 viol.	✓ Clean	`C(COCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCO)O`
AQN RCSB PDB	4C0X	Q88IY3	288.3 Da LogP 1.71 TPSA 88.5	✓ Ro5	Alert	`c1ccc2c(c1)C(=O)c3ccc(cc3C2=O)S(=O)(=O)O`
CBD RCSB PDB	3W78	C0STY1	774.2 Da LogP 3.85 TPSA 298.0	3 viol.	Alert	`c1ccc2c(c1)C(=O)c3c(cc(c(c3C2=O)N)S(=O)(=O)O)Nc…`
DTC RCSB PDB	2Z9C	P41407	336.3 Da LogP 2.21 TPSA 86.7	✓ Ro5	✓ Clean	`c1ccc2c(c1)C(=O)C(C(=O)O2)CC3C(=O)c4ccccc4OC3=O`
FD5 RCSB PDB	4C14	Q88IY3	1180.2 Da LogP 5.33 TPSA 503.1	4 viol.	✓ Clean	`Cc1cc2c(cc1C)N(C3=NC(=O)N(C(=O)C3=N2)OCCS(c4ccc…`
NHE RCSB PDB	6JXN	G9QLG5	207.3 Da LogP 0.80 TPSA 66.4	✓ Ro5	✓ Clean	`C1CCC(CC1)NCCS(=O)(=O)O`
ORI RCSB PDB	3W79	C0STY1	328.3 Da LogP 4.21 TPSA 99.3	✓ Ro5	Alert	`c1ccc2c(c1)c(ccc2O)/N=N/c3ccc(cc3)S(=O)(=O)O`
PE8 RCSB PDB	6JXN	G9QLG5	370.4 Da LogP -0.91 TPSA 105.1	✓ Ro5	✓ Clean	`C(COCCOCCOCCOCCOCCOCCOCCO)O`
RE8 RCSB PDB	3W7A	C0STY1	378.4 Da LogP 5.36 TPSA 99.3	1 viol.	Alert	`c1ccc2c(c1)ccc(c2/N=N/c3ccc(c4c3cccc4)S(=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 ZINC	1.000	458.5 Da LogP -0.88 TPSA 123.5	1 viol.	✓ Clean	`OCCOCCOCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC1710230 ZINC	1.000	207.3 Da LogP 0.80 TPSA 66.4	✓ Ro5	✓ Clean	`O=S(=O)(O)CCNC1CCCCC1`
ZINC3874716 ZINC	1.000	414.5 Da LogP -0.90 TPSA 114.3	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC3875860 ZINC	1.000	288.3 Da LogP 1.71 TPSA 88.5	✓ Ro5	Alert	`O=C1c2ccccc2C(=O)c2cc(S(=O)(=O)O)ccc21`
ZINC4283769 ZINC	1.000	238.3 Da LogP -0.96 TPSA 77.4	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCO`
ZINC4416663 ZINC	1.000	328.3 Da LogP 4.21 TPSA 99.3	✓ Ro5	Alert	`O=S(=O)(O)c1ccc(/N=N/c2ccc(O)c3ccccc23)cc1`
ZINC4521548 ZINC	1.000	282.3 Da LogP -0.95 TPSA 86.6	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCOCCO`
ZINC5178829 ZINC	1.000	326.4 Da LogP -0.93 TPSA 95.8	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCOCCOCCO`
ZINC5178830 ZINC	1.000	370.4 Da LogP -0.91 TPSA 105.1	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC3964228 ZINC	0.875	368.3 Da LogP 0.96 TPSA 142.9	✓ Ro5	Alert	`O=C1c2ccc(S(=O)(=O)O)cc2C(=O)c2ccc(S(=O)(=O)O)c…`
ZINC4783235 ZINC	0.875	368.3 Da LogP 0.96 TPSA 142.9	✓ Ro5	Alert	`O=C1c2ccc(S(=O)(=O)O)cc2C(=O)c2cc(S(=O)(=O)O)cc…`
ZINC2023420 ZINC	0.800	340.3 Da LogP 1.39 TPSA 125.8	✓ Ro5	✓ Clean	`O=C1c2cc(S(=O)(=O)O)ccc2-c2ccc(S(=O)(=O)O)cc21`
ZINC2004372 ZINC	0.786	221.3 Da LogP 1.19 TPSA 66.4	✓ Ro5	✓ Clean	`O=S(=O)(O)CCCNC1CCCCC1`
ZINC38364153 ZINC	0.786	235.3 Da LogP 1.58 TPSA 66.4	✓ Ro5	✓ Clean	`O=S(=O)(O)CCCCNC1CCCCC1`
ZINC4543519 ZINC	0.784	327.4 Da LogP 3.61 TPSA 105.1	✓ Ro5	Alert	`NS(=O)(=O)c1ccc(/N=N/c2ccc(O)c3ccccc23)cc1`
ZINC143962765 ZINC	0.714	458.5 Da LogP 4.61 TPSA 153.7	✓ Ro5	Alert	`O=S(=O)(O)c1ccc(/N=N/c2c(O)cc(S(=O)(=O)O)c3cccc…`
ZINC5739708 ZINC	0.698	381.5 Da LogP 4.75 TPSA 82.3	✓ Ro5	Alert	`O=S(=O)(c1ccc(/N=N/c2ccc(O)c3ccccc23)cc1)N1CCCC1`
ZINC5553422 ZINC	0.697	368.3 Da LogP 0.96 TPSA 142.9	✓ Ro5	Alert	`O=C1c2ccc(S(=O)(=O)O)cc2C(=O)c2c1cccc2S(=O)(=O)O`
ZINC5553424 ZINC	0.697	368.3 Da LogP 0.96 TPSA 142.9	✓ Ro5	Alert	`O=C1c2cc(S(=O)(=O)O)ccc2C(=O)c2c1cccc2S(=O)(=O)O`
ZINC115086873 ZINC	0.688	209.2 Da LogP -1.08 TPSA 83.2	✓ Ro5	✓ Clean	`NOCCOCCOCCOCCO`
ZINC137432264 ZINC	0.688	457.6 Da LogP -0.91 TPSA 129.3	1 viol.	✓ Clean	`NCCOCCOCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC146143823 ZINC	0.688	237.3 Da LogP -1.00 TPSA 83.2	✓ Ro5	✓ Clean	`NCCOCCOCCOCCOCCO`
ZINC1542984442 ZINC	0.688	413.5 Da LogP -0.93 TPSA 120.1	✓ Ro5	✓ Clean	`NCCOCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC1565503710 ZINC	0.688	254.3 Da LogP -0.03 TPSA 57.2	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCS`
ZINC1580161 ZINC	0.688	208.3 Da LogP -0.33 TPSA 57.2	✓ Ro5	✓ Clean	`COCCOCCOCCOCCO`
ZINC16052118 ZINC	0.688	340.4 Da LogP -0.28 TPSA 84.8	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCO`
ZINC16052257 ZINC	0.688	384.5 Da LogP -0.26 TPSA 94.1	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC1857792028 ZINC	0.688	430.6 Da LogP 0.04 TPSA 94.1	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCOCCOCCOCCOCCS`
ZINC1857792057 ZINC	0.688	474.6 Da LogP 0.06 TPSA 103.3	1 viol.	✓ Clean	`OCCOCCOCCOCCOCCOCCOCCOCCOCCOCCS`
ZINC230494776 ZINC	0.688	325.4 Da LogP -0.96 TPSA 101.6	✓ Ro5	✓ Clean	`NCCOCCOCCOCCOCCOCCOCCO`
ZINC34317654 ZINC	0.688	472.6 Da LogP -0.23 TPSA 112.5	1 viol.	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC38917157 ZINC	0.688	210.3 Da LogP -0.04 TPSA 47.9	✓ Ro5	✓ Clean	`OCCOCCOCCOCCS`
ZINC44076059 ZINC	0.688	428.5 Da LogP -0.24 TPSA 103.3	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC5210101 ZINC	0.688	252.3 Da LogP -0.31 TPSA 66.4	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCO`
ZINC5650743 ZINC	0.688	222.3 Da LogP 0.07 TPSA 57.2	✓ Ro5	✓ Clean	`CCOCCOCCOCCOCCO`
ZINC5997860 ZINC	0.688	296.4 Da LogP -0.29 TPSA 75.6	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCO`
ZINC6403917 ZINC	0.688	354.4 Da LogP 0.11 TPSA 84.8	✓ Ro5	✓ Clean	`CCOCCOCCOCCOCCOCCOCCOCCO`
ZINC77271182 ZINC	0.688	281.3 Da LogP -0.98 TPSA 92.4	✓ Ro5	✓ Clean	`NCCOCCOCCOCCOCCOCCO`
ZINC83253921 ZINC	0.688	369.5 Da LogP -0.95 TPSA 110.9	✓ Ro5	✓ Clean	`NCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC90741446 ZINC	0.688	386.5 Da LogP 0.02 TPSA 84.8	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCOCCOCCOCCS`
ZINC90741447 ZINC	0.688	298.4 Da LogP -0.01 TPSA 66.4	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCOCCS`
ZINC4091246 ZINC	0.676	322.7 Da LogP 2.36 TPSA 88.5	✓ Ro5	Alert	`O=C1c2ccc(S(=O)(=O)O)cc2C(=O)c2c(Cl)cccc21`
ZINC17322476 ZINC	0.674	329.3 Da LogP 3.60 TPSA 112.2	✓ Ro5	Alert	`O=S(=O)(O)c1ccc(/N=N\c2ccc(O)c3ncccc23)cc1`
ZINC4707421 ZINC	0.674	329.3 Da LogP 3.60 TPSA 112.2	✓ Ro5	Alert	`O=S(=O)(O)c1ccc(/N=N/c2ccc(O)c3ncccc23)cc1`
ZINC1857800661 ZINC	0.667	292.3 Da LogP 4.66 TPSA 82.2	✓ Ro5	Alert	`O=C(O)c1ccc(N=Nc2ccc(O)c3ccccc23)cc1`
ZINC257347676 ZINC	0.667	342.4 Da LogP 4.51 TPSA 88.3	✓ Ro5	Alert	`COc1ccc(N=Nc2ccc(S(=O)(=O)O)cc2)c2ccccc12`
ZINC33246176 ZINC	0.667	355.4 Da LogP 4.57 TPSA 82.3	✓ Ro5	Alert	`CN(C)c1ccc(/N=N\c2ccc(S(=O)(=O)O)cc2)c2ccccc12`
ZINC3895982 ZINC	0.667	355.4 Da LogP 4.57 TPSA 82.3	✓ Ro5	Alert	`CN(C)c1ccc(/N=N/c2ccc(S(=O)(=O)O)cc2)c2ccccc12`
ZINC5739715 ZINC	0.667	397.5 Da LogP 3.98 TPSA 91.6	✓ Ro5	Alert	`O=S(=O)(c1ccc(/N=N/c2ccc(O)c3ccccc23)cc1)N1CCOC…`
ZINC4804160 ZINC	0.660	458.5 Da LogP 4.61 TPSA 153.7	✓ Ro5	Alert	`O=S(=O)(O)c1cc(/N=N/c2c(O)ccc3ccccc23)cc2c(S(=O…`

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.