Protein profile

KP13_01742

Fatty acid oxidation complex subunit alpha multifunctional enzyme

Genome: KpKP13

Gene: fadB AHE46955.1 Structure source: AlphaFold + ColabFold UniProt A0A0H3GPY7

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Amino acids 729

Annotations 14

Features 32

PDB binders 8

Druggability 0.91

Overview

Basic information about this protein and its source genome.

Accession: KP13_01742
Assembly: Klebsiella pneumoniae subsp. pneumoniae Kp13, complete sequence
Gene: fadB AHE46955.1
Status: annotated
Amino acids: 729
Structure source: AlphaFold + ColabFold

GO:0004165 Catalysis of the reactions: a (3Z)-enoyl-CoA = a 4-saturated (2E)-enoyl-CoA or a (3E)-enoyl-CoA = a 4-saturated (2E)-enoyl-CoA. GO:0016616 Catalysis of an oxidation-reduction (redox) reaction in which a CH-OH group acts as a hydrogen or electron donor and reduces NAD+ or NADP. GO:0004300 Catalysis of the reaction: a 3-hydroxy-fatty acyl-CoA = a enoyl-CoA + H2O. This reaction usually occurs in the reverse direction, leading to the reduction of the double bound of enoyl-CoA in position 2 or 3. Specific reactions catalyzed include: a 4-saturated-(3S)-3-hydroxyacyl-CoA = a (3E)-enoyl-CoA + H2O and a (3S)-3-hydroxyacyl-CoA = a (2E)-enoyl-CoA + H2O. GO:0006631 The chemical reactions and pathways involving fatty acids, aliphatic monocarboxylic acids liberated from naturally occurring fats and oils by hydrolysis. GO:0070403 Binding to the oxidized form, NAD, of nicotinamide adenine dinucleotide, a coenzyme involved in many redox and biosynthetic reactions. GO:0016491 Catalysis of an oxidation-reduction (redox) reaction, a reversible chemical reaction in which the oxidation state of an atom or atoms within a molecule is altered. One substrate acts as a hydrogen or electron donor and becomes oxidized, while the other acts as hydrogen or electron acceptor and becomes reduced.

Target profile

Computed evidence for target prioritization.

Human off-target: hit
Human identity (%): 42.742
Human E-value: 6.9e-25
Gut microbiome off-target: hit
Essential (DEG): Y
DEG identity (%): 55.804
DEG E-value: 0.0
Localization: Cytoplasmic
ColabFold pLDDT: 95.37

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 0.91

Structure A0A0H3GPY7

Pocket Pocket 1

P2Rank 0.861

Structure A0A0H3GPY7

Pocket Pocket 1

ColabFold model

FPocket 0.906 · Pocket 1

P2Rank 0.861 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 143 / 4744 genomes with a hit

Normalized 0.03

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

14 GO

Gene Ontology (GO)

GO:0004165 Catalysis of the reactions: a (3Z)-enoyl-CoA = a 4-saturated (2E)-enoyl-CoA or a (3E)-enoyl-CoA = a 4-saturated (2E)-enoyl-CoA.
GO:0016616 Catalysis of an oxidation-reduction (redox) reaction in which a CH-OH group acts as a hydrogen or electron donor and reduces NAD+ or NADP.
GO:0004300 Catalysis of the reaction: a 3-hydroxy-fatty acyl-CoA = a enoyl-CoA + H2O. This reaction usually occurs in the reverse direction, leading to the reduction of the double bound of enoyl-CoA in position 2 or 3. Specific reactions catalyzed include: a 4-saturated-(3S)-3-hydroxyacyl-CoA = a (3E)-enoyl-CoA + H2O and a (3S)-3-hydroxyacyl-CoA = a (2E)-enoyl-CoA + H2O.
GO:0006631 The chemical reactions and pathways involving fatty acids, aliphatic monocarboxylic acids liberated from naturally occurring fats and oils by hydrolysis.
GO:0070403 Binding to the oxidized form, NAD, of nicotinamide adenine dinucleotide, a coenzyme involved in many redox and biosynthetic reactions.
GO:0016491 Catalysis of an oxidation-reduction (redox) reaction, a reversible chemical reaction in which the oxidation state of an atom or atoms within a molecule is altered. One substrate acts as a hydrogen or electron donor and becomes oxidized, while the other acts as hydrogen or electron acceptor and becomes reduced.
GO:0036125 A multienzyme complex possessing three kinds of enzymes that catalyze the chain reactions in the fatty acid beta-oxidation cycle, enoyl-CoA hydratase (ECH), 3-hydroxyacyl-CoA dehydrogenase (HACD), and acetyl-CoA C-acyltransferase (KACT).
GO:0003824 Catalysis of a biochemical reaction at physiological temperatures. In biologically catalyzed reactions, the reactants are known as substrates, and the catalysts are naturally occurring macromolecular substances known as enzymes. Enzymes possess specific binding sites for substrates, and are usually composed wholly or largely of protein, but RNA that has catalytic activity (ribozyme) is often also regarded as enzymatic.
GO:0008692 Catalysis of the reaction: (S)-3-hydroxybutanoyl-CoA = (R)-3-hydroxybutanoyl-CoA.
GO:0009062 The chemical reactions and pathways resulting in the breakdown 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:0003857 Catalysis of the reaction: a (3S)-3-hydroxyacyl-CoA + NAD+ = a 3-oxoacyl-CoA + NADH + H+.
GO:0018812 Catalysis of the reaction: a 3-hydroxy-fatty acyl-CoA = a (2E)-enoyl-CoA + H2O.
GO:0016509 Catalysis of the reaction: a long-chain (3S)-3-hydroxy fatty acyl-CoA + NAD+ = a long-chain 3-oxo-fatty acyl-CoA + H+ + NADH. A long-chain fatty acid has an aliphatic tail containing 13 to 22 carbons.
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).

Sequence Features

Domain/signature hits from InterPro and related databases.

32 records

Show feature table

Start	End	DB	Term	Name
313	498	FunFam	G3DSA:3.40.50.720:FF:000009	Fatty oxidation complex, alpha subunit
496	592	Pfam	PF00725	3-hydroxyacyl-CoA dehydrogenase, C-terminal domain
496	592	InterPro	IPR006108	3-hydroxyacyl-CoA dehydrogenase, C-terminal
627	691	Pfam	PF00725	3-hydroxyacyl-CoA dehydrogenase, C-terminal domain
627	691	InterPro	IPR006108	3-hydroxyacyl-CoA dehydrogenase, C-terminal
14	203	CDD	cd06558	crotonase-like
1	714	NCBIfam	TIGR02437	fatty acid oxidation complex subunit alpha FadB
1	714	InterPro	IPR012799	Fatty oxidation complex, alpha subunit FadB
499	718	Gene3D	G3DSA:1.10.1040.50	-
106	126	ProSitePatterns	PS00166	Enoyl-CoA hydratase/isomerase signature.
106	126	InterPro	IPR018376	Enoyl-CoA hydratase/isomerase, conserved site
499	714	FunFam	G3DSA:1.10.1040.50:FF:000001	Fatty acid oxidation complex subunit alpha
622	714	SUPERFAMILY	SSF48179	6-phosphogluconate dehydrogenase C-terminal domain-like
622	714	InterPro	IPR008927	6-phosphogluconate dehydrogenase-like, C-terminal domain superfamily
493	517	ProSitePatterns	PS00067	3-hydroxyacyl-CoA dehydrogenase signature.
493	517	InterPro	IPR006180	3-hydroxyacyl-CoA dehydrogenase, conserved site
4	714	PANTHER	PTHR43612	TRIFUNCTIONAL ENZYME SUBUNIT ALPHA
3	303	SUPERFAMILY	SSF52096	ClpP/crotonase
3	303	InterPro	IPR029045	ClpP/crotonase-like domain superfamily
316	494	Pfam	PF02737	3-hydroxyacyl-CoA dehydrogenase, NAD binding domain
316	494	InterPro	IPR006176	3-hydroxyacyl-CoA dehydrogenase, NAD binding
495	639	SUPERFAMILY	SSF48179	6-phosphogluconate dehydrogenase C-terminal domain-like
495	639	InterPro	IPR008927	6-phosphogluconate dehydrogenase-like, C-terminal domain superfamily
1	715	Hamap	MF_01621	Fatty acid oxidation complex subunit alpha [fadB].
1	715	InterPro	IPR012799	Fatty oxidation complex, alpha subunit FadB
314	495	SUPERFAMILY	SSF51735	NAD(P)-binding Rossmann-fold domains
314	495	InterPro	IPR036291	NAD(P)-binding domain superfamily
1	312	Gene3D	G3DSA:3.90.226.10	-
313	498	Gene3D	G3DSA:3.40.50.720	-
1	312	FunFam	G3DSA:3.90.226.10:FF:000018	Fatty acid oxidation complex subunit alpha
14	206	Pfam	PF00378	Enoyl-CoA hydratase/isomerase
14	206	InterPro	IPR001753	Enoyl-CoA hydratase/isomerase

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_A0A0H3GPY7	AlphaFold	—	—	full sequence	—	Viewing
ColabFold KP13_01742	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				0.91
28				0.262

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	18.16	0.816
2	17.3	0.8
3	7.09	0.368
4	2.21	0.053
5	1.51	0.022

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				0.906
16				0.282

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	19.0	0.833
2	15.93	0.766
3	4.42	0.187
4	1.45	0.019
5	1.42	0.018

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.

58 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
3H9	3ZWA	P07896	877.7 Da LogP -3.31 TPSA 395.2	3 viol.	✓ Clean	`CCC[C@@H](CC(=O)SCCNC(=O)CCNC(=O)[C@@H](C(C)(C)…`
3HC	1F12	Q16836	853.6 Da LogP -1.56 TPSA 383.9	3 viol.	✓ Clean	`CC(CC(=O)SCCNC(=O)CCNC(=O)[C@@H](C(C)(C)CO[P@](…`
CAA	4KUH	C4IEM5	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…`
HSC	3ZWC	P07896	933.8 Da LogP -1.75 TPSA 395.2	3 viol.	✓ Clean	`CCCCCCC[C@@H](CC(=O)SCCNC(=O)CCNC(=O)[C@@H](C(C…`
N8E	1WDL	P28793	350.5 Da LogP 2.42 TPSA 66.4	✓ Ro5	✓ Clean	`CCCCCCCCOCCOCCOCCOCCOCCO`
T1G	3ZW9	P07896	863.6 Da LogP -3.85 TPSA 395.2	3 viol.	✓ Clean	`C[C@@H]([C@H](C)O)C(=O)SCCNC(=O)CCNC(=O)[C@@H](…`
TC6	3ZWB	P07896	859.6 Da LogP -2.51 TPSA 374.9	2 viol.	✓ Clean	`CCC/C=C/C(=O)SCCNC(=O)CCNC(=O)[C@@H](C(C)(C)COP…`
ZOZ	5OMO	P07896	935.8 Da LogP 0.98 TPSA 380.7	3 viol.	✓ Clean	`CCCCCCCC(=O)CC(=O)SCCNC(=O)CCNC(=O)[C@@H](C(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
ZINC100014200	1.000	494.7 Da LogP 4.02 TPSA 84.8	✓ Ro5	✓ Clean	`CCCCCCCCCCCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC100070166	1.000	290.4 Da LogP 3.17 TPSA 47.9	✓ Ro5	✓ Clean	`CCCCCCCCCCOCCOCCOCCO`
ZINC100310628	1.000	478.7 Da LogP 4.78 TPSA 75.6	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCCOCCOCCOCCOCCOCCOCCO`
ZINC100365196	1.000	302.5 Da LogP 4.71 TPSA 38.7	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCCOCCOCCO`
ZINC101772322	1.000	434.7 Da LogP 4.76 TPSA 66.4	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCCOCCOCCOCCOCCOCCO`
ZINC103600921	1.000	466.7 Da LogP 3.24 TPSA 84.8	✓ Ro5	✓ Clean	`CCCCCCCCCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC14880431	1.000	378.6 Da LogP 3.20 TPSA 66.4	✓ Ro5	✓ Clean	`CCCCCCCCCCOCCOCCOCCOCCOCCO`
ZINC14881140	1.000	306.4 Da LogP 2.41 TPSA 57.2	✓ Ro5	✓ Clean	`CCCCCCCCOCCOCCOCCOCCO`
ZINC16051619	1.000	350.5 Da LogP 2.42 TPSA 66.4	✓ Ro5	✓ Clean	`CCCCCCCCOCCOCCOCCOCCOCCO`
ZINC2584424	1.000	218.3 Da LogP 2.37 TPSA 38.7	✓ Ro5	✓ Clean	`CCCCCCCCOCCOCCO`
ZINC4521877	1.000	234.3 Da LogP 1.61 TPSA 47.9	✓ Ro5	✓ Clean	`CCCCCCOCCOCCOCCO`
ZINC5273610	1.000	322.4 Da LogP 1.64 TPSA 66.4	✓ Ro5	✓ Clean	`CCCCCCOCCOCCOCCOCCOCCO`
ZINC58538366	1.000	392.6 Da LogP 3.59 TPSA 66.4	✓ Ro5	✓ Clean	`CCCCCCCCCCCOCCOCCOCCOCCOCCO`
ZINC58631420	1.000	422.6 Da LogP 3.22 TPSA 75.6	✓ Ro5	✓ Clean	`CCCCCCCCCCOCCOCCOCCOCCOCCOCCO`
ZINC59441819	1.000	318.5 Da LogP 3.95 TPSA 47.9	✓ Ro5	✓ Clean	`CCCCCCCCCCCCOCCOCCOCCO`
ZINC59622400	1.000	274.4 Da LogP 3.93 TPSA 38.7	✓ Ro5	✓ Clean	`CCCCCCCCCCCCOCCOCCO`
ZINC71788551	1.000	334.5 Da LogP 3.19 TPSA 57.2	✓ Ro5	✓ Clean	`CCCCCCCCCCOCCOCCOCCOCCO`
ZINC71788564	1.000	262.4 Da LogP 2.39 TPSA 47.9	✓ Ro5	✓ Clean	`CCCCCCCCOCCOCCOCCO`
ZINC71788567	1.000	406.6 Da LogP 3.98 TPSA 66.4	✓ Ro5	✓ Clean	`CCCCCCCCCCCCOCCOCCOCCOCCOCCO`
ZINC8214594	1.000	362.6 Da LogP 3.97 TPSA 57.2	✓ Ro5	✓ Clean	`CCCCCCCCCCCCOCCOCCOCCOCCO`
ZINC88260008	1.000	390.6 Da LogP 4.75 TPSA 57.2	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCCOCCOCCOCCOCCO`
ZINC95784968	1.000	450.7 Da LogP 4.00 TPSA 75.6	✓ Ro5	✓ Clean	`CCCCCCCCCCCCOCCOCCOCCOCCOCCOCCO`
ZINC95863931	1.000	464.7 Da LogP 4.39 TPSA 75.6	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCOCCOCCOCCOCCOCCOCCO`
ZINC1849711	0.950	202.3 Da LogP 3.14 TPSA 29.5	✓ Ro5	✓ Clean	`CCCCCCCCCCOCCO`
ZINC1850542	0.950	216.4 Da LogP 3.53 TPSA 29.5	✓ Ro5	✓ Clean	`CCCCCCCCCCCOCCO`
ZINC2555269	0.950	220.3 Da LogP 1.22 TPSA 47.9	✓ Ro5	✓ Clean	`CCCCCOCCOCCOCCO`
ZINC59660505	0.950	244.4 Da LogP 4.31 TPSA 29.5	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCOCCO`
ZINC8437287	0.950	230.4 Da LogP 3.92 TPSA 29.5	✓ Ro5	✓ Clean	`CCCCCCCCCCCCOCCO`
ZINC85733754	0.950	258.4 Da LogP 4.70 TPSA 29.5	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCCOCCO`
ZINC1644613	0.810	206.3 Da LogP 0.83 TPSA 47.9	✓ Ro5	✓ Clean	`CCCCOCCOCCOCCO`
ZINC59545536	0.773	258.4 Da LogP 4.70 TPSA 29.5	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCOCCCO`
ZINC95831576	0.773	230.4 Da LogP 3.92 TPSA 29.5	✓ Ro5	✓ Clean	`CCCCCCCCCCOCCCCO`
ZINC1627284	0.700	214.4 Da LogP 4.94 TPSA 9.2	✓ Ro5	✓ Clean	`CCCCCCCOCCCCCCC`
ZINC2564179	0.700	214.4 Da LogP 4.94 TPSA 9.2	✓ Ro5	✓ Clean	`CCCCCCCCOCCCCCC`
ZINC100302699	0.600	332.5 Da LogP 3.48 TPSA 65.0	✓ Ro5	✓ Clean	`CCCCCCCCCCCC(=O)OCCOCCOCCO`
ZINC101013974	0.600	273.5 Da LogP 3.90 TPSA 44.5	✓ Ro5	✓ Clean	`CCCCCCCCCCCCOCCOCCN`
ZINC101367966	0.600	232.3 Da LogP 1.90 TPSA 55.8	✓ Ro5	✓ Clean	`CCCCCCCC(=O)OCCOCCO`
ZINC44583812	0.600	380.6 Da LogP 3.49 TPSA 57.2	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCCCCCCCCCCS`
ZINC44583816	0.600	468.7 Da LogP 3.52 TPSA 75.6	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCOCCOCCCCCCCCCCCS`
ZINC6620298	0.600	336.5 Da LogP 3.47 TPSA 47.9	✓ Ro5	✓ Clean	`OCCOCCOCCOCCCCCCCCCCCS`
ZINC86039630	0.600	288.4 Da LogP 3.46 TPSA 55.8	✓ Ro5	✓ Clean	`CCCCCCCCCCCC(=O)OCCOCCO`
ZINC100684628	0.586	330.6 Da LogP 4.77 TPSA 29.5	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCC[N+](C)(C)CCOCCO`
ZINC4978403	0.583	248.4 Da LogP 2.00 TPSA 47.9	✓ Ro5	✓ Clean	`CCCCOCCCOCCCOCCCO`
ZINC100090646	0.571	448.6 Da LogP 4.86 TPSA 83.5	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCCOCCOCCOCCOCCOCC(=O)O`
ZINC100645716	0.571	273.5 Da LogP 4.60 TPSA 35.2	✓ Ro5	✓ Clean	`CCCCCCCCCCCCOCCC(N)=S`
ZINC100970335	0.571	331.5 Da LogP 3.44 TPSA 70.8	✓ Ro5	✓ Clean	`CCCCCCCCCCCCOCCOCCOCC(N)=O`
ZINC2041048	0.571	218.3 Da LogP 2.64 TPSA 27.7	✓ Ro5	✓ Clean	`CCCCOCCOCCOCCCC`
ZINC1697133	0.565	214.4 Da LogP 4.94 TPSA 9.2	✓ Ro5	✓ Clean	`CCCCCCCCCCCCOCC`
ZINC5650743	0.565	222.3 Da LogP 0.07 TPSA 57.2	✓ Ro5	✓ Clean	`CCOCCOCCOCCOCCO`
ZINC6403917	0.565	354.4 Da LogP 0.11 TPSA 84.8	✓ Ro5	✓ Clean	`CCOCCOCCOCCOCCOCCOCCOCCO`

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.