Protein profile

PA2940

acyl-CoA thiolase

Genome: NC_002516.2

Gene: PA2940 Structure source: Experimental + AlphaFold UniProt Q9HZQ7

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Amino acids 379

Annotations 7

Features 22

PDB binders 11

Druggability 0.851

Overview

Basic information about this protein and its source genome.

Accession: PA2940
Assembly: Pseudomonas aeruginosa PAO1, complete genome
Gene: PA2940
Status: annotated
Amino acids: 379
Structure source: Experimental + AlphaFold

GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. GO:0033812 Catalysis of the reaction: succinyl-CoA + acetyl-CoA = CoA + 3-oxoadipyl-CoA. GO:0003988 Catalysis of the reaction: acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA. GO:0006635 A fatty acid oxidation process that results in the complete oxidation of a long-chain fatty acid. Fatty acid beta-oxidation begins with the addition of coenzyme A to a fatty acid, and occurs by successive cycles of reactions during each of which the fatty acid is shortened by a two-carbon fragment removed as acetyl coenzyme A; the cycle continues until only two or three carbons remain (as acetyl-CoA or propionyl-CoA respectively). GO:0010124 The chemical reactions and pathways resulting in the breakdown of phenylacetate. GO:0016746 Catalysis of the transfer of an acyl group from one compound (donor) to another (acceptor).

Target profile

Computed evidence for target prioritization.

Human off-target: hit
Human identity (%): 39.32
Human E-value: 3.4399999999999997e-34
Gut microbiome off-target: hit
Essential (DEG): Y
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 0.851

Structure –

Pocket –

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

7 GO

Gene Ontology (GO)

GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
GO:0033812 Catalysis of the reaction: succinyl-CoA + acetyl-CoA = CoA + 3-oxoadipyl-CoA.
GO:0003988 Catalysis of the reaction: acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA.
GO:0006635 A fatty acid oxidation process that results in the complete oxidation of a long-chain fatty acid. Fatty acid beta-oxidation begins with the addition of coenzyme A to a fatty acid, and occurs by successive cycles of reactions during each of which the fatty acid is shortened by a two-carbon fragment removed as acetyl coenzyme A; the cycle continues until only two or three carbons remain (as acetyl-CoA or propionyl-CoA respectively).
GO:0010124 The chemical reactions and pathways resulting in the breakdown of phenylacetate.
GO:0016746 Catalysis of the transfer of an acyl group from one compound (donor) to another (acceptor).
GO:0016747 Catalysis of the transfer of an acyl group, other than amino-acyl, from one compound (donor) to another (acceptor).

Sequence Features

Domain/signature hits from InterPro and related databases.

22 records

Show feature table

Start	End	DB	Term	Name
1	379	PIRSF	PIRSF000429	Ac-CoA_Ac_transf
1	379	InterPro	IPR002155	Thiolase
6	248	Pfam	PF00108	Thiolase, N-terminal domain
6	248	InterPro	IPR020616	Thiolase, N-terminal
324	340	ProSitePatterns	PS00737	Thiolases signature 2.
324	340	InterPro	IPR020613	Thiolase, conserved site
257	376	SUPERFAMILY	SSF53901	Thiolase-like
257	376	InterPro	IPR016039	Thiolase-like
4	379	Gene3D	G3DSA:3.40.47.10	-
4	379	InterPro	IPR016039	Thiolase-like
5	378	PANTHER	PTHR43853	3-KETOACYL-COA THIOLASE, PEROXISOMAL
88	106	ProSitePatterns	PS00098	Thiolases acyl-enzyme intermediate signature.
88	106	InterPro	IPR020615	Thiolase, acyl-enzyme intermediate active site
257	376	Pfam	PF02803	Thiolase, C-terminal domain
257	376	InterPro	IPR020617	Thiolase, C-terminal
7	377	CDD	cd00751	thiolase
7	377	InterPro	IPR002155	Thiolase
4	378	FunFam	G3DSA:3.40.47.10:FF:000010	Acetyl-CoA acetyltransferase (Thiolase)
5	253	SUPERFAMILY	SSF53901	Thiolase-like
5	253	InterPro	IPR016039	Thiolase-like
8	376	NCBIfam	TIGR01930	acetyl-CoA C-acyltransferase
8	376	InterPro	IPR002155	Thiolase

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...

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Structural evidence

2 + 1

Experimental PDB entries and predicted models. Click Switch to display a different structure in the viewer.

Entry	Method	Resolution	Chain	Coverage	Links	Status
PDB 8GQM	X-ray	1.45 Å	A	100.0% 1-379	PDBe RCSB PDBj File	Viewing
PDB 8GQF	X-ray	1.80 Å	A,B,C,D	100.0% 1-379	PDBe RCSB PDBj File	Loaded
AlphaFold PA2940	AlphaFold	—	—	full sequence	—	Loaded

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
2				0.851
1				0.441

Pockets (P2RANK)

Showing top-ranked P2Rank candidates by probability. Probability is color-coded per P2Rank calibration: high (≥ 0.5), medium (0.2 – 0.49), low (< 0.2).

P2RANK	Score	Probability
1	20.67	0.86
2	3.91	0.154
3	2.11	0.048
4	1.1	0.008

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
2				0.871
5				0.531

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.

61 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
168	1OU6	P07097	388.5 Da LogP 0.15 TPSA 131.0	✓ Ro5	✓ Clean	`CC(=O)OCCNC(=O)CCNC(=O)[C@@H](C(C)(C)COC(=O)C(C…`
3G6	4UBT	I6XHI4	344.5 Da LogP 4.86 TPSA 54.4	✓ Ro5	✓ Clean	`C[C@@H]([C@H]1CC[C@@H]2[C@@]1(CC[C@H]3[C@H]2CCC…`
5UG	5F38	P76461	438.3 Da LogP -0.85 TPSA 191.7	1 viol.	✓ Clean	`CC(C)(COP(=O)(O)OP(=O)(O)O)[C@@H](C(=O)NCCC(=O)…`
CAA	1M1O	P07097	851.6 Da LogP -1.36 TPSA 380.7	3 viol.	✓ Clean	`CC(=O)CC(=O)SCCNC(=O)CCNC(=O)[C@@H](C(C)(C)CO[P…`
COZ	5F38	P76461	767.5 Da LogP -1.67 TPSA 346.6	3 viol.	✓ Clean	`CC(C)(CO[P@](=O)(O)O[P@](=O)(O)OC[C@@H]1[C@H]([…`
DNO	2WKU	P07097	180.2 Da LogP -3.38 TPSA 118.2	✓ Ro5	✓ Clean	`C([C@H]([C@H]([C@@H]([C@@H](C=O)O)O)O)O)O`
DTT	4C2K	P42765	154.3 Da LogP -0.43 TPSA 40.5	✓ Ro5	✓ Clean	`C([C@@H]([C@H](CS)O)O)S`
O8Y	6PCC	Q88N39	100.2 Da LogP 1.77 TPSA 17.1	✓ Ro5	✓ Clean	`CCCCCC=O`
OPI	2VU1	P07097	346.4 Da LogP -0.42 TPSA 125.0	✓ Ro5	✓ Clean	`CC(C)(C)C(=O)OCC(C)(C)[C@H](C(=O)NCCC(=O)NCCO)O`
OYA	6PCD	Q88N39	128.2 Da LogP 2.55 TPSA 17.1	✓ Ro5	✓ Clean	`CCCCCCCC=O`
PN5	2VU2	P07097	362.5 Da LogP 0.52 TPSA 104.7	✓ Ro5	✓ Clean	`CC(C)(C)C(=O)OCC(C)(C)[C@H](C(=O)NCCC(=O)NCCS)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
ZINC4403984	1.000	344.5 Da LogP 4.86 TPSA 54.4	✓ Ro5	✓ Clean	`C[C@@H](C(=O)O)[C@H]1CC[C@H]2[C@@H]3CCC4=CC(=O)…`
ZINC5763280	1.000	344.5 Da LogP 4.86 TPSA 54.4	✓ Ro5	✓ Clean	`C[C@H](C(=O)O)[C@H]1CC[C@H]2[C@@H]3CCC4=CC(=O)C…`
ZINC100056793	0.950	210.2 Da LogP -4.02 TPSA 138.5	1 viol.	✓ Clean	`O=C[C@@H](O)[C@@H](O)[C@H](O)[C@H](O)[C@@H](O)CO`
ZINC100056796	0.950	210.2 Da LogP -4.02 TPSA 138.5	1 viol.	✓ Clean	`O=C[C@@H](O)[C@@H](O)[C@H](O)[C@H](O)[C@H](O)CO`
ZINC12953159	0.950	210.2 Da LogP -4.02 TPSA 138.5	1 viol.	✓ Clean	`O=C[C@H](O)[C@H](O)[C@H](O)[C@H](O)[C@@H](O)CO`
ZINC12953162	0.950	210.2 Da LogP -4.02 TPSA 138.5	1 viol.	✓ Clean	`O=C[C@H](O)[C@H](O)[C@H](O)[C@@H](O)[C@H](O)CO`
ZINC12953168	0.950	210.2 Da LogP -4.02 TPSA 138.5	1 viol.	✓ Clean	`O=C[C@H](O)[C@H](O)[C@H](O)[C@@H](O)[C@@H](O)CO`
ZINC13522675	0.950	210.2 Da LogP -4.02 TPSA 138.5	1 viol.	✓ Clean	`O=C[C@H](O)[C@H](O)[C@H](O)[C@H](O)[C@H](O)CO`
ZINC13522684	0.950	210.2 Da LogP -4.02 TPSA 138.5	1 viol.	✓ Clean	`O=C[C@@H](O)[C@H](O)[C@@H](O)[C@@H](O)[C@H](O)CO`
ZINC4353166	0.950	240.2 Da LogP -4.66 TPSA 158.7	1 viol.	✓ Clean	`O=C[C@@H](O)[C@@H](O)[C@@H](O)[C@@H](O)[C@@H](O…`
ZINC4353167	0.950	240.2 Da LogP -4.66 TPSA 158.7	1 viol.	✓ Clean	`O=C[C@@H](O)[C@@H](O)[C@@H](O)[C@@H](O)[C@@H](O…`
ZINC4353168	0.950	240.2 Da LogP -4.66 TPSA 158.7	1 viol.	✓ Clean	`O=C[C@@H](O)[C@@H](O)[C@@H](O)[C@@H](O)[C@H](O)…`
ZINC4353169	0.950	240.2 Da LogP -4.66 TPSA 158.7	1 viol.	✓ Clean	`O=C[C@@H](O)[C@@H](O)[C@@H](O)[C@@H](O)[C@H](O)…`
ZINC4353180	0.950	210.2 Da LogP -4.02 TPSA 138.5	1 viol.	✓ Clean	`O=C[C@@H](O)[C@@H](O)[C@@H](O)[C@@H](O)[C@@H](O…`
ZINC4353181	0.950	210.2 Da LogP -4.02 TPSA 138.5	1 viol.	✓ Clean	`O=C[C@@H](O)[C@@H](O)[C@@H](O)[C@@H](O)[C@H](O)…`
ZINC4353182	0.950	210.2 Da LogP -4.02 TPSA 138.5	1 viol.	✓ Clean	`O=C[C@@H](O)[C@@H](O)[C@@H](O)[C@H](O)[C@@H](O)…`
ZINC95884213	0.950	210.2 Da LogP -4.02 TPSA 138.5	1 viol.	✓ Clean	`O=C[C@@H](O)[C@H](O)[C@H](O)[C@@H](O)[C@@H](O)CO`
ZINC9915770	0.950	210.2 Da LogP -4.02 TPSA 138.5	1 viol.	✓ Clean	`O=C[C@H](O)[C@H](O)[C@@H](O)[C@H](O)[C@H](O)CO`
ZINC9915771	0.950	210.2 Da LogP -4.02 TPSA 138.5	1 viol.	✓ Clean	`O=C[C@@H](O)[C@@H](O)[C@@H](O)[C@H](O)[C@H](O)CO`
ZINC1693894	0.938	212.4 Da LogP 4.89 TPSA 17.1	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCC=O`
ZINC13542964	0.796	316.5 Da LogP 4.52 TPSA 37.3	✓ Ro5	✓ Clean	`C[C@@H](O)[C@H]1CC[C@H]2[C@@H]3CCC4=CC(=O)CC[C@…`
ZINC253497962	0.796	316.5 Da LogP 4.52 TPSA 37.3	✓ Ro5	✓ Clean	`C[C@@H](O)[C@@H]1CC[C@@H]2[C@H]3CCC4=CC(=O)CC[C…`
ZINC253497963	0.796	316.5 Da LogP 4.52 TPSA 37.3	✓ Ro5	✓ Clean	`C[C@H](O)[C@@H]1CC[C@@H]2[C@H]3CCC4=CC(=O)CC[C@…`
ZINC2539736	0.796	316.5 Da LogP 4.52 TPSA 37.3	✓ Ro5	✓ Clean	`C[C@@H](O)[C@@H]1CC[C@H]2[C@@H]3CCC4=CC(=O)CC[C…`
ZINC36323232	0.796	316.5 Da LogP 4.52 TPSA 37.3	✓ Ro5	✓ Clean	`C[C@@H](O)[C@@H]1CC[C@@H]2[C@H]3CCC4=CC(=O)CC[C…`
ZINC3875971	0.796	316.5 Da LogP 4.52 TPSA 37.3	✓ Ro5	✓ Clean	`C[C@H](O)[C@H]1CC[C@H]2[C@@H]3CCC4=CC(=O)CC[C@]…`
ZINC4096295	0.796	316.5 Da LogP 4.52 TPSA 37.3	✓ Ro5	✓ Clean	`C[C@H](O)[C@@H]1CC[C@@H]2[C@H]3CCC4=CC(=O)CC[C@…`
ZINC968170	0.796	316.5 Da LogP 4.52 TPSA 37.3	✓ Ro5	✓ Clean	`C[C@H](O)[C@@H]1CC[C@H]2[C@@H]3CCC4=CC(=O)CC[C@…`
ZINC43061660	0.789	210.4 Da LogP 4.66 TPSA 17.1	✓ Ro5	✓ Clean	`CCCCCC/C=C\CCCCCC=O`
ZINC43061664	0.789	210.4 Da LogP 4.66 TPSA 17.1	✓ Ro5	✓ Clean	`CCCCCC/C=C/CCCCCC=O`
ZINC13540558	0.750	330.5 Da LogP 4.76 TPSA 37.3	✓ Ro5	✓ Clean	`C[C@H](CO)[C@H]1CC[C@H]2[C@@H]3CCC4=CC(=O)CC[C@…`
ZINC1848438168	0.750	330.5 Da LogP 4.76 TPSA 37.3	✓ Ro5	✓ Clean	`C[C@H](CO)[C@H]1CC[C@@H]2[C@@H]3CCC4=CC(=O)CC[C…`
ZINC1848438169	0.750	330.5 Da LogP 4.76 TPSA 37.3	✓ Ro5	✓ Clean	`C[C@@H](CO)[C@H]1CC[C@@H]2[C@@H]3CCC4=CC(=O)CC[…`
ZINC256518048	0.750	330.5 Da LogP 4.76 TPSA 37.3	✓ Ro5	✓ Clean	`C[C@H](CO)[C@@H]1CC[C@@H]2[C@H]3CCC4=CC(=O)CC[C…`
ZINC257359313	0.750	330.5 Da LogP 4.76 TPSA 37.3	✓ Ro5	✓ Clean	`C[C@H](CO)[C@@H]1CC[C@@H]2[C@@H]3CCC4=CC(=O)CC[…`
ZINC257359314	0.750	330.5 Da LogP 4.76 TPSA 37.3	✓ Ro5	✓ Clean	`C[C@H](CO)[C@@H]1CC[C@@H]2[C@@H]3CCC4=CC(=O)CC[…`
ZINC257359315	0.750	330.5 Da LogP 4.76 TPSA 37.3	✓ Ro5	✓ Clean	`C[C@H](CO)[C@@H]1CC[C@@H]2[C@H]3CCC4=CC(=O)CC[C…`
ZINC13759936	0.731	328.5 Da LogP 4.97 TPSA 34.1	✓ Ro5	✓ Clean	`C[C@@H](C=O)[C@H]1CC[C@H]2[C@@H]3CCC4=CC(=O)CC[…`
ZINC1700147	0.731	328.5 Da LogP 4.97 TPSA 34.1	✓ Ro5	✓ Clean	`C[C@H](C=O)[C@@H]1CC[C@H]2[C@@H]3CCC4=CC(=O)CC[…`
ZINC2042904	0.731	328.5 Da LogP 4.97 TPSA 34.1	✓ Ro5	✓ Clean	`C[C@@H](C=O)[C@@H]1CC[C@H]2[C@@H]3CCC4=CC(=O)CC…`
ZINC255004289	0.731	328.5 Da LogP 4.97 TPSA 34.1	✓ Ro5	✓ Clean	`C[C@H](C=O)[C@@H]1CC[C@@H]2[C@H]3CCC4=CC(=O)CC[…`
ZINC255004290	0.731	328.5 Da LogP 4.97 TPSA 34.1	✓ Ro5	✓ Clean	`C[C@@H](C=O)[C@@H]1CC[C@@H]2[C@H]3CCC4=CC(=O)CC…`
ZINC255004291	0.731	328.5 Da LogP 4.97 TPSA 34.1	✓ Ro5	✓ Clean	`C[C@H](C=O)[C@@H]1CC[C@@H]2[C@H]3CCC4=CC(=O)CC[…`
ZINC36323209	0.731	328.5 Da LogP 4.97 TPSA 34.1	✓ Ro5	✓ Clean	`C[C@@H](C=O)[C@@H]1CC[C@@H]2[C@H]3CCC4=CC(=O)CC…`
ZINC4416476	0.731	328.5 Da LogP 4.97 TPSA 34.1	✓ Ro5	✓ Clean	`C[C@H](C=O)[C@H]1CC[C@H]2[C@@H]3CCC4=CC(=O)CC[C…`
ZINC245224552	0.706	316.4 Da LogP 4.22 TPSA 54.4	✓ Ro5	✓ Clean	`C[C@]12CC[C@@H]3[C@H](CCC4=CC(=O)CC[C@@]43C)[C@…`
ZINC253618174	0.706	316.4 Da LogP 4.22 TPSA 54.4	✓ Ro5	✓ Clean	`C[C@@]12CCC(=O)C=C1CC[C@H]1[C@H]2CC[C@]2(C)[C@H…`
ZINC253648944	0.706	316.4 Da LogP 4.22 TPSA 54.4	✓ Ro5	✓ Clean	`C[C@]12CC[C@H]3[C@@H](CCC4=CC(=O)CC[C@@]43C)[C@…`
ZINC32911458	0.706	316.4 Da LogP 4.22 TPSA 54.4	✓ Ro5	✓ Clean	`C[C@]12CC[C@H]3[C@@H](CCC4=CC(=O)CC[C@@]43C)[C@…`
ZINC3927796	0.706	316.4 Da LogP 4.22 TPSA 54.4	✓ Ro5	✓ Clean	`C[C@]12CC[C@H]3[C@@H](CCC4=CC(=O)CC[C@@]43C)[C@…`

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.