Protein profile

PA1373

3-oxoacyl-ACP synthase

Genome: NC_002516.2

Gene: fabF2 PA1373 Structure source: AlphaFold UniProt Q9I3X1

Export view

Amino acids 422

Annotations 6

Features 25

PDB binders 13

Druggability 0.783

Overview

Basic information about this protein and its source genome.

Accession: PA1373
Assembly: Pseudomonas aeruginosa PAO1, complete genome
Gene: fabF2 PA1373
Status: annotated
Amino acids: 422
Structure source: AlphaFold

2.3.1.179

GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. GO:0004315 Catalysis of the reaction: acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein] = 3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]. GO:0006633 The chemical reactions and pathways resulting in the formation of a fatty acid, any of the aliphatic monocarboxylic acids that can be liberated by hydrolysis from naturally occurring fats and oils. Fatty acids are predominantly straight-chain acids of 4 to 24 carbon atoms, which may be saturated or unsaturated; branched fatty acids and hydroxy fatty acids also occur, and very long chain acids of over 30 carbons are found in waxes. 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).

Target profile

Computed evidence for target prioritization.

Human off-target: hit
Human identity (%): 44.762
Human E-value: 8.03e-112
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 0.783

Structure –

Pocket –

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 5 GO

Enzyme Commission (EC)

2.3.1.179

Gene Ontology (GO)

GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
GO:0004315 Catalysis of the reaction: acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein] = 3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein].
GO:0006633 The chemical reactions and pathways resulting in the formation of a fatty acid, any of the aliphatic monocarboxylic acids that can be liberated by hydrolysis from naturally occurring fats and oils. Fatty acids are predominantly straight-chain acids of 4 to 24 carbon atoms, which may be saturated or unsaturated; branched fatty acids and hydroxy fatty acids also occur, and very long chain acids of over 30 carbons are found in waxes.
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.

25 records

Show feature table

Start	End	DB	Term	Name
3	256	Pfam	PF00109	Beta-ketoacyl synthase, N-terminal domain
3	256	InterPro	IPR014030	Beta-ketoacyl synthase, N-terminal
1	421	Gene3D	G3DSA:3.40.47.10	-
1	421	InterPro	IPR016039	Thiolase-like
1	422	PIRSF	PIRSF000447	KAS_II
1	422	InterPro	IPR017568	3-oxoacyl-[acyl-carrier-protein] synthase 2
3	419	NCBIfam	TIGR03150	beta-ketoacyl-ACP synthase II
3	419	InterPro	IPR017568	3-oxoacyl-[acyl-carrier-protein] synthase 2
3	418	CDD	cd00834	KAS_I_II
3	418	InterPro	IPR000794	Beta-ketoacyl synthase
163	179	ProSitePatterns	PS00606	Ketosynthase family 3 (KS3) active site signature.
163	179	InterPro	IPR018201	Beta-ketoacyl synthase, active site
2	420	PANTHER	PTHR11712	POLYKETIDE SYNTHASE-RELATED
2	420	InterPro	IPR000794	Beta-ketoacyl synthase
223	421	SUPERFAMILY	SSF53901	Thiolase-like
223	421	InterPro	IPR016039	Thiolase-like
3	261	SUPERFAMILY	SSF53901	Thiolase-like
3	261	InterPro	IPR016039	Thiolase-like
265	378	Pfam	PF02801	Beta-ketoacyl synthase, C-terminal domain
265	378	InterPro	IPR014031	Beta-ketoacyl synthase, C-terminal
2	420	ProSiteProfiles	PS52004	Ketosynthase family 3 (KS3) domain profile.
2	420	InterPro	IPR020841	Polyketide synthase, beta-ketoacyl synthase domain
5	421	SMART	SM00825	Beta-ketoacyl synthase
5	421	InterPro	IPR020841	Polyketide synthase, beta-ketoacyl synthase domain
1	421	FunFam	G3DSA:3.40.47.10:FF:000009	3-oxoacyl-[acyl-carrier-protein] synthase 2

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...

Legend High Medium Low

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 PA1373	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
3				0.783
1				0.641

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.

63 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
1LR	4JPF	G3XDA2	257.2 Da LogP 2.34 TPSA 86.6	✓ Ro5	✓ Clean	`c1ccc(cc1)C(=O)Nc2cccc(c2O)C(=O)O`
1X9	4LS7	O34340	223.3 Da LogP 1.11 TPSA 72.7	✓ Ro5	✓ Clean	`C/C=C/C/C=C/CCC(=O)[C@@H]1[C@@H](O1)C(=O)N`
1XG	4LS8	O34340	225.3 Da LogP 1.09 TPSA 80.4	✓ Ro5	✓ Clean	`C/C=C/C/C=C/CCC(=O)[C@@H](CC(=O)N)O`
840	3I8P	P0AAI5	455.5 Da LogP 1.96 TPSA 153.4	✓ Ro5	✓ Clean	`C[C@@]1([C@H]2[C@@]34C[C@]35CC2(C=CC1=O)[C@H]([…`
CER	1B3N	P0AAI5	225.3 Da LogP 1.09 TPSA 80.4	✓ Ro5	✓ Clean	`C\C=C\C\C=C\CCC(=O)[C@H](CC(=O)N)O`
DAO	2GFY	P0AAI5	200.3 Da LogP 3.99 TPSA 37.3	✓ Ro5	✓ Clean	`CCCCCCCCCCCC(=O)O`
MRJ	6OLT	P0AAI5	523.6 Da LogP 2.14 TPSA 174.3	2 viol.	✓ Clean	`CCCCCCCCCCCC(=O)NCCNC(=O)CCNC(=O)[C@@H](C(C)(C)…`
MU4	6OKG	P0AAI5	579.7 Da LogP 3.70 TPSA 174.3	2 viol.	✓ Clean	`CCCCCCCCCCCCCCCC(=O)NCCNC(=O)CCNC(=O)[C@@H](C(C…`
N32	4F32	A4JL30	425.5 Da LogP 4.02 TPSA 123.9	✓ Ro5	✓ Clean	`C[C@@]1([C@@H]2C[C@@H]3CC[C@]2(CC3=C)C=CC1=O)CC…`
N3A	3HO9	P0AAI5	441.5 Da LogP 2.99 TPSA 144.2	✓ Ro5	✓ Clean	`C[C@@]1([C@@H]2C[C@@H]3C[C@H]([C@]2(CC3=C)C=CC1…`
P9A	3G0Y	P0AAI5	443.5 Da LogP 3.46 TPSA 133.2	✓ Ro5	✓ Clean	`C[C@@]12C[C@@]34CCC(=O)[C@@]([C@@H]3[C@@H](O1)C…`
P9C	3G11	P0AAI5	519.6 Da LogP 4.85 TPSA 133.2	1 viol.	✓ Clean	`C[C@]12C[C@]34C[C@H]1C[C@@H]([C@H]3[C@](C(=O)C[…`
PMN	2GFX	P0AAI5	441.5 Da LogP 3.23 TPSA 133.2	✓ Ro5	✓ Clean	`C[C@]12C[C@]34C[C@H]1C[C@@H]([C@H]3[C@](C(=O)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).

Ligand	Tanimoto	MW · LogP · TPSA	Lipinski	PAINS	SMILES
ZINC1429478	1.000	257.2 Da LogP 2.34 TPSA 86.6	✓ Ro5	✓ Clean	`O=C(Nc1cccc(C(=O)O)c1O)c1ccccc1`
ZINC1529498	1.000	200.3 Da LogP 3.99 TPSA 37.3	✓ Ro5	✓ Clean	`CCCCCCCCCCCC(=O)O`
ZINC1530417	1.000	228.4 Da LogP 4.77 TPSA 37.3	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCC(=O)O`
ZINC1628119	1.000	214.3 Da LogP 4.38 TPSA 37.3	✓ Ro5	✓ Clean	`CCCCCCCCCCCCC(=O)O`
ZINC168677815	1.000	441.5 Da LogP 3.23 TPSA 133.2	✓ Ro5	✓ Clean	`C[C@@]1(CCC(=O)Nc2c(O)ccc(C(=O)O)c2O)C(=O)C=C[C…`
ZINC256352556	1.000	441.5 Da LogP 3.23 TPSA 133.2	✓ Ro5	✓ Clean	`C[C@@]1(CCC(=O)Nc2c(O)ccc(C(=O)O)c2O)C(=O)C=C[C…`
ZINC29050726	1.000	441.5 Da LogP 3.23 TPSA 133.2	✓ Ro5	✓ Clean	`C[C@]12C[C@@]34C=CC(=O)[C@@](C)(CCC(=O)Nc5c(O)c…`
ZINC29050858	1.000	425.5 Da LogP 4.02 TPSA 123.9	✓ Ro5	✓ Clean	`C=C1C[C@@]23C=CC(=O)[C@@](C)(CCC(=O)Nc4c(O)ccc(…`
ZINC138457918	0.850	228.3 Da LogP 3.56 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCCC(=O)CCCCC(=O)O`
ZINC138458029	0.850	228.3 Da LogP 3.56 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCC(=O)CCCCCC(=O)O`
ZINC144395054	0.850	242.4 Da LogP 3.95 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCC(=O)CCCCCCCC(=O)O`
ZINC14619628	0.850	270.4 Da LogP 4.73 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCC(=O)CCCCCCCCCC(=O)O`
ZINC196749828	0.850	214.3 Da LogP 3.17 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCC(=O)CCCCC(=O)O`
ZINC2113934076	0.850	256.4 Da LogP 4.34 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCC(=O)CCCCCCCC(=O)O`
ZINC2113934082	0.850	256.4 Da LogP 4.34 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCCC(=O)CCCCCCC(=O)O`
ZINC2113934083	0.850	256.4 Da LogP 4.34 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCCCCC(=O)CCCCC(=O)O`
ZINC2243670	0.850	228.3 Da LogP 3.56 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCC(=O)CCCCCCC(=O)O`
ZINC2569203	0.850	214.3 Da LogP 3.17 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCC(=O)CCCCCC(=O)O`
ZINC4798470	0.850	270.4 Da LogP 4.73 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCC(=O)CCCCCCCCC(=O)O`
ZINC5973005	0.850	242.4 Da LogP 3.95 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCC(=O)CCCCCCC(=O)O`
ZINC71418182	0.850	270.4 Da LogP 4.73 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCCCCCC(=O)CCCCC(=O)O`
ZINC79244776	0.850	270.4 Da LogP 4.73 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCCC(=O)CCCCCCCC(=O)O`
ZINC86037082	0.850	270.4 Da LogP 4.73 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCCCCC(=O)CCCCCC(=O)O`
ZINC86037089	0.850	270.4 Da LogP 4.73 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCCCC(=O)CCCCCCC(=O)O`
ZINC86039283	0.850	242.4 Da LogP 3.95 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCCCC(=O)CCCCC(=O)O`
ZINC3160730	0.810	214.3 Da LogP 3.17 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCCC(=O)CCCC(=O)O`
ZINC4582907	0.810	200.3 Da LogP 2.78 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCC(=O)CCCC(=O)O`
ZINC4727003	0.810	312.4 Da LogP 4.69 TPSA 71.4	✓ Ro5	✓ Clean	`CCCCCCC(=O)CCC(=O)CCCCCCCC(=O)O`
ZINC86037074	0.810	270.4 Da LogP 4.73 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCCCCCCC(=O)CCCC(=O)O`
ZINC2378801	0.800	200.3 Da LogP 2.78 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCC(=O)CCCCC(=O)O`
ZINC1429482	0.771	291.7 Da LogP 3.00 TPSA 86.6	✓ Ro5	✓ Clean	`O=C(Nc1cccc(C(=O)O)c1O)c1ccc(Cl)cc1`
ZINC1429492	0.771	271.3 Da LogP 2.65 TPSA 86.6	✓ Ro5	✓ Clean	`Cc1ccc(C(=O)Nc2cccc(C(=O)O)c2O)cc1`
ZINC1432221	0.771	275.2 Da LogP 2.48 TPSA 86.6	✓ Ro5	✓ Clean	`O=C(Nc1cccc(C(=O)O)c1O)c1ccc(F)cc1`
ZINC2113934081	0.762	270.4 Da LogP 4.73 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCC(=O)CCCCCCCCCCC(=O)O`
ZINC2243668	0.762	214.3 Da LogP 3.17 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCC(=O)CCCCCCC(=O)O`
ZINC2378799	0.762	200.3 Da LogP 2.78 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCC(=O)CCCCCC(=O)O`
ZINC33820423	0.762	242.4 Da LogP 3.95 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCC(=O)CCCCCCCCC(=O)O`
ZINC1429473	0.750	313.4 Da LogP 3.64 TPSA 86.6	✓ Ro5	✓ Clean	`CC(C)(C)c1ccc(C(=O)Nc2cccc(C(=O)O)c2O)cc1`
ZINC97718	0.742	241.2 Da LogP 2.64 TPSA 66.4	✓ Ro5	✓ Clean	`O=C(Nc1ccccc1C(=O)O)c1ccccc1`
ZINC2387442	0.739	246.4 Da LogP 4.34 TPSA 37.3	✓ Ro5	✓ Clean	`CCCCCCCCSCCCCC(=O)O`
ZINC31778284	0.739	310.4 Da LogP 4.47 TPSA 71.4	✓ Ro5	✓ Clean	`CCCCCCC(=O)/C=C\C(=O)CCCCCCCC(=O)O`
ZINC5540108	0.739	310.4 Da LogP 4.47 TPSA 71.4	✓ Ro5	✓ Clean	`CCCCCCC(=O)/C=C/C(=O)CCCCCCCC(=O)O`
ZINC64633397	0.739	226.4 Da LogP 4.55 TPSA 37.3	✓ Ro5	✓ Clean	`CCCCCC/C=C\CCCCCC(=O)O`
ZINC1429487	0.730	336.1 Da LogP 3.11 TPSA 86.6	✓ Ro5	✓ Clean	`O=C(Nc1cccc(C(=O)O)c1O)c1cccc(Br)c1`
ZINC1432220	0.730	275.2 Da LogP 2.48 TPSA 86.6	✓ Ro5	✓ Clean	`O=C(Nc1cccc(C(=O)O)c1O)c1cccc(F)c1`
ZINC59545317	0.727	200.3 Da LogP 2.78 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCCC(=O)CCC(=O)O`
ZINC59545320	0.727	270.4 Da LogP 4.73 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCCCCCCCC(=O)CCC(=O)O`
ZINC59545336	0.727	214.3 Da LogP 3.17 TPSA 54.4	✓ Ro5	✓ Clean	`CCCCCCCCC(=O)CCC(=O)O`
ZINC104125601	0.722	271.3 Da LogP 2.43 TPSA 75.6	✓ Ro5	✓ Clean	`COC(=O)c1cccc(NC(=O)c2ccccc2)c1O`
ZINC4593317	0.714	291.7 Da LogP 3.00 TPSA 86.6	✓ Ro5	✓ Clean	`O=C(Nc1cccc(C(=O)O)c1O)c1ccccc1Cl`

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.