Protein profile

KP13_02898

Acetoin:2,6-dichlorophenolindophenol oxidoreductase, alpha subunit

Genome: KpKP13

Gene: AHE46174.1 acoA Structure source: AlphaFold + ColabFold UniProt A0A0H3GN62

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Amino acids 319

Annotations 3

Features 7

PDB binders 7

Druggability 0.579

Overview

Basic information about this protein and its source genome.

Accession: KP13_02898
Assembly: Klebsiella pneumoniae subsp. pneumoniae Kp13, complete sequence
Gene: AHE46174.1 acoA
Status: annotated
Amino acids: 319
Structure source: AlphaFold + ColabFold

GO:0016624 Catalysis of an oxidation-reduction (redox) reaction in which an aldehyde or ketone (oxo) group acts as a hydrogen or electron donor and reduces a disulfide. GO:0004739 Catalysis of the reaction: N(6)-[(R)-lipoyl]-L-lysyl-[protein] + pyruvate + H+ = N(6)-[(R)-S(8)-acetyldihydrolipoyl]-L-lysyl-[protein] + CO2. GO:0006086 The chemical reactions and pathways resulting in the formation of acetyl-CoA from pyruvate. In most organisms, this pathway links glycolysis to the TCA cycle, by a series of three reactions carried out by a multisubunit complex called the 'pyruvate dehydrogenase complex', even though pyruvate dehydrogenase activity describes only one of those reactions. The combination of the three reactions can be summarized as: pyruvate + coenzyme A + NAD+ -> acetyl-CoA + CO2 + NADH.

Target profile

Computed evidence for target prioritization.

Human off-target: hit
Human identity (%): 36.76
Human E-value: 5.18e-62
Gut microbiome off-target: hit
Essential (DEG): Y
DEG identity (%): 43.218
DEG E-value: 1.31e-74
Localization: Cytoplasmic
ColabFold pLDDT: 96.77

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 0.579

Structure A0A0H3GN62

Pocket Pocket 9

P2Rank 0.84

Structure A0A0H3GN62

Pocket Pocket 1

ColabFold model

FPocket 0.471 · Pocket 1

P2Rank 0.883 · Pocket 1

Core conservation Accessory gene

Roary accessory

CoreCruncher accessory

Gut microbiome 56 / 4744 genomes with a hit

Normalized 0.012

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

3 GO

Gene Ontology (GO)

GO:0016624 Catalysis of an oxidation-reduction (redox) reaction in which an aldehyde or ketone (oxo) group acts as a hydrogen or electron donor and reduces a disulfide.
GO:0004739 Catalysis of the reaction: N(6)-[(R)-lipoyl]-L-lysyl-[protein] + pyruvate + H+ = N(6)-[(R)-S(8)-acetyldihydrolipoyl]-L-lysyl-[protein] + CO2.
GO:0006086 The chemical reactions and pathways resulting in the formation of acetyl-CoA from pyruvate. In most organisms, this pathway links glycolysis to the TCA cycle, by a series of three reactions carried out by a multisubunit complex called the 'pyruvate dehydrogenase complex', even though pyruvate dehydrogenase activity describes only one of those reactions. The combination of the three reactions can be summarized as: pyruvate + coenzyme A + NAD+ -> acetyl-CoA + CO2 + NADH.

Sequence Features

Domain/signature hits from InterPro and related databases.

7 records

Show feature table

Start	End	DB	Term	Name
3	318	SUPERFAMILY	SSF52518	Thiamin diphosphate-binding fold (THDP-binding)
3	318	InterPro	IPR029061	Thiamin diphosphate-binding fold
10	300	CDD	cd02000	TPP_E1_PDC_ADC_BCADC
2	317	PANTHER	PTHR11516	PYRUVATE DEHYDROGENASE E1 COMPONENT, ALPHA SUBUNIT BACTERIAL AND ORGANELLAR
1	319	Gene3D	G3DSA:3.40.50.970	-
12	308	Pfam	PF00676	Dehydrogenase E1 component
12	308	InterPro	IPR001017	Dehydrogenase, E1 component

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_A0A0H3GN62	AlphaFold	—	—	full sequence	—	Viewing
ColabFold KP13_02898	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
9				0.579
1				0.288

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	Sticks	Spheres	Surfaces	Score	Probability	Labels	Zoom	Positions
1				13.03	0.672

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				0.471

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	Sticks	Spheres	Surfaces	Score	Probability	Labels	Zoom	Positions
1				15.95	0.766
2				1.53	0.023

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.

73 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
4MV	1UMC	Q5SLR4	116.2 Da LogP 1.51 TPSA 37.3	✓ Ro5	✓ Clean	`CC(C)CCC(=O)O`
A5X	6CFO	P08559	533.4 Da LogP 0.47 TPSA 226.5	2 viol.	✓ Clean	`Cc1c(sc([n+]1Cc2cnc(nc2N)C)[C@@](C)(O)P(=O)O)CC…`
BEN	1V11	P12694	120.2 Da LogP 0.97 TPSA 49.9	✓ Ro5	✓ Clean	`[H]/N=C(\c1ccccc1)/N`
THV	2BEU	P12694	496.4 Da LogP 1.75 TPSA 189.2	✓ Ro5	✓ Clean	`Cc1c(sc([n+]1Cc2cnc(nc2N)C)[C-](C(C)C)O)CCO[P@@…`
THW	2BEW	P12694	530.4 Da LogP 2.14 TPSA 189.2	1 viol.	✓ Clean	`Cc1c(sc([n+]1Cc2cnc(nc2N)C)[C-](c3ccccc3)O)CCO[…`
THY	2BEV	P12694	510.4 Da LogP 2.14 TPSA 189.2	1 viol.	✓ Clean	`CC[C@H](C)[C-](c1[n+](c(c(s1)CCO[P@](=O)(O)OP(=…`
TZD	2BFC	P12694	440.3 Da LogP 0.72 TPSA 187.1	✓ Ro5	✓ Clean	`Cc1ncc(c(n1)N)CN2C(=C(SC2=O)CCO[P@@](=O)(O)OP(=…`

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).

Ligand	UniProt (homolog)	pchembl	MW · LogP · TPSA	Lipinski	PAINS	SMILES
CHEMBL5419102	P29804	8.35	397.5 Da LogP 3.74 TPSA 87.3	✓ Ro5	✓ Clean	`COc1ccc(C(=O)OCCc2scc(Cc3cnc(C)nc3N)c2C)cc1`
CHEMBL5417802	P29804	8.30	424.6 Da LogP 3.39 TPSA 82.3	✓ Ro5	✓ Clean	`COc1ccc(C2(NCCc3scc(Cc4cnc(C)nc4N)c3C)COC2)cc1`
CHEMBL5420203	P29804	7.76	402.5 Da LogP 2.89 TPSA 90.6	✓ Ro5	✓ Clean	`COc1ccc(C(=O)OCC[C@H]2SCN(Cc3cnc(C)nc3N)[C@H]2C…`
0YN	P29804	7.75	263.4 Da LogP 1.86 TPSA 72.0	✓ Ro5	✓ Clean	`Cc1c(csc1CCO)Cc2cnc(nc2N)C`
CHEMBL5440127	P29804	7.59	396.5 Da LogP 3.31 TPSA 90.1	✓ Ro5	✓ Clean	`COc1ccc(C(=O)NCCc2scc(Cc3cnc(C)nc3N)c2C)cc1`
CHEMBL5271689	P29804	7.52	419.5 Da LogP 2.30 TPSA 122.5	✓ Ro5	✓ Clean	`COc1ccc(-c2cn(CCCCc3cn(Cc4cnc(C)nc4N)nn3)nn2)cc1`
CHEMBL5408769	P29804	7.50	368.4 Da LogP 1.42 TPSA 118.0	✓ Ro5	✓ Clean	`COc1ccc(C(=O)OCCc2cn(Cc3cnc(C)nc3N)nn2)cc1`
CHEMBL5417344	P29804	7.41	395.5 Da LogP 1.07 TPSA 113.0	✓ Ro5	✓ Clean	`COc1ccc(C2(NCCc3cn(Cc4cnc(C)nc4N)nn3)COC2)cc1`
CHEMBL5290932	P29804	7.40	305.3 Da LogP 0.23 TPSA 131.8	✓ Ro5	✓ Clean	`Cc1ncc(Cn2cc(CCCCC(=O)NO)nn2)c(N)n1`
CHEMBL5268763	P29804	7.35	291.3 Da LogP -0.16 TPSA 131.8	✓ Ro5	✓ Clean	`Cc1ncc(Cn2cc(CCCC(=O)NO)nn2)c(N)n1`
DXH	P08559	7.04	503.5 Da LogP 5.75 TPSA 97.6	2 viol.	✓ Clean	`Cc1ccc(cc1Nc2c3cnn(c3nc(n2)c4cccnc4)C)C(=O)Nc5c…`
CHEMBL5437447	P29804	6.98	268.4 Da LogP 1.01 TPSA 75.3	✓ Ro5	✓ Clean	`Cc1ncc(CN2CS[C@H](CCO)[C@@H]2C)c(N)n1`
CHEMBL4277786	P29804	6.82	234.3 Da LogP -0.46 TPSA 102.7	✓ Ro5	✓ Clean	`Cc1ncc(Cn2cc(CCO)nn2)c(N)n1`
CHEMBL5406774	P29804	6.76	367.4 Da LogP 0.99 TPSA 120.8	✓ Ro5	✓ Clean	`COc1ccc(C(=O)NCCc2cn(Cc3cnc(C)nc3N)nn2)cc1`
DWT	P08559	6.35	503.5 Da LogP 5.75 TPSA 97.6	2 viol.	✓ Clean	`Cc1ccc(cc1Nc2c3cn(nc3nc(n2)c4cccnc4)C)C(=O)Nc5c…`
CHEMBL1061	P26284	—	223.3 Da LogP 1.29 TPSA 66.4	✓ Ro5	✓ Clean	`O=C1NC(=O)C(Cc2ccc(O)cc2)S1`

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
ZINC26575565	1.000	223.3 Da LogP 1.29 TPSA 66.4	✓ Ro5	✓ Clean	`O=C1NC(=O)[C@H](Cc2ccc(O)cc2)S1`
ZINC26575566	1.000	223.3 Da LogP 1.29 TPSA 66.4	✓ Ro5	✓ Clean	`O=C1NC(=O)[C@@H](Cc2ccc(O)cc2)S1`
ZINC1453005	0.750	241.7 Da LogP 2.23 TPSA 46.2	✓ Ro5	✓ Clean	`O=C1NC(=O)[C@H](Cc2ccc(Cl)cc2)S1`
ZINC1453006	0.750	241.7 Da LogP 2.23 TPSA 46.2	✓ Ro5	✓ Clean	`O=C1NC(=O)[C@@H](Cc2ccc(Cl)cc2)S1`
ZINC22059407	0.750	225.2 Da LogP 1.72 TPSA 46.2	✓ Ro5	✓ Clean	`O=C1NC(=O)[C@H](Cc2ccc(F)cc2)S1`
ZINC22059410	0.750	225.2 Da LogP 1.72 TPSA 46.2	✓ Ro5	✓ Clean	`O=C1NC(=O)[C@@H](Cc2ccc(F)cc2)S1`
ZINC136823231	0.727	286.1 Da LogP 2.34 TPSA 46.2	✓ Ro5	✓ Clean	`O=C1NC(=O)[C@@H](Cc2ccc(Br)cc2)S1`
ZINC136823276	0.727	286.1 Da LogP 2.34 TPSA 46.2	✓ Ro5	✓ Clean	`O=C1NC(=O)[C@H](Cc2ccc(Br)cc2)S1`
ZINC1395202	0.727	222.3 Da LogP 1.16 TPSA 72.2	✓ Ro5	Alert	`Nc1ccc(C[C@@H]2SC(=O)NC2=O)cc1`
ZINC1395203	0.727	222.3 Da LogP 1.16 TPSA 72.2	✓ Ro5	Alert	`Nc1ccc(C[C@H]2SC(=O)NC2=O)cc1`
ZINC1453011	0.727	221.3 Da LogP 1.89 TPSA 46.2	✓ Ro5	✓ Clean	`Cc1ccc(C[C@@H]2SC(=O)NC2=O)cc1`
ZINC1453012	0.727	221.3 Da LogP 1.89 TPSA 46.2	✓ Ro5	✓ Clean	`Cc1ccc(C[C@H]2SC(=O)NC2=O)cc1`
ZINC1453007	0.719	207.3 Da LogP 1.58 TPSA 46.2	✓ Ro5	✓ Clean	`O=C1NC(=O)[C@H](Cc2ccccc2)S1`
ZINC1453008	0.719	207.3 Da LogP 1.58 TPSA 46.2	✓ Ro5	✓ Clean	`O=C1NC(=O)[C@@H](Cc2ccccc2)S1`
ZINC33876997	0.686	239.3 Da LogP 0.99 TPSA 86.6	✓ Ro5	Alert	`O=C1NC(=O)[C@@H](Cc2ccc(O)c(O)c2)S1`
ZINC33876999	0.686	239.3 Da LogP 0.99 TPSA 86.6	✓ Ro5	Alert	`O=C1NC(=O)[C@H](Cc2ccc(O)c(O)c2)S1`
ZINC1386519	0.676	208.2 Da LogP 0.98 TPSA 59.1	✓ Ro5	✓ Clean	`O=C1NC(=O)[C@H](Cc2ccncc2)S1`
ZINC4052182	0.676	208.2 Da LogP 0.98 TPSA 59.1	✓ Ro5	✓ Clean	`O=C1NC(=O)[C@@H](Cc2ccncc2)S1`
ZINC144529043	0.667	223.3 Da LogP 1.29 TPSA 66.4	✓ Ro5	✓ Clean	`O=C1NC(=O)[C@H](Cc2cccc(O)c2)S1`
ZINC144529255	0.667	223.3 Da LogP 1.29 TPSA 66.4	✓ Ro5	✓ Clean	`O=C1NC(=O)[C@@H](Cc2cccc(O)c2)S1`
ZINC1841074	0.636	200.3 Da LogP 3.85 TPSA 37.3	✓ Ro5	✓ Clean	`CC(C)CCCCCCCCC(=O)O`
ZINC2013445	0.636	214.3 Da LogP 4.24 TPSA 37.3	✓ Ro5	✓ Clean	`CC(C)CCCCCCCCCC(=O)O`
ZINC2575042	0.636	228.4 Da LogP 4.63 TPSA 37.3	✓ Ro5	✓ Clean	`CC(C)CCCCCCCCCCC(=O)O`
ZINC218823900	0.632	257.7 Da LogP 1.94 TPSA 66.4	✓ Ro5	✓ Clean	`O=C1NC(=O)[C@H](Cc2ccc(O)c(Cl)c2)S1`
ZINC218823984	0.632	257.7 Da LogP 1.94 TPSA 66.4	✓ Ro5	✓ Clean	`O=C1NC(=O)[C@@H](Cc2ccc(O)c(Cl)c2)S1`
ZINC218824096	0.632	302.1 Da LogP 2.05 TPSA 66.4	✓ Ro5	✓ Clean	`O=C1NC(=O)[C@H](Cc2ccc(O)c(Br)c2)S1`
ZINC218824164	0.632	302.1 Da LogP 2.05 TPSA 66.4	✓ Ro5	✓ Clean	`O=C1NC(=O)[C@@H](Cc2ccc(O)c(Br)c2)S1`
ZINC8215517	0.618	425.3 Da LogP 0.84 TPSA 169.0	✓ Ro5	✓ Clean	`Cc1ncc(C[n+]2csc(CCO[P@@](=O)(O)OP(=O)(O)O)c2C)…`
ZINC1037079	0.615	265.3 Da LogP 1.51 TPSA 72.5	✓ Ro5	✓ Clean	`CC(=O)Oc1ccc(C[C@@H]2SC(=O)NC2=O)cc1`
ZINC1037080	0.615	265.3 Da LogP 1.51 TPSA 72.5	✓ Ro5	✓ Clean	`CC(=O)Oc1ccc(C[C@H]2SC(=O)NC2=O)cc1`
ZINC34472979	0.600	281.3 Da LogP 1.04 TPSA 92.7	✓ Ro5	✓ Clean	`O=C(O)COc1ccc(C[C@H]2SC(=O)NC2=O)cc1`
ZINC34472980	0.600	281.3 Da LogP 1.04 TPSA 92.7	✓ Ro5	✓ Clean	`O=C(O)COc1ccc(C[C@@H]2SC(=O)NC2=O)cc1`
ZINC148984399	0.585	253.3 Da LogP 1.29 TPSA 75.6	✓ Ro5	✓ Clean	`COc1cc(C[C@@H]2SC(=O)NC2=O)ccc1O`
ZINC148984633	0.585	253.3 Da LogP 1.29 TPSA 75.6	✓ Ro5	✓ Clean	`COc1cc(C[C@H]2SC(=O)NC2=O)ccc1O`
ZINC4108904	0.585	273.3 Da LogP 1.77 TPSA 64.0	✓ Ro5	✓ Clean	`O=C1NC(=O)[C@@H](Cc2ccc(-n3cccn3)cc2)S1`
ZINC4108906	0.585	273.3 Da LogP 1.77 TPSA 64.0	✓ Ro5	✓ Clean	`O=C1NC(=O)[C@H](Cc2ccc(-n3cccn3)cc2)S1`
ZINC145838685	0.583	200.3 Da LogP 3.70 TPSA 37.3	✓ Ro5	✓ Clean	`CC(C)CCC[C@@H](C)CCCC(=O)O`
ZINC145838882	0.583	200.3 Da LogP 3.70 TPSA 37.3	✓ Ro5	✓ Clean	`CC(C)CCC[C@H](C)CCCC(=O)O`
ZINC9109306	0.575	255.7 Da LogP 2.54 TPSA 46.2	✓ Ro5	✓ Clean	`Cc1ccc(C[C@H]2SC(=O)NC2=O)cc1Cl`
ZINC9109307	0.575	255.7 Da LogP 2.54 TPSA 46.2	✓ Ro5	✓ Clean	`Cc1ccc(C[C@@H]2SC(=O)NC2=O)cc1Cl`
ZINC1396290	0.564	222.3 Da LogP 1.16 TPSA 72.2	✓ Ro5	✓ Clean	`Nc1cccc(C[C@@H]2SC(=O)NC2=O)c1`
ZINC1396291	0.564	222.3 Da LogP 1.16 TPSA 72.2	✓ Ro5	✓ Clean	`Nc1cccc(C[C@H]2SC(=O)NC2=O)c1`
ZINC218823161	0.564	225.2 Da LogP 1.72 TPSA 46.2	✓ Ro5	✓ Clean	`O=C1NC(=O)[C@H](Cc2cccc(F)c2)S1`
ZINC218823233	0.564	225.2 Da LogP 1.72 TPSA 46.2	✓ Ro5	✓ Clean	`O=C1NC(=O)[C@@H](Cc2cccc(F)c2)S1`
ZINC218823522	0.564	241.7 Da LogP 2.23 TPSA 46.2	✓ Ro5	✓ Clean	`O=C1NC(=O)[C@H](Cc2cccc(Cl)c2)S1`
ZINC218823606	0.564	241.7 Da LogP 2.23 TPSA 46.2	✓ Ro5	✓ Clean	`O=C1NC(=O)[C@@H](Cc2cccc(Cl)c2)S1`
ZINC218823701	0.564	286.1 Da LogP 2.34 TPSA 46.2	✓ Ro5	✓ Clean	`O=C1NC(=O)[C@H](Cc2cccc(Br)c2)S1`
ZINC218823783	0.564	286.1 Da LogP 2.34 TPSA 46.2	✓ Ro5	✓ Clean	`O=C1NC(=O)[C@@H](Cc2cccc(Br)c2)S1`
ZINC33968825	0.564	335.5 Da LogP 3.88 TPSA 66.4	✓ Ro5	✓ Clean	`CC(C)(C)c1cc(C[C@H]2SC(=O)NC2=O)cc(C(C)(C)C)c1O`
ZINC33968826	0.564	335.5 Da LogP 3.88 TPSA 66.4	✓ Ro5	✓ Clean	`CC(C)(C)c1cc(C[C@@H]2SC(=O)NC2=O)cc(C(C)(C)C)c1O`

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.