Protein profile

PA2968

malonyl CoA-ACP transacylase

Genome: NC_002516.2

Gene: fabD PA2968 Structure source: AlphaFold UniProt G3XCZ6 UniProt O54437

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Amino acids 312

Annotations 5

Features 17

PDB binders 10

Druggability 0.79

Overview

Basic information about this protein and its source genome.

Accession: PA2968
Assembly: Pseudomonas aeruginosa PAO1, complete genome
Gene: fabD PA2968
Status: annotated
Amino acids: 312
Structure source: AlphaFold

2.3.1.39

GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. GO:0004314 Catalysis of the reaction: malonyl-CoA + [acyl-carrier protein] = CoA + malonyl-[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:0016740 Catalysis of the transfer of a group, e.g. a methyl group, glycosyl group, acyl group, phosphorus-containing, or other groups, from one compound (generally regarded as the donor) to another compound (generally regarded as the acceptor). Transferase is the systematic name for any enzyme of EC class 2.

Target profile

Computed evidence for target prioritization.

Human off-target: hit
Human identity (%): 31.803
Human E-value: 9.03e-35
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 0.79

Structure –

Pocket –

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 4 GO

Enzyme Commission (EC)

2.3.1.39

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:0004314 Catalysis of the reaction: malonyl-CoA + [acyl-carrier protein] = CoA + malonyl-[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:0016740 Catalysis of the transfer of a group, e.g. a methyl group, glycosyl group, acyl group, phosphorus-containing, or other groups, from one compound (generally regarded as the donor) to another compound (generally regarded as the acceptor). Transferase is the systematic name for any enzyme of EC class 2.

Sequence Features

Domain/signature hits from InterPro and related databases.

17 records

Show feature table

Start	End	DB	Term	Name
5	290	NCBIfam	TIGR00128	ACP S-malonyltransferase
5	290	InterPro	IPR004410	Malonyl CoA-acyl carrier protein transacylase, FabD-type
5	299	SUPERFAMILY	SSF52151	FabD/lysophospholipase-like
5	299	InterPro	IPR016035	Acyl transferase/acyl hydrolase/lysophospholipase
2	311	PIRSF	PIRSF000446	Mct
2	311	InterPro	IPR024925	Malonyl CoA-acyl carrier protein transacylase
7	275	Pfam	PF00698	Acyl transferase domain
7	275	InterPro	IPR014043	Acyl transferase
8	311	SMART	SM00827	Acyl transferase domain in polyketide synthase (PKS) enzymes.
8	311	InterPro	IPR014043	Acyl transferase
126	198	FunFam	G3DSA:3.30.70.250:FF:000001	Malonyl CoA-acyl carrier protein transacylase
7	286	Gene3D	G3DSA:3.40.366.10	-
7	286	InterPro	IPR001227	Acyl transferase domain superfamily
126	198	Gene3D	G3DSA:3.30.70.250	-
4	295	PANTHER	PTHR42681	MALONYL-COA-ACYL CARRIER PROTEIN TRANSACYLASE, MITOCHONDRIAL
129	198	SUPERFAMILY	SSF55048	Probable ACP-binding domain of malonyl-CoA ACP transacylase
129	198	InterPro	IPR016036	Malonyl-CoA ACP transacylase, ACP-binding

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 PA2968	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
4				0.79
1				0.768

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.

60 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
8JZ	3HJV	Q9KQH6	116.2 Da LogP 1.35 TPSA 26.3	✓ Ro5	✓ Clean	`CCCCOC(=O)C`
9EF	6U0J	P0AAI9	383.3 Da LogP -1.76 TPSA 174.3	1 viol.	✓ Clean	`CC(=O)NCCNC(=O)CCNC(=O)[C@@H](C(C)(C)COP(=O)(O)…`
AE3	2C2N	Q8IVS2	134.2 Da LogP 0.03 TPSA 38.7	✓ Ro5	✓ Clean	`CCOCCOCCO`
AE4	2C2N	Q8IVS2	266.3 Da LogP 0.08 TPSA 66.4	✓ Ro5	✓ Clean	`CCOCCOCCOCCOCCOCCO`
COZ	2G2Z	P0AAI9	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]([…`
CXS	3HJV	Q9KQH6	221.3 Da LogP 1.19 TPSA 66.4	✓ Ro5	✓ Clean	`C1CCC(CC1)NCCCS(=O)(=O)O`
DXE	2C2N	Q8IVS2	90.1 Da LogP 0.28 TPSA 18.5	✓ Ro5	✓ Clean	`COCCOC`
MLA	2G2Z	P0AAI9	104.1 Da LogP -0.45 TPSA 74.6	✓ Ro5	✓ Clean	`C(C(=O)O)C(=O)O`
MLI	2G2Y	P0AAI9	102.0 Da LogP -3.12 TPSA 80.3	✓ Ro5	✓ Clean	`C(C(=O)[O-])C(=O)[O-]`
NHE	3R97	Q5H4I7	207.3 Da LogP 0.80 TPSA 66.4	✓ Ro5	✓ Clean	`C1CCC(CC1)NCCS(=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).

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
ZINC2004372	1.000	221.3 Da LogP 1.19 TPSA 66.4	✓ Ro5	✓ Clean	`O=S(=O)(O)CCCNC1CCCCC1`
ZINC5650743	1.000	222.3 Da LogP 0.07 TPSA 57.2	✓ Ro5	✓ Clean	`CCOCCOCCOCCOCCO`
ZINC6403917	1.000	354.4 Da LogP 0.11 TPSA 84.8	✓ Ro5	✓ Clean	`CCOCCOCCOCCOCCOCCOCCOCCO`
ZINC38364153	0.926	235.3 Da LogP 1.58 TPSA 66.4	✓ Ro5	✓ Clean	`O=S(=O)(O)CCCCNC1CCCCC1`
ZINC1677799	0.810	200.3 Da LogP 3.69 TPSA 26.3	✓ Ro5	✓ Clean	`CCCCCCCCCCOC(C)=O`
ZINC1694423	0.810	228.4 Da LogP 4.47 TPSA 26.3	✓ Ro5	✓ Clean	`CCCCCCCCCCCCOC(C)=O`
ZINC1848558	0.810	214.3 Da LogP 4.08 TPSA 26.3	✓ Ro5	✓ Clean	`CCCCCCCCCCCOC(C)=O`
ZINC59725169	0.810	242.4 Da LogP 4.86 TPSA 26.3	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCOC(C)=O`
ZINC1710230	0.786	207.3 Da LogP 0.80 TPSA 66.4	✓ Ro5	✓ Clean	`O=S(=O)(O)CCNC1CCCCC1`
ZINC1692489	0.727	222.3 Da LogP 0.33 TPSA 46.2	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOC`
ZINC4530388	0.727	266.3 Da LogP 0.35 TPSA 55.4	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOC`
ZINC5701172	0.727	310.4 Da LogP 0.36 TPSA 64.6	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOC`
ZINC5997861	0.727	398.5 Da LogP 0.40 TPSA 83.1	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCOCCOC`
ZINC15146151	0.700	286.4 Da LogP 4.01 TPSA 52.6	✓ Ro5	✓ Clean	`CC(=O)OCCCCCCCCCCCCOC(C)=O`
ZINC1532902	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`
ZINC1684744	0.700	244.3 Da LogP 2.84 TPSA 52.6	✓ Ro5	✓ Clean	`CC(=O)OCCCCCCCCCOC(C)=O`
ZINC1694794	0.700	202.2 Da LogP 1.67 TPSA 52.6	✓ Ro5	✓ Clean	`CC(=O)OCCCCCCOC(C)=O`
ZINC2018106	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`
ZINC2386050	0.700	230.3 Da LogP 2.45 TPSA 52.6	✓ Ro5	✓ Clean	`CC(=O)OCCCCCCCCOC(C)=O`
ZINC2556930	0.700	216.3 Da LogP 2.06 TPSA 52.6	✓ Ro5	✓ Clean	`CC(=O)OCCCCCCCOC(C)=O`
ZINC5161313	0.700	258.4 Da LogP 3.23 TPSA 52.6	✓ Ro5	✓ Clean	`CC(=O)OCCCCCCCCCCOC(C)=O`
ZINC12501520	0.688	458.5 Da LogP -0.88 TPSA 123.5	1 viol.	✓ Clean	`OCCOCCOCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC3874716	0.688	414.5 Da LogP -0.90 TPSA 114.3	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC4283769	0.688	238.3 Da LogP -0.96 TPSA 77.4	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCO`
ZINC4521548	0.688	282.3 Da LogP -0.95 TPSA 86.6	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCOCCO`
ZINC5178829	0.688	326.4 Da LogP -0.93 TPSA 95.8	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCOCCOCCO`
ZINC5178830	0.688	370.4 Da LogP -0.91 TPSA 105.1	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC5859031	0.688	294.4 Da LogP 1.13 TPSA 55.4	✓ Ro5	✓ Clean	`CCOCCOCCOCCOCCOCCOCC`
ZINC1586759	0.667	202.2 Da LogP 1.67 TPSA 52.6	✓ Ro5	✓ Clean	`CCCCOC(=O)C(=O)OCCCC`
ZINC3593496	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	0.652	206.2 Da LogP -1.16 TPSA 121.1	✓ Ro5	✓ Clean	`COC(=O)C[C@](O)(CC(=O)O)C(=O)O`
ZINC1850172	0.630	240.4 Da LogP 4.64 TPSA 26.3	✓ Ro5	✓ Clean	`CCCCCCCC/C=C/CCCOC(C)=O`
ZINC2018958	0.630	226.4 Da LogP 4.25 TPSA 26.3	✓ Ro5	✓ Clean	`CCCC/C=C/CCCCCCOC(C)=O`
ZINC43068418	0.630	240.4 Da LogP 4.64 TPSA 26.3	✓ Ro5	✓ Clean	`CCCCCCCC/C=C\CCCOC(C)=O`
ZINC4543853	0.630	226.4 Da LogP 4.25 TPSA 26.3	✓ Ro5	✓ Clean	`CCCC/C=C\CCCCCCOC(C)=O`
ZINC5188799	0.630	280.5 Da LogP 4.39 TPSA 24.1	✓ Ro5	✓ Clean	`C(CCCNC1CCCCC1)CCNC1CCCCC1`
ZINC59725075	0.630	226.4 Da LogP 4.25 TPSA 26.3	✓ Ro5	✓ Clean	`CCCCCC/C=C/CCCCOC(C)=O`
ZINC59725096	0.630	226.4 Da LogP 4.25 TPSA 26.3	✓ Ro5	✓ Clean	`CCCCCC/C=C\CCCCOC(C)=O`
ZINC100812469	0.625	200.2 Da LogP 1.12 TPSA 60.4	✓ Ro5	✓ Clean	`CCCCOC(=O)C(C(C)=O)C(C)=O`
ZINC14686440	0.625	436.4 Da LogP -2.64 TPSA 247.9	1 viol.	✓ Clean	`O=C(O)C[C@](O)(CC(=O)NCCCCNC(=O)C[C@@](O)(CC(=O…`
ZINC14686442	0.625	436.4 Da LogP -2.64 TPSA 247.9	1 viol.	✓ Clean	`O=C(O)C[C@@](O)(CC(=O)NCCCCNC(=O)C[C@](O)(CC(=O…`
ZINC14686444	0.625	436.4 Da LogP -2.64 TPSA 247.9	1 viol.	✓ Clean	`O=C(O)C[C@@](O)(CC(=O)NCCCCNC(=O)C[C@@](O)(CC(=…`
ZINC39205441	0.625	258.3 Da LogP 2.02 TPSA 69.7	✓ Ro5	✓ Clean	`CCCCOC(=O)CC(=O)CC(=O)OCCCC`
ZINC1576862	0.609	230.3 Da LogP 2.45 TPSA 52.6	✓ Ro5	✓ Clean	`CCCCOC(=O)CCC(=O)OCCCC`
ZINC1641637	0.609	216.3 Da LogP 2.06 TPSA 52.6	✓ Ro5	✓ Clean	`CCCCOC(=O)CC(=O)OCCCC`
ZINC15146078	0.607	224.3 Da LogP 4.02 TPSA 26.3	✓ Ro5	✓ Clean	`CCCC/C=C/C=C\CCCCOC(C)=O`
ZINC59725114	0.607	224.3 Da LogP 4.02 TPSA 26.3	✓ Ro5	✓ Clean	`CCCC/C=C\C=C/CCCCOC(C)=O`
ZINC16052257	0.600	384.5 Da LogP -0.26 TPSA 94.1	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC34317654	0.600	472.6 Da LogP -0.23 TPSA 112.5	1 viol.	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC44076059	0.600	428.5 Da LogP -0.24 TPSA 103.3	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCOCCOCCO`

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.