Protein target profile

PA4986

oxidoreductase

Genome: NC_002516.2

Gene: PA4986 3D evidence: AlphaFold DB model UniProt Q9HUH9

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Length 648

Pocket druggability 0.694

Ligand records 3

EC / GO 0 / 6

Target summary

Target candidate with partial support; inspect missing evidence before prioritizing.

4 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: PA4986
Assembly: Pseudomonas aeruginosa PAO1, complete genome
Gene: PA4986
Status: annotated
Amino acids: 648
3D evidence: AlphaFold DB model

GO:0008670 Catalysis of the reactions: a 4,5-saturated-(2E)-enoyl-CoA + NADP+ = a (2E,4E)-dienoyl-CoA + H+ + NADPH, and a (2E,4Z)-dienoyl-CoA + H+ + NADPH = a 4,5-saturated-(2E)-enoyl-CoA + NADP+. GO:0010181 Binding to flavin mono nucleotide. Flavin mono nucleotide (FMN) is the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes. GO:0051536 Binding to an iron-sulfur cluster, a combination of iron and sulfur atoms. GO:0046872 Binding to a metal ion. GO:0033543 A fatty acid beta-oxidation pathway by which fatty acids having cis-double bonds on even-numbered carbons are degraded. In this pathway, the intermediate 2,4-dienoyl-CoA is converted to trans-2-enoyl-CoA by 2,4-dienoyl-CoA reductase and delta3-delta2-enoyl-CoA isomerase; trans-2-enoyl-CoA returns to the core beta-oxidation pathway for further degradation. Fatty acid beta-oxidation begins with the addition of coenzyme A to a fatty acid, and ends when only two or three carbons remain (as acetyl-CoA or propionyl-CoA respectively). 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: 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 0.694

Structure –

Pocket –

Sequence

Primary amino-acid sequence viewer.

MNFPHLFSPLEIRGKRLKNRIMSSGHDTSMPTDNLVNEPLVAYHRARARGGAGLIVMQVAGVHDSARYTSHVLMATDDACIPGYRRVAEACHAEGCVVLSQIFHPGREIMESADGLLAVAYSASASPNERFRVMPRELDQPLIDEIVAGYAAAARRLHQAGLDGVEVVASHGYLPAQFLNPRVNRRTDGYNGDLDARLRFLREVLAAVRAATSEDFIVGLRLSADERDPEGLSESESLQAAEAVQGELDYLHIVAGTSASLGGAIHIVPPMAIEPAYLAREASTFKARLAIPLFVTGRINQPQEAEAILARGQADVCGMTRALICDPQMPNKAEAGRSDDVRACIACNQACIGHFHRGYPISCIQHPETGRELTYATPNPASRRKRVLVAGGGPAGMKAAAVAAQRGHEVVLCEAGAQLGGQVNLAQLLPRRAEFGGASTNLQREMQLAGVEVRRNTPVDRALVERERPDLVIVATGAEPYWPPFERGGELQVVDAWQVLRGEVRVGRSVLVTDWRGDWIGPGIAEKLVREGHQVRLAVNGTHCGESLPLYVRDQLAGELHRLGIPVTPYARLYGCDDTTVYMQHSASGEAMLFEEVDTLVLCQGHQPVDRLADSLHGLAEVLRIGDCLAPRTAEEAIYEGLKAAWSI

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

6 GO

Gene Ontology (GO)

GO:0008670 Catalysis of the reactions: a 4,5-saturated-(2E)-enoyl-CoA + NADP+ = a (2E,4E)-dienoyl-CoA + H+ + NADPH, and a (2E,4Z)-dienoyl-CoA + H+ + NADPH = a 4,5-saturated-(2E)-enoyl-CoA + NADP+.
GO:0010181 Binding to flavin mono nucleotide. Flavin mono nucleotide (FMN) is the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes.
GO:0051536 Binding to an iron-sulfur cluster, a combination of iron and sulfur atoms.
GO:0046872 Binding to a metal ion.
GO:0033543 A fatty acid beta-oxidation pathway by which fatty acids having cis-double bonds on even-numbered carbons are degraded. In this pathway, the intermediate 2,4-dienoyl-CoA is converted to trans-2-enoyl-CoA by 2,4-dienoyl-CoA reductase and delta3-delta2-enoyl-CoA isomerase; trans-2-enoyl-CoA returns to the core beta-oxidation pathway for further degradation. Fatty acid beta-oxidation begins with the addition of coenzyme A to a fatty acid, and ends when only two or three carbons remain (as acetyl-CoA or propionyl-CoA respectively).
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.

16 records

Show feature table

Start	End	DB	Term	Name
469	487	PRINTS	PR00368	FAD-dependent pyridine nucleotide reductase signature
387	406	PRINTS	PR00368	FAD-dependent pyridine nucleotide reductase signature
385	614	Pfam	PF07992	Pyridine nucleotide-disulphide oxidoreductase
385	614	InterPro	IPR023753	FAD/NAD(P)-binding domain
1	368	SUPERFAMILY	SSF51395	FMN-linked oxidoreductases
1	534	PANTHER	PTHR42917	2,4-DIENOYL-COA REDUCTASE
6	339	Pfam	PF00724	NADH:flavin oxidoreductase / NADH oxidase family
6	339	InterPro	IPR001155	NADH:flavin oxidoreductase/NADH oxidase, N-terminal
6	348	CDD	cd04734	OYE_like_3_FMN
386	641	Gene3D	G3DSA:3.40.50.720	-
481	605	Gene3D	G3DSA:3.50.50.60	-
481	605	InterPro	IPR036188	FAD/NAD(P)-binding domain superfamily
363	648	SUPERFAMILY	SSF51905	FAD/NAD(P)-binding domain
363	648	InterPro	IPR036188	FAD/NAD(P)-binding domain superfamily
1	380	Gene3D	G3DSA:3.20.20.70	Aldolase class I
1	380	InterPro	IPR013785	Aldolase-type TIM barrel

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.

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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 PA4986	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

0.694

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Site 2 FPocket #2

0.534

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Site 3 FPocket #19

0.306

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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.

3 records

Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 3 via homologs

Structural ligands 3 0 loaded crystals

Bioactive compounds 0 0 ZINC proposed compounds

Drug-like & clean 1 0 PAINS alerts

Best available ligand signal

FLC PDB via homolog 189.1 Da · LogP -5.25 · TPSA 140.6 Open detail RCSB PDB

Detail RCSB PDB FLC PDB via homolog

Detail RCSB PDB J5H PDB via homolog

Detail RCSB PDB MDE 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
FLC RCSB PDB	6L6J	A0A0L8AFM7	189.1 Da LogP -5.25 TPSA 140.6	✓ Ro5	✓ Clean	`C(C(=O)[O-])C(CC(=O)[O-])(C(=O)[O-])O`
J5H RCSB PDB	6QKR	E1YD54	921.7 Da LogP 1.13 TPSA 363.6	3 viol.	✓ Clean	`CC(C)(COP(=O)(O)OP(=O)(O)OC[C@@H]1[C@H]([C@H]([…`
MDE RCSB PDB	1PS9	P42593	994.9 Da LogP 0.91 TPSA 382.6	3 viol.	✓ Clean	`CCCCC[C@@H](C\C=C\C(=O)SCCNC(=O)CCNC(C(=O)C(C)(…`

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.