Target Pathogen

Overview

Basic information about this protein and its source genome.

Accession: PA2008
Assembly: Pseudomonas aeruginosa PAO1, complete genome
Gene: PA2008 fahA
Status: annotated
Amino acids: 432
Structure source: AlphaFold

EC

3.7.1.2

GO

GO:0004334 Catalysis of the reaction: 4-fumarylacetoacetate + H2O = acetoacetate + fumarate + H+. GO:0046872 Binding to a metal ion. GO:1902000 The chemical reactions and pathways resulting in the breakdown of homogentisate. GO:0006559 The chemical reactions and pathways resulting in the breakdown of L-phenylalanine. GO:0006572 The chemical reactions and pathways resulting in the breakdown of L-tyrosine. GO:0003824 Catalysis of a biochemical reaction at physiological temperatures. In biologically catalyzed reactions, the reactants are known as substrates, and the catalysts are naturally occurring macromolecular substances known as enzymes. Enzymes possess specific binding sites for substrates, and are usually composed wholly or largely of protein, but RNA that has catalytic activity (ribozyme) is often also regarded as enzymatic.

Target profile

Computed evidence for target prioritization.

Human off-target: hit
Human identity (%): 64.865
Human E-value: 4.55e-11
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 0.785

Structure –

Pocket –

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 7 GO

Enzyme Commission (EC)

1

3.7.1.2

Gene Ontology (GO)

7

GO:0004334 Catalysis of the reaction: 4-fumarylacetoacetate + H2O = acetoacetate + fumarate + H+.
GO:0046872 Binding to a metal ion.
GO:1902000 The chemical reactions and pathways resulting in the breakdown of homogentisate.
GO:0006559 The chemical reactions and pathways resulting in the breakdown of L-phenylalanine.
GO:0006572 The chemical reactions and pathways resulting in the breakdown of L-tyrosine.
GO:0003824 Catalysis of a biochemical reaction at physiological temperatures. In biologically catalyzed reactions, the reactants are known as substrates, and the catalysts are naturally occurring macromolecular substances known as enzymes. Enzymes possess specific binding sites for substrates, and are usually composed wholly or largely of protein, but RNA that has catalytic activity (ribozyme) is often also regarded as enzymatic.
GO:0009072 The chemical reactions and pathways involving aromatic amino acid family, amino acids with aromatic ring (phenylalanine, tyrosine, tryptophan).

Sequence Features

Domain/signature hits from InterPro and related databases.

17 records

Show feature table

Start	End	DB	Term	Name
117	427	Gene3D	G3DSA:3.90.850.10	-
117	427	InterPro	IPR036663	Fumarylacetoacetase-like, C-terminal domain superfamily
23	119	Pfam	PF09298	Fumarylacetoacetase N-terminal
23	119	InterPro	IPR015377	Fumarylacetoacetase, N-terminal
121	425	SUPERFAMILY	SSF56529	FAH
121	425	InterPro	IPR036663	Fumarylacetoacetase-like, C-terminal domain superfamily
117	428	FunFam	G3DSA:3.90.850.10:FF:000009	Fumarylacetoacetase
8	119	SUPERFAMILY	SSF63433	Fumarylacetoacetate hydrolase, FAH, N-terminal domain
8	119	InterPro	IPR036462	Fumarylacetoacetase, N-terminal domain superfamily
2	116	Gene3D	G3DSA:2.30.30.230	-
2	116	InterPro	IPR036462	Fumarylacetoacetase, N-terminal domain superfamily
126	423	Pfam	PF01557	Fumarylacetoacetate (FAA) hydrolase family
126	423	InterPro	IPR011234	Fumarylacetoacetase-like, C-terminal
9	426	PANTHER	PTHR43069	FUMARYLACETOACETASE
9	426	InterPro	IPR005959	Fumarylacetoacetase
9	427	NCBIfam	TIGR01266	fumarylacetoacetase
9	427	InterPro	IPR005959	Fumarylacetoacetase

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 PA2008	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				0.785

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.

17 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
AAE	1QCO	P35505	102.1 Da LogP 0.05 TPSA 54.4	✓ Ro5	✓ Clean	`CC(=O)CC(=O)O`
CAC	1QQJ	P35505	137.0 Da LogP -0.52 TPSA 40.1	✓ Ro5	✓ Clean	`C[As](=O)(C)[O-]`
DHJ	2HZY	P35505	238.1 Da LogP -0.22 TPSA 129.0	✓ Ro5	✓ Clean	`C(C[P@](=O)(CC(=O)CC(=O)O)O)C(=O)O`
FUM	1QCO	P35505	116.1 Da LogP -0.29 TPSA 74.6	✓ Ro5	✓ Clean	`C(=C/C(=O)O)\C(=O)O`
HBU	1HYO	P35505	180.1 Da LogP -0.07 TPSA 91.7	✓ Ro5	✓ Clean	`C[P@](=O)(CC(=O)CC(=O)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
DWT	P16930	7.56	503.5 Da LogP 5.75 TPSA 97.6	2 viol.	✓ Clean	`Cc1ccc(cc1Nc2c3cn(nc3nc(n2)c4cccnc4)C)C(=O)Nc5c…`

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
ZINC3165652	0.652	210.1 Da LogP 0.21 TPSA 111.9	✓ Ro5	✓ Clean	`O=C(O)CCP(=O)(O)CCC(=O)O`
ZINC220133900	0.538	398.3 Da LogP 3.77 TPSA 85.1	✓ Ro5	✓ Clean	`Cc1nc2nc(-c3cccnc3)nn2cc1C(=O)Nc1cccc(C(F)(F)F)…`
ZINC3115751	0.533	239.2 Da LogP -0.25 TPSA 123.9	✓ Ro5	✓ Clean	`O=C(O)CCNC[P@](=O)(O)CCC(=O)O`
ZINC20148987	0.532	414.4 Da LogP 4.50 TPSA 97.1	✓ Ro5	✓ Clean	`Cc1ccc(C(=O)Nc2cccc(C(F)(F)F)c2)cc1Nc1cncc(C(N)…`
ZINC9306398	0.512	398.3 Da LogP 3.77 TPSA 85.1	✓ Ro5	✓ Clean	`Cc1c(C(=O)Nc2cccc(C(F)(F)F)c2)cnc2nc(-c3cccnc3)…`
ZINC5049572	0.507	336.3 Da LogP 4.22 TPSA 58.2	✓ Ro5	✓ Clean	`CC(=O)Nc1cc(C(=O)Nc2cccc(C(F)(F)F)c2)ccc1C`
ZINC100473925	0.500	256.2 Da LogP -1.50 TPSA 132.8	✓ Ro5	✓ Clean	`O=C(O)/C=C\C(=O)NCCNC(=O)/C=C\C(=O)O`
ZINC1679042	0.500	256.2 Da LogP -1.50 TPSA 132.8	✓ Ro5	✓ Clean	`O=C(O)/C=C/C(=O)NCCNC(=O)/C=C/C(=O)O`
ZINC4866352	0.500	282.3 Da LogP -1.06 TPSA 115.2	✓ Ro5	✓ Clean	`O=C(O)/C=C/C(=O)N1CCN(C(=O)/C=C/C(=O)O)CC1`
ZINC8616656	0.500	256.2 Da LogP -1.50 TPSA 132.8	✓ Ro5	✓ Clean	`O=C(O)C=CC(=O)NCCNC(=O)C=CC(=O)O`
ZINC90623560	0.500	256.2 Da LogP -1.50 TPSA 132.8	✓ Ro5	✓ Clean	`O=C(O)/C=C\C(=O)NCCNC(=O)/C=C/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.

PA2008