Protein target profile

PA3166

bifunctional chorismate mutase/prephenate dehydratase

Genome: NC_002516.2

Gene: pheA PA3166 3D evidence: AlphaFold DB model UniProt Q9HZ67

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Length 365

Pocket druggability 0.716

Ligand records 52

EC / GO 0 / 5

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: PA3166
Assembly: Pseudomonas aeruginosa PAO1, complete genome
Gene: pheA PA3166
Status: annotated
Amino acids: 365
3D evidence: AlphaFold DB model

GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. GO:0004106 Catalysis of the reaction: chorismate = prephenate. GO:0004664 Catalysis of the reaction: prephenate = phenylpyruvate + H2O + CO2. GO:0046417 The chemical reactions and pathways involving chorismate, the anion of (3R-trans)-3-((1-carboxyethenyl)oxy)-4-hydroxy-1,5-cyclohexadiene-1-carboxylic acid. GO:0009094 The chemical reactions and pathways resulting in the formation of L-phenylalanine, the L-enantiomer of 2-amino-3-phenylpropanoic acid, i.e. (2S)-2-amino-3-phenylpropanoic acid.

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 0.716

Structure –

Pocket –

Sequence

Primary amino-acid sequence viewer.

MADQDQLKALRLRIDSLDEKLLELISERARCAQDVARVKTQTLGEGEAPVFYRPEREAWVLKHIMQLNKGPLDNEEVARLFREIMSSCLALEQPLKVAYLGPEGTFTQAAALKHFGNAVISTPMAAIDEVFREVAAGAVNFGVVPVENSTEGAVNHTLDSFLEHDMVICGEVELRIHHHLLVGETTKTDNITRIYSHAQSLAQCRKWLDSHYPSVERVAVSSNADAAKRVKSEWNSAAIAGDMAASLYDLSKLHEKIEDRPDNSTRFLIIGNQEVPPTGDDKTSIIVSMRNKPGALHELLVPFHNNGIDLTRIETRPSRSGKWTYVFFIDFVGHHKEPLIKDVLEKIGQEAVALKVLGSYPKAVL

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

5 GO

Gene Ontology (GO)

GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
GO:0004106 Catalysis of the reaction: chorismate = prephenate.
GO:0004664 Catalysis of the reaction: prephenate = phenylpyruvate + H2O + CO2.
GO:0046417 The chemical reactions and pathways involving chorismate, the anion of (3R-trans)-3-((1-carboxyethenyl)oxy)-4-hydroxy-1,5-cyclohexadiene-1-carboxylic acid.
GO:0009094 The chemical reactions and pathways resulting in the formation of L-phenylalanine, the L-enantiomer of 2-amino-3-phenylpropanoic acid, i.e. (2S)-2-amino-3-phenylpropanoic acid.

Sequence Features

Domain/signature hits from InterPro and related databases.

40 records

Show feature table

Start	End	DB	Term	Name
96	281	SUPERFAMILY	SSF53850	Periplasmic binding protein-like II
310	317	ProSitePatterns	PS00858	Prephenate dehydratase signature 2.
310	317	InterPro	IPR018528	Prephenate dehydratase, conserved site
99	270	Gene3D	G3DSA:3.40.190.10	-
284	361	ProSiteProfiles	PS51671	ACT domain profile.
284	361	InterPro	IPR002912	ACT domain
248	270	ProSitePatterns	PS00857	Prephenate dehydratase signature 1.
248	270	InterPro	IPR018528	Prephenate dehydratase, conserved site
96	272	ProSiteProfiles	PS51171	Prephenate dehydratase domain profile.
96	272	InterPro	IPR001086	Prephenate dehydratase
177	261	Gene3D	G3DSA:3.40.190.10	-
1	365	PIRSF	PIRSF001500	Chor_mut_pdt_Ppr
1	365	InterPro	IPR008242	Bifunctional P-protein, chorismate mutase/prephenate dehydratase
275	364	Gene3D	G3DSA:3.30.70.260	-
180	261	FunFam	G3DSA:3.40.190.10:FF:000034	Chorismate mutase/prephenate dehydratase
6	99	SUPERFAMILY	SSF48600	Chorismate mutase II
6	99	InterPro	IPR036263	Chorismate mutase type II superfamily
7	27	Coils	Coil	Coil
76	361	PANTHER	PTHR21022	PREPHENATE DEHYDRATASE P PROTEIN
99	179	FunFam	G3DSA:3.40.190.10:FF:000029	Chorismate mutase/Prephenate dehydratase
283	348	Pfam	PF01842	ACT domain
283	348	InterPro	IPR002912	ACT domain
94	274	CDD	cd13630	PBP2_PDT_1
275	365	FunFam	G3DSA:3.30.70.260:FF:000012	Prephenate dehydratase
11	95	SMART	SM00830	CM_2_4
11	95	InterPro	IPR002701	Chorismate mutase II, prokaryotic-type
7	85	NCBIfam	TIGR01807	chorismate mutase
7	85	InterPro	IPR010957	Gamma/beta/epsilon proteobacterial P-protein, chorismate mutase domain
282	361	CDD	cd04905	ACT_CM-PDT
5	96	FunFam	G3DSA:1.20.59.10:FF:000004	Prephenate dehydratase
97	274	Pfam	PF00800	Prephenate dehydratase
97	274	InterPro	IPR001086	Prephenate dehydratase
4	97	Gene3D	G3DSA:1.20.59.10	Chorismate mutase
4	97	InterPro	IPR036979	Chorismate mutase domain superfamily
267	362	SUPERFAMILY	SSF55021	ACT-like
267	362	InterPro	IPR045865	ACT-like domain
11	93	Pfam	PF01817	Chorismate mutase type II
11	93	InterPro	IPR002701	Chorismate mutase II, prokaryotic-type
1	96	ProSiteProfiles	PS51168	Chorismate mutase domain profile.
1	96	InterPro	IPR002701	Chorismate mutase II, prokaryotic-type

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 PA3166	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

0.716

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Site 2 FPocket #8

0.439

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Site 3 FPocket #2

0.419

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Site 4 FPocket #4

0.316

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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.

52 records

Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 52 via homologs

Structural ligands 2 0 loaded crystals

Bioactive compounds 0 50 ZINC proposed compounds

Drug-like & clean 50 2 PAINS alerts

Best available ligand signal

7LH PDB via homolog 356.3 Da · LogP -0.73 · TPSA 164.8 Open detail RCSB PDB

Detail RCSB PDB 7LH PDB via homolog

Detail RCSB PDB TSA PDB via homolog

Detail ZINC ZINC113264413 ZINC proposed compound · Tanimoto 0.778

Detail ZINC ZINC113264415 ZINC proposed compound · Tanimoto 0.778

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
7LH RCSB PDB	5GMU	P39912	356.3 Da LogP -0.73 TPSA 164.8	1 viol.	Alert	`c1cc(c(cc1CCC(=O)O[C@@H]2C[C@](C[C@H]([C@@H]2O)…`
TSA RCSB PDB	1ECM	P0A9J8	228.2 Da LogP -0.38 TPSA 104.1	✓ Ro5	✓ Clean	`C1[C@@H]2[C@@H](C=C[C@]1(C[C@H](O2)C(=O)O)C(=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
ZINC113264413 ZINC	0.778	317.4 Da LogP 3.98 TPSA 63.3	✓ Ro5	✓ Clean	`N[C@@H](Cc1ccc(-c2ccc(-c3ccccc3)cc2)cc1)C(=O)O`
ZINC113264415 ZINC	0.778	317.4 Da LogP 3.98 TPSA 63.3	✓ Ro5	✓ Clean	`N[C@H](Cc1ccc(-c2ccc(-c3ccccc3)cc2)cc1)C(=O)O`
ZINC2244337 ZINC	0.778	241.3 Da LogP 2.31 TPSA 63.3	✓ Ro5	✓ Clean	`N[C@@H](Cc1ccc(-c2ccccc2)cc1)C(=O)O`
ZINC2244338 ZINC	0.778	241.3 Da LogP 2.31 TPSA 63.3	✓ Ro5	✓ Clean	`N[C@H](Cc1ccc(-c2ccccc2)cc1)C(=O)O`
ZINC1834294 ZINC	0.769	252.3 Da LogP -0.40 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@@H](Cc1cccc(C[C@H](N)C(=O)O)c1)C(=O)O`
ZINC1834295 ZINC	0.769	252.3 Da LogP -0.40 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@@H](Cc1cccc(C[C@@H](N)C(=O)O)c1)C(=O)O`
ZINC1834297 ZINC	0.769	252.3 Da LogP -0.40 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@H](Cc1cccc(C[C@@H](N)C(=O)O)c1)C(=O)O`
ZINC39351856 ZINC	0.731	328.4 Da LogP 1.26 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@@H](Cc1ccc(-c2ccc(C[C@H](N)C(=O)O)cc2)cc1)C…`
ZINC2561081 ZINC	0.724	269.3 Da LogP 1.87 TPSA 80.4	✓ Ro5	✓ Clean	`N[C@H](Cc1ccc(C(=O)c2ccccc2)cc1)C(=O)O`
ZINC2561082 ZINC	0.724	269.3 Da LogP 1.87 TPSA 80.4	✓ Ro5	✓ Clean	`N[C@@H](Cc1ccc(C(=O)c2ccccc2)cc1)C(=O)O`
ZINC113539705 ZINC	0.700	265.3 Da LogP 2.04 TPSA 63.3	✓ Ro5	✓ Clean	`N[C@@H](Cc1ccc(C#Cc2ccccc2)cc1)C(=O)O`
ZINC113539708 ZINC	0.700	265.3 Da LogP 2.04 TPSA 63.3	✓ Ro5	✓ Clean	`N[C@H](Cc1ccc(C#Cc2ccccc2)cc1)C(=O)O`
ZINC116910786 ZINC	0.700	269.3 Da LogP 3.06 TPSA 88.0	✓ Ro5	Alert	`N[C@@H](Cc1ccc(/N=N/c2ccccc2)cc1)C(=O)O`
ZINC1532902 ZINC	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 ZINC	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`
ZINC29566843 ZINC	0.700	241.3 Da LogP 2.31 TPSA 63.3	✓ Ro5	✓ Clean	`N[C@H](Cc1cccc(-c2ccccc2)c1)C(=O)O`
ZINC29570997 ZINC	0.700	241.3 Da LogP 2.31 TPSA 63.3	✓ Ro5	✓ Clean	`N[C@@H](Cc1cccc(-c2ccccc2)c1)C(=O)O`
ZINC44283581 ZINC	0.700	257.3 Da LogP 2.43 TPSA 72.5	✓ Ro5	✓ Clean	`N[C@@H](Cc1ccc(Oc2ccccc2)cc1)C(=O)O`
ZINC44283583 ZINC	0.700	257.3 Da LogP 2.43 TPSA 72.5	✓ Ro5	✓ Clean	`N[C@H](Cc1ccc(Oc2ccccc2)cc1)C(=O)O`
ZINC2111574 ZINC	0.692	252.3 Da LogP -0.40 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@@H](Cc1ccccc1C[C@H](N)C(=O)O)C(=O)O`
ZINC2111575 ZINC	0.692	252.3 Da LogP -0.40 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@@H](Cc1ccccc1C[C@@H](N)C(=O)O)C(=O)O`
ZINC2111578 ZINC	0.692	252.3 Da LogP -0.40 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@H](Cc1ccccc1C[C@@H](N)C(=O)O)C(=O)O`
ZINC12648269 ZINC	0.690	237.3 Da LogP 0.73 TPSA 100.6	✓ Ro5	✓ Clean	`N[C@H](C[C@@H](Cc1ccccc1)C(=O)O)C(=O)O`
ZINC1616445 ZINC	0.690	354.5 Da LogP 0.36 TPSA 110.2	✓ Ro5	✓ Clean	`N[C@@H](Cc1ccccc1)C(=O)NCCNC(=O)[C@H](N)Cc1cccc…`
ZINC1616446 ZINC	0.690	354.5 Da LogP 0.36 TPSA 110.2	✓ Ro5	✓ Clean	`N[C@H](Cc1ccccc1)C(=O)NCCNC(=O)[C@H](N)Cc1ccccc1`
ZINC1616447 ZINC	0.690	354.5 Da LogP 0.36 TPSA 110.2	✓ Ro5	✓ Clean	`N[C@@H](Cc1ccccc1)C(=O)NCCNC(=O)[C@@H](N)Cc1ccc…`
ZINC5225893 ZINC	0.690	237.3 Da LogP 0.73 TPSA 100.6	✓ Ro5	✓ Clean	`N[C@@H](C[C@H](Cc1ccccc1)C(=O)O)C(=O)O`
ZINC133159 ZINC	0.688	271.3 Da LogP 2.22 TPSA 72.5	✓ Ro5	✓ Clean	`N[C@@H](Cc1ccc(OCc2ccccc2)cc1)C(=O)O`
ZINC133162 ZINC	0.688	271.3 Da LogP 2.22 TPSA 72.5	✓ Ro5	✓ Clean	`N[C@H](Cc1ccc(OCc2ccccc2)cc1)C(=O)O`
ZINC32333 ZINC	0.679	244.1 Da LogP 1.40 TPSA 63.3	✓ Ro5	✓ Clean	`N[C@@H](Cc1ccc(Br)cc1)C(=O)O`
ZINC32334 ZINC	0.679	244.1 Da LogP 1.40 TPSA 63.3	✓ Ro5	✓ Clean	`N[C@H](Cc1ccc(Br)cc1)C(=O)O`
ZINC3679925 ZINC	0.679	291.1 Da LogP 1.25 TPSA 63.3	✓ Ro5	✓ Clean	`N[C@H](Cc1ccc(I)cc1)C(=O)O`
ZINC391104 ZINC	0.679	291.1 Da LogP 1.25 TPSA 63.3	✓ Ro5	✓ Clean	`N[C@@H](Cc1ccc(I)cc1)C(=O)O`
ZINC4202286 ZINC	0.679	209.2 Da LogP 0.34 TPSA 100.6	✓ Ro5	✓ Clean	`N[C@@H](Cc1ccc(C(=O)O)cc1)C(=O)O`
ZINC4202287 ZINC	0.679	209.2 Da LogP 0.34 TPSA 100.6	✓ Ro5	✓ Clean	`N[C@H](Cc1ccc(C(=O)O)cc1)C(=O)O`
ZINC6092920 ZINC	0.679	223.2 Da LogP 0.27 TPSA 100.6	✓ Ro5	✓ Clean	`N[C@@H](Cc1ccc(CC(=O)O)cc1)C(=O)O`
ZINC6506146 ZINC	0.679	223.2 Da LogP 0.27 TPSA 100.6	✓ Ro5	✓ Clean	`N[C@H](Cc1ccc(CC(=O)O)cc1)C(=O)O`
ZINC6580731 ZINC	0.679	225.3 Da LogP 2.44 TPSA 43.1	✓ Ro5	✓ Clean	`N[C@H](Cc1ccccc1)C(=O)c1ccccc1`
ZINC90624143 ZINC	0.679	225.3 Da LogP 2.44 TPSA 43.1	✓ Ro5	✓ Clean	`N[C@@H](Cc1ccccc1)C(=O)c1ccccc1`
ZINC54918280 ZINC	0.667	254.3 Da LogP 1.87 TPSA 55.1	✓ Ro5	✓ Clean	`N[C@@H](Cc1ccccc1)C(=O)NCc1ccccc1`
ZINC54918281 ZINC	0.667	254.3 Da LogP 1.87 TPSA 55.1	✓ Ro5	✓ Clean	`N[C@H](Cc1ccccc1)C(=O)NCc1ccccc1`
ZINC14982778 ZINC	0.655	207.2 Da LogP 0.84 TPSA 80.4	✓ Ro5	✓ Clean	`CC(=O)c1ccc(C[C@@H](N)C(=O)O)cc1`
ZINC14982780 ZINC	0.655	207.2 Da LogP 0.84 TPSA 80.4	✓ Ro5	✓ Clean	`CC(=O)c1ccc(C[C@H](N)C(=O)O)cc1`
ZINC156948 ZINC	0.655	255.3 Da LogP 2.30 TPSA 52.3	✓ Ro5	✓ Clean	`N[C@@H](Cc1ccccc1)C(=O)OCc1ccccc1`
ZINC2575618 ZINC	0.655	208.2 Da LogP -0.26 TPSA 106.4	✓ Ro5	✓ Clean	`NC(=O)c1ccc(C[C@H](N)C(=O)O)cc1`
ZINC391855 ZINC	0.655	255.3 Da LogP 2.30 TPSA 52.3	✓ Ro5	✓ Clean	`N[C@H](Cc1ccccc1)C(=O)OCc1ccccc1`
ZINC4241956 ZINC	0.655	208.2 Da LogP -0.26 TPSA 106.4	✓ Ro5	✓ Clean	`NC(=O)c1ccc(C[C@@H](N)C(=O)O)cc1`
ZINC3593496 ZINC	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 ZINC	0.652	206.2 Da LogP -1.16 TPSA 121.1	✓ Ro5	✓ Clean	`COC(=O)C[C@](O)(CC(=O)O)C(=O)O`
ZINC128256 ZINC	0.645	215.3 Da LogP 1.79 TPSA 63.3	✓ Ro5	✓ Clean	`N[C@@H](Cc1ccc2ccccc2c1)C(=O)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.