Protein profile

PA3112

acetyl-CoA carboxylase carboxyltransferase subunit beta

Genome: NC_002516.2

Gene: accD PA3112 Structure source: AlphaFold UniProt Q9HZA7

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Amino acids 290

Annotations 10

Features 24

PDB binders 6

Druggability 0.506

Overview

Basic information about this protein and its source genome.

Accession: PA3112
Assembly: Pseudomonas aeruginosa PAO1, complete genome
Gene: accD PA3112
Status: annotated
Amino acids: 290
Structure source: AlphaFold

2.1.3.15

GO:0009329 A heterotetrameric enzyme complex made up of two alpha subunits and two beta subunits. Part of the acetyl-CoA carboxylase complex. Catalyzes the transfer of a carboxyl group to form malonyl-CoA. GO:0003989 Catalysis of the reaction: ATP + acetyl-CoA + HCO3- = ADP + phosphate + malonyl-CoA. GO:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. GO:0016743 Catalysis of the transfer of a carboxyl- or carbamoyl group from one compound (donor) to another (acceptor). GO:0008270 Binding to a zinc ion (Zn). 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.

Target profile

Computed evidence for target prioritization.

Human off-target: hit
Human identity (%): 29.06
Human E-value: 2.94e-06
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 0.506

Structure –

Pocket –

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 9 GO

Enzyme Commission (EC)

2.1.3.15

Gene Ontology (GO)

GO:0009329 A heterotetrameric enzyme complex made up of two alpha subunits and two beta subunits. Part of the acetyl-CoA carboxylase complex. Catalyzes the transfer of a carboxyl group to form malonyl-CoA.
GO:0003989 Catalysis of the reaction: ATP + acetyl-CoA + HCO3- = ADP + phosphate + malonyl-CoA.
GO:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
GO:0016743 Catalysis of the transfer of a carboxyl- or carbamoyl group from one compound (donor) to another (acceptor).
GO:0008270 Binding to a zinc ion (Zn).
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:2001295 The chemical reactions and pathways resulting in the formation of malonyl-CoA, the S-malonyl derivative of coenzyme A.
GO:0017148 Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of proteins by the translation of mRNA or circRNA.
GO:0009317 A protein complex that catalyzes the first step in long-chain fatty acid biosynthesis. For example, in E. coli the complex is heterohexameric and composed of biotin carbonyl carrier protein, biotin carboxylase and the acetate CoA-transferase complex.

Sequence Features

Domain/signature hits from InterPro and related databases.

24 records

Show feature table

Start	End	DB	Term	Name
27	290	ProSiteProfiles	PS50980	Acetyl-coenzyme A (CoA) carboxyltransferase N-terminal domain profile.
27	290	InterPro	IPR011762	Acetyl-coenzyme A carboxyltransferase, N-terminal
14	286	NCBIfam	TIGR00515	acetyl-CoA carboxylase, carboxyltransferase subunit beta
14	286	InterPro	IPR000438	Acetyl-CoA carboxylase carboxyl transferase, beta subunit
165	183	PRINTS	PR01070	Acetyl-CoA carboxylase carboxyl transferase beta subunit signature
165	183	InterPro	IPR000438	Acetyl-CoA carboxylase carboxyl transferase, beta subunit
253	262	PRINTS	PR01070	Acetyl-CoA carboxylase carboxyl transferase beta subunit signature
253	262	InterPro	IPR000438	Acetyl-CoA carboxylase carboxyl transferase, beta subunit
131	145	PRINTS	PR01070	Acetyl-CoA carboxylase carboxyl transferase beta subunit signature
131	145	InterPro	IPR000438	Acetyl-CoA carboxylase carboxyl transferase, beta subunit
231	242	PRINTS	PR01070	Acetyl-CoA carboxylase carboxyl transferase beta subunit signature
231	242	InterPro	IPR000438	Acetyl-CoA carboxylase carboxyl transferase, beta subunit
202	219	PRINTS	PR01070	Acetyl-CoA carboxylase carboxyl transferase beta subunit signature
202	219	InterPro	IPR000438	Acetyl-CoA carboxylase carboxyl transferase, beta subunit
96	241	Pfam	PF01039	Carboxyl transferase domain
96	241	InterPro	IPR034733	Acetyl-CoA carboxylase
2	283	Hamap	MF_01395	Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta, chloroplastic [accD].
2	283	InterPro	IPR000438	Acetyl-CoA carboxylase carboxyl transferase, beta subunit
28	53	Pfam	PF17848	Acetyl-coA carboxylase zinc finger domain
28	53	InterPro	IPR041010	Acetyl-coA carboxylase zinc finger domain
27	285	Gene3D	G3DSA:3.90.226.10	-
17	284	PANTHER	PTHR42995	ACETYL-COENZYME A CARBOXYLASE CARBOXYL TRANSFERASE SUBUNIT BETA, CHLOROPLASTIC
27	285	SUPERFAMILY	SSF52096	ClpP/crotonase
27	285	InterPro	IPR029045	ClpP/crotonase-like domain superfamily

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 PA3112	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				0.506
6				0.4
2				0.209

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.

56 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
1VU	1XNY	Q9X4K7	823.6 Da LogP -0.93 TPSA 363.6	3 viol.	✓ Clean	`CCC(=O)SCCNC(=O)CCNC(=O)[C@@H](C(C)(C)COP(=O)(O…`
BTI	3N6R	Q168G2	228.3 Da LogP 0.91 TPSA 58.2	✓ Ro5	✓ Clean	`C1[C@H]2[C@@H]([C@@H](S1)CCCCC=O)NC(=O)N2`
DXX	1ON3	Q8GBW6	118.1 Da LogP -0.21 TPSA 74.6	✓ Ro5	✓ Clean	`CC(C(=O)O)C(=O)O`
HXC	5INF	A0ACI9	865.7 Da LogP 0.25 TPSA 363.6	3 viol.	✓ Clean	`CCCCCC(=O)SCCNC(=O)CCNC(=O)[C@@H](C(C)(C)CO[P@@…`
MCA	1ON3	Q8GBW6	867.6 Da LogP -1.61 TPSA 400.9	3 viol.	✓ Clean	`C[C@H](C(=O)O)C(=O)SCCNC(=O)CCNC(=O)[C@@H](C(C)…`
YT5	5KDR	Q2FXM6	453.5 Da LogP 1.98 TPSA 121.4	✓ Ro5	✓ Clean	`C/C=C/C=C/C(=O)N[C@@H](CC(=O)N[C@@H](C(C)C)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
ZINC34603442	0.703	215.3 Da LogP 0.28 TPSA 67.1	✓ Ro5	✓ Clean	`NCCCC[C@@H]1SC[C@@H]2NC(=O)N[C@H]12`
ZINC34182012	0.667	230.3 Da LogP 0.70 TPSA 61.4	✓ Ro5	✓ Clean	`O=C1N[C@@H]2[C@H](CCCCCO)SC[C@@H]2N1`
ZINC1532548	0.634	244.3 Da LogP 0.80 TPSA 78.4	✓ Ro5	✓ Clean	`O=C(O)CCCC[C@H]1SC[C@@H]2NC(=O)N[C@@H]21`
ZINC2169825	0.634	244.3 Da LogP 0.80 TPSA 78.4	✓ Ro5	✓ Clean	`O=C(O)CCCC[C@H]1SC[C@H]2NC(=O)N[C@H]21`
ZINC2169827	0.634	244.3 Da LogP 0.80 TPSA 78.4	✓ Ro5	✓ Clean	`O=C(O)CCCC[C@H]1SC[C@@H]2NC(=O)N[C@H]21`
ZINC3869709	0.634	243.3 Da LogP 0.20 TPSA 84.2	✓ Ro5	✓ Clean	`NC(=O)CCCC[C@@H]1SC[C@H]2NC(=O)N[C@@H]21`
ZINC3869710	0.634	243.3 Da LogP 0.20 TPSA 84.2	✓ Ro5	✓ Clean	`NC(=O)CCCC[C@@H]1SC[C@@H]2NC(=O)N[C@H]12`
ZINC3869711	0.634	243.3 Da LogP 0.20 TPSA 84.2	✓ Ro5	✓ Clean	`NC(=O)CCCC[C@@H]1SC[C@H]2NC(=O)N[C@H]21`
ZINC3869712	0.634	243.3 Da LogP 0.20 TPSA 84.2	✓ Ro5	✓ Clean	`NC(=O)CCCC[C@@H]1SC[C@@H]2NC(=O)N[C@@H]12`
ZINC22052067	0.609	301.4 Da LogP -0.09 TPSA 107.5	✓ Ro5	✓ Clean	`O=C(O)CNC(=O)CCCC[C@@H]1SC[C@@H]2NC(=O)N[C@H]12`
ZINC59286406	0.609	300.4 Da LogP -0.69 TPSA 113.3	✓ Ro5	✓ Clean	`NC(=O)CNC(=O)CCCC[C@@H]1SC[C@@H]2NC(=O)N[C@H]12`
ZINC222024244	0.600	283.4 Da LogP 0.99 TPSA 70.2	✓ Ro5	✓ Clean	`O=C(CCCC[C@@H]1SC[C@@H]2NC(=O)N[C@@H]12)NC1CC1`
ZINC48391181	0.600	283.4 Da LogP 0.99 TPSA 70.2	✓ Ro5	✓ Clean	`O=C(CCCC[C@@H]1SC[C@@H]2NC(=O)N[C@H]12)NC1CC1`
ZINC53464107	0.600	283.4 Da LogP 0.99 TPSA 70.2	✓ Ro5	✓ Clean	`O=C(CCCC[C@@H]1SC[C@H]2NC(=O)N[C@@H]21)NC1CC1`
ZINC53464111	0.600	283.4 Da LogP 0.99 TPSA 70.2	✓ Ro5	✓ Clean	`O=C(CCCC[C@@H]1SC[C@H]2NC(=O)N[C@H]21)NC1CC1`
ZINC2121285	0.578	258.3 Da LogP 0.89 TPSA 67.4	✓ Ro5	✓ Clean	`COC(=O)CCCC[C@@H]1SC[C@H]2NC(=O)N[C@H]21`
ZINC4038545	0.578	258.3 Da LogP 0.89 TPSA 67.4	✓ Ro5	✓ Clean	`COC(=O)CCCC[C@H]1SC[C@H]2NC(=O)N[C@H]21`
ZINC5005298	0.578	258.3 Da LogP 0.89 TPSA 67.4	✓ Ro5	✓ Clean	`COC(=O)CCCC[C@@H]1SC[C@H]2NC(=O)N[C@@H]21`
ZINC5224322	0.578	258.3 Da LogP 0.89 TPSA 67.4	✓ Ro5	✓ Clean	`COC(=O)CCCC[C@@H]1SC[C@@H]2NC(=O)N[C@H]12`
ZINC90514224	0.578	258.3 Da LogP 0.89 TPSA 67.4	✓ Ro5	✓ Clean	`COC(=O)CCCC[C@@H]1SC[C@@H]2NC(=O)N[C@@H]12`
ZINC27065097	0.574	311.5 Da LogP 1.77 TPSA 70.2	✓ Ro5	✓ Clean	`O=C(CCCC[C@@H]1SC[C@@H]2NC(=O)N[C@H]12)NC1CCCC1`
ZINC5157321	0.574	287.4 Da LogP -0.18 TPSA 90.5	✓ Ro5	✓ Clean	`O=C(CCCC[C@@H]1SC[C@@H]2NC(=O)N[C@H]12)NCCO`
ZINC206908803	0.571	315.4 Da LogP 0.00 TPSA 96.5	✓ Ro5	✓ Clean	`COC(=O)CNC(=O)CCCC[C@@H]1SC[C@H]2NC(=O)N[C@@H]21`
ZINC334161970	0.571	315.4 Da LogP 0.00 TPSA 96.5	✓ Ro5	✓ Clean	`COC(=O)CNC(=O)CCCC[C@@H]1SC[C@@H]2NC(=O)N[C@@H]…`
ZINC62001297	0.571	315.4 Da LogP 0.00 TPSA 96.5	✓ Ro5	✓ Clean	`COC(=O)CNC(=O)CCCC[C@@H]1SC[C@@H]2NC(=O)N[C@H]12`
ZINC75611263	0.571	315.4 Da LogP 0.00 TPSA 96.5	✓ Ro5	✓ Clean	`COC(=O)CNC(=O)CCCC[C@@H]1SC[C@H]2NC(=O)N[C@H]21`
ZINC104112886	0.568	242.3 Da LogP 0.57 TPSA 78.4	✓ Ro5	✓ Clean	`O=C(O)/C=C\CC[C@@H]1SC[C@H]2NC(=O)N[C@@H]21`
ZINC13543600	0.568	242.3 Da LogP 0.57 TPSA 78.4	✓ Ro5	✓ Clean	`O=C(O)/C=C\CC[C@@H]1SC[C@@H]2NC(=O)N[C@H]12`
ZINC4216800	0.568	242.3 Da LogP 0.57 TPSA 78.4	✓ Ro5	✓ Clean	`O=C(O)/C=C/CC[C@@H]1SC[C@@H]2NC(=O)N[C@H]12`
ZINC5082085	0.568	242.3 Da LogP 0.57 TPSA 78.4	✓ Ro5	✓ Clean	`O=C(O)/C=C/CC[C@@H]1SC[C@H]2NC(=O)N[C@@H]21`
ZINC5082088	0.568	242.3 Da LogP 0.57 TPSA 78.4	✓ Ro5	✓ Clean	`O=C(O)/C=C/CC[C@@H]1SC[C@H]2NC(=O)N[C@H]21`
ZINC5082090	0.568	242.3 Da LogP 0.57 TPSA 78.4	✓ Ro5	✓ Clean	`O=C(O)/C=C/CC[C@@H]1SC[C@@H]2NC(=O)N[C@@H]12`
ZINC77273222	0.568	428.6 Da LogP 1.36 TPSA 119.6	✓ Ro5	✓ Clean	`O=C1N[C@@H]2[C@H](CCCC(CCC[C@@H]3SC[C@@H]4NC(=O…`
ZINC107559942	0.563	283.4 Da LogP 1.01 TPSA 70.2	✓ Ro5	✓ Clean	`C=CCNC(=O)CCCC[C@@H]1SC[C@@H]2NC(=O)N[C@H]12`
ZINC12624504	0.563	339.5 Da LogP 2.55 TPSA 70.2	✓ Ro5	✓ Clean	`O=C(CCCC[C@@H]1SC[C@@H]2NC(=O)N[C@H]12)NC1CCCCC…`
ZINC13509480	0.563	315.4 Da LogP 0.30 TPSA 107.5	✓ Ro5	✓ Clean	`O=C(O)CCNC(=O)CCCC[C@@H]1SC[C@@H]2NC(=O)N[C@H]12`
ZINC141396702	0.563	303.5 Da LogP 0.76 TPSA 70.2	✓ Ro5	✓ Clean	`O=C(CCCC[C@@H]1SC[C@@H]2NC(=O)N[C@H]12)NCCS`
ZINC149421996	0.563	286.4 Da LogP -0.21 TPSA 96.2	✓ Ro5	✓ Clean	`NCCNC(=O)CCCC[C@H]1SC[C@H]2NC(=O)N[C@H]21`
ZINC22048411	0.563	286.4 Da LogP -0.21 TPSA 96.2	✓ Ro5	✓ Clean	`NCCNC(=O)CCCC[C@@H]1SC[C@H]2NC(=O)N[C@@H]21`
ZINC222218978	0.563	284.4 Da LogP 1.44 TPSA 67.4	✓ Ro5	✓ Clean	`C=CCOC(=O)CCCC[C@@H]1SC[C@@H]2NC(=O)N[C@@H]12`
ZINC222438745	0.563	339.5 Da LogP 2.55 TPSA 70.2	✓ Ro5	✓ Clean	`O=C(CCCC[C@@H]1SC[C@@H]2NC(=O)N[C@@H]12)NC1CCCC…`
ZINC34440530	0.563	301.4 Da LogP 0.21 TPSA 90.5	✓ Ro5	✓ Clean	`O=C(CCCC[C@@H]1SC[C@@H]2NC(=O)N[C@H]12)NCCCO`
ZINC39935771	0.563	286.4 Da LogP -0.21 TPSA 96.2	✓ Ro5	✓ Clean	`NCCNC(=O)CCCC[C@@H]1SC[C@H]2NC(=O)N[C@H]21`
ZINC39935772	0.563	286.4 Da LogP -0.21 TPSA 96.2	✓ Ro5	✓ Clean	`NCCNC(=O)CCCC[C@@H]1SC[C@@H]2NC(=O)N[C@@H]12`
ZINC5192432	0.563	286.4 Da LogP -0.21 TPSA 96.2	✓ Ro5	✓ Clean	`NCCNC(=O)CCCC[C@@H]1SC[C@@H]2NC(=O)N[C@H]12`
ZINC80301665	0.563	284.4 Da LogP 1.44 TPSA 67.4	✓ Ro5	✓ Clean	`C=CCOC(=O)CCCC[C@@H]1SC[C@@H]2NC(=O)N[C@H]12`
ZINC95966269	0.563	284.4 Da LogP 1.44 TPSA 67.4	✓ Ro5	✓ Clean	`C=CCOC(=O)CCCC[C@@H]1SC[C@H]2NC(=O)N[C@@H]21`
ZINC95966271	0.563	284.4 Da LogP 1.44 TPSA 67.4	✓ Ro5	✓ Clean	`C=CCOC(=O)CCCC[C@@H]1SC[C@H]2NC(=O)N[C@H]21`
ZINC9691512	0.563	339.5 Da LogP 2.55 TPSA 70.2	✓ Ro5	✓ Clean	`O=C(CCCC[C@@H]1SC[C@H]2NC(=O)N[C@@H]21)NC1CCCCC…`
ZINC9691514	0.563	339.5 Da LogP 2.55 TPSA 70.2	✓ Ro5	✓ Clean	`O=C(CCCC[C@@H]1SC[C@H]2NC(=O)N[C@H]21)NC1CCCCCC1`

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.