Protein profile

KP13_02958

Biotin carboxyl carrier protein of acetyl-CoA carboxylase

Genome: KpKP13

Gene: AHE42416.1 accB Structure source: AlphaFold + ColabFold UniProt A0A0H3H3Q3

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Amino acids 155

Annotations 3

Features 20

PDB binders 2

Druggability 0.549

Overview

Basic information about this protein and its source genome.

Accession: KP13_02958
Assembly: Klebsiella pneumoniae subsp. pneumoniae Kp13, complete sequence
Gene: AHE42416.1 accB
Status: annotated
Amino acids: 155
Structure source: AlphaFold + ColabFold

GO:0003989 Catalysis of the reaction: ATP + acetyl-CoA + HCO3- = ADP + phosphate + malonyl-CoA. 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. 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 (%): 37.5
Human E-value: 3.1e-06
Gut microbiome off-target: hit
Essential (DEG): Y
DEG identity (%): 87.821
DEG E-value: 1.84e-94
Localization: Cytoplasmic
ColabFold pLDDT: 81.84

Selected Druggability evidence

AlphaFold / UniProt model

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 0.549

Structure A0A0H3H3Q3

Pocket Pocket 1

P2Rank

Structure A0A0H3H3Q3

Pocket No pockets

ColabFold model

FPocket 0.552 · Pocket 6

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 242 / 4744 genomes with a hit

Normalized 0.051

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

3 GO

Gene Ontology (GO)

GO:0003989 Catalysis of the reaction: ATP + acetyl-CoA + HCO3- = ADP + phosphate + malonyl-CoA.
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.
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.

Sequence Features

Domain/signature hits from InterPro and related databases.

20 records

Show feature table

Start	End	DB	Term	Name
72	155	ProSiteProfiles	PS50968	Biotinyl/lipoyl domain profile.
72	155	InterPro	IPR000089	Biotin/lipoyl attachment
73	155	FunFam	G3DSA:2.40.50.100:FF:000003	Acetyl-CoA carboxylase biotin carboxyl carrier protein
111	128	ProSitePatterns	PS00188	Biotin-requiring enzymes attachment site.
111	128	InterPro	IPR001882	Biotin-binding site
20	155	PANTHER	PTHR45266	OXALOACETATE DECARBOXYLASE ALPHA CHAIN
82	154	Pfam	PF00364	Biotin-requiring enzyme
82	154	InterPro	IPR000089	Biotin/lipoyl attachment
116	129	PRINTS	PR01071	Acetyl-CoA biotin carboxyl carrier protein signature
116	129	InterPro	IPR001249	Acetyl-CoA biotin carboxyl carrier
101	115	PRINTS	PR01071	Acetyl-CoA biotin carboxyl carrier protein signature
101	115	InterPro	IPR001249	Acetyl-CoA biotin carboxyl carrier
84	97	PRINTS	PR01071	Acetyl-CoA biotin carboxyl carrier protein signature
84	97	InterPro	IPR001249	Acetyl-CoA biotin carboxyl carrier
80	155	SUPERFAMILY	SSF51230	Single hybrid motif
80	155	InterPro	IPR011053	Single hybrid motif
1	155	NCBIfam	TIGR00531	acetyl-CoA carboxylase biotin carboxyl carrier protein
1	155	InterPro	IPR001249	Acetyl-CoA biotin carboxyl carrier
76	155	Gene3D	G3DSA:2.40.50.100	-
82	154	CDD	cd06850	biotinyl_domain

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

0 + 2

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

Entry	Method	Resolution	Chain	Coverage	Links	Status
AlphaFold AF_A0A0H3H3Q3	AlphaFold	—	—	full sequence	—	Viewing
ColabFold KP13_02958	ColabFold	—	—	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
1				0.549
2				0.078
5				0.005
4				0.001

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
6				0.552
4				0.009
9				0.001
1				0.0

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.

52 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
BTI	5KS8	Q1H157	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`
PYR	5KS8	Q1H157	88.1 Da LogP -0.34 TPSA 54.4	✓ Ro5	✓ Clean	`CC(=O)C(=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
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.