Protein profile

KP13_02390

Enolase

Genome: KpKP13

Gene: AHE42961.1 eno Structure source: AlphaFold + ColabFold UniProt A0A0H3GUG9

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Amino acids 432

Annotations 7

Features 44

PDB binders 10

Druggability 0.651

Overview

Basic information about this protein and its source genome.

Accession: KP13_02390
Assembly: Klebsiella pneumoniae subsp. pneumoniae Kp13, complete sequence
Gene: AHE42961.1 eno
Status: annotated
Amino acids: 432
Structure source: AlphaFold + ColabFold

4.2.1.11

GO:0000015 A multimeric enzyme complex, usually a dimer or an octamer, that catalyzes the conversion of 2-phospho-D-glycerate to phosphoenolpyruvate and water. GO:0004634 Catalysis of the reaction: 2-phospho-D-glycerate = phosphoenolpyruvate + H2O. GO:0000287 Binding to a magnesium (Mg) ion. GO:0006096 The chemical reactions and pathways resulting in the breakdown of a carbohydrate into pyruvate, with the concomitant production of a small amount of ATP and the reduction of NAD(P) to NAD(P)H. Glycolysis begins with the metabolism of a carbohydrate to generate products that can enter the pathway and ends with the production of pyruvate. Pyruvate may be converted to acetyl-coenzyme A, ethanol, lactate, or other small molecules. GO:0009986 The external part of the cell wall and/or plasma membrane. GO:0005576 The space external to the outermost structure of a cell. For cells without external protective or external encapsulating structures this refers to space outside of the plasma membrane. This term covers the host cell environment outside an intracellular parasite.

Target profile

Computed evidence for target prioritization.

Human off-target: hit
Human identity (%): 61.644
Human E-value: 4.81e-49
Gut microbiome off-target: hit
Essential (DEG): Y
DEG identity (%): 97.454
DEG E-value: 0.0
Localization: Cytoplasmic
ColabFold pLDDT: 98.24

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 0.651

Structure A0A0H3GUG9

Pocket Pocket 5

P2Rank 0.621

Structure A0A0H3GUG9

Pocket Pocket 1

ColabFold model

FPocket 0.674 · Pocket 4

P2Rank 0.561 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 3523 / 4744 genomes with a hit

Normalized 0.743

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 6 GO

Enzyme Commission (EC)

4.2.1.11

Gene Ontology (GO)

GO:0000015 A multimeric enzyme complex, usually a dimer or an octamer, that catalyzes the conversion of 2-phospho-D-glycerate to phosphoenolpyruvate and water.
GO:0004634 Catalysis of the reaction: 2-phospho-D-glycerate = phosphoenolpyruvate + H2O.
GO:0000287 Binding to a magnesium (Mg) ion.
GO:0006096 The chemical reactions and pathways resulting in the breakdown of a carbohydrate into pyruvate, with the concomitant production of a small amount of ATP and the reduction of NAD(P) to NAD(P)H. Glycolysis begins with the metabolism of a carbohydrate to generate products that can enter the pathway and ends with the production of pyruvate. Pyruvate may be converted to acetyl-coenzyme A, ethanol, lactate, or other small molecules.
GO:0009986 The external part of the cell wall and/or plasma membrane.
GO:0005576 The space external to the outermost structure of a cell. For cells without external protective or external encapsulating structures this refers to space outside of the plasma membrane. This term covers the host cell environment outside an intracellular parasite.

Sequence Features

Domain/signature hits from InterPro and related databases.

44 records

Show feature table

Start	End	DB	Term	Name
143	430	SMART	SM01192	Enolase_C_3
143	430	InterPro	IPR020810	Enolase, C-terminal TIM barrel domain
144	429	Pfam	PF00113	Enolase, C-terminal TIM barrel domain
144	429	InterPro	IPR020810	Enolase, C-terminal TIM barrel domain
128	432	FunFam	G3DSA:3.20.20.120:FF:000001	Enolase
6	414	CDD	cd03313	enolase
6	414	InterPro	IPR000941	Enolase
128	432	Gene3D	G3DSA:3.20.20.120	-
128	432	InterPro	IPR036849	Enolase-like, C-terminal domain superfamily
4	134	SMART	SM01193	Enolase_N_3
4	134	InterPro	IPR020811	Enolase, N-terminal
4	428	NCBIfam	TIGR01060	phosphopyruvate hydratase
4	428	InterPro	IPR000941	Enolase
1	127	FunFam	G3DSA:3.30.390.10:FF:000001	Enolase
1	430	PIRSF	PIRSF001400	Enolase
1	430	InterPro	IPR000941	Enolase
143	427	SUPERFAMILY	SSF51604	Enolase C-terminal domain-like
143	427	InterPro	IPR036849	Enolase-like, C-terminal domain superfamily
339	352	ProSitePatterns	PS00164	Enolase signature.
339	352	InterPro	IPR020809	Enolase, conserved site
2	416	Hamap	MF_00318	Enolase [eno].
2	416	InterPro	IPR000941	Enolase
339	353	PRINTS	PR00148	Enolase signature
339	353	InterPro	IPR000941	Enolase
368	385	PRINTS	PR00148	Enolase signature
368	385	InterPro	IPR000941	Enolase
37	51	PRINTS	PR00148	Enolase signature
37	51	InterPro	IPR000941	Enolase
316	327	PRINTS	PR00148	Enolase signature
316	327	InterPro	IPR000941	Enolase
107	123	PRINTS	PR00148	Enolase signature
107	123	InterPro	IPR000941	Enolase
165	178	PRINTS	PR00148	Enolase signature
165	178	InterPro	IPR000941	Enolase
1	127	Gene3D	G3DSA:3.30.390.10	-
1	127	InterPro	IPR029017	Enolase-like, N-terminal
4	134	Pfam	PF03952	Enolase, N-terminal domain
3	426	PANTHER	PTHR11902	ENOLASE
3	426	InterPro	IPR000941	Enolase
1	416	SFLD	SFLDG00178	enolase
1	416	SFLD	SFLDF00002	enolase
1	416	InterPro	IPR000941	Enolase
3	138	SUPERFAMILY	SSF54826	Enolase N-terminal domain-like
3	138	InterPro	IPR029017	Enolase-like, N-terminal

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_A0A0H3GUG9	AlphaFold	—	—	full sequence	—	Viewing
ColabFold KP13_02390	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
5				0.651
16				0.355
17				0.258
22				0.249

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				11.85	0.628

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				0.674

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				10.41	0.559

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.

45 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
0V5	3UJS	P09104	170.1 Da LogP -0.43 TPSA 104.1	✓ Ro5	✓ Clean	`C[C@H](C(=O)O)OP(=O)(O)O`
2PG	6BFY	P0A6P9	186.1 Da LogP -1.46 TPSA 124.3	✓ Ro5	✓ Clean	`C([C@H](C(=O)O)OP(=O)(O)O)O`
4NG	6D3Q	P0A6P9	197.1 Da LogP -1.53 TPSA 118.3	✓ Ro5	✓ Clean	`C1[C@@H](C(=O)N([C@H]1O)O)P(=O)(O)O`
5TX	5EU9	P09104	211.1 Da LogP -1.14 TPSA 118.3	✓ Ro5	✓ Clean	`C[C@@]1(C[C@@H](N(C1=O)O)O)P(=O)(O)O`
6BM	5IDZ	P09104	195.1 Da LogP -0.46 TPSA 98.1	✓ Ro5	✓ Clean	`C1C[C@@H](C(=O)N(C1)O)P(=O)(O)O`
KVM	6NPF	P0A6P9	195.1 Da LogP -1.32 TPSA 115.1	✓ Ro5	✓ Clean	`C1[C@@H](C(=O)N(C1=O)O)P(=O)(O)O`
PAH	4ZA0	P09104	155.0 Da LogP -1.33 TPSA 106.9	✓ Ro5	✓ Clean	`C(C(=O)NO)P(=O)(O)O`
PEP	6BFZ	P0A6P9	168.0 Da LogP -0.31 TPSA 104.1	✓ Ro5	✓ Clean	`C=C(C(=O)O)OP(=O)(O)O`
TLA	6NPF	P0A6P9	150.1 Da LogP -2.12 TPSA 115.1	✓ Ro5	✓ Clean	`[C@@H]([C@H](C(=O)O)O)(C(=O)O)O`
XSP	3UJS	P09104	184.0 Da LogP -1.25 TPSA 121.1	✓ Ro5	✓ Clean	`C(=O)[C@H](C(=O)O)OP(=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
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`
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`
ZINC12359024	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@H](O)[C@H](O)[C@@H](O)C(=O)O`
ZINC13533920	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@H](O)[C@@H](O)[C@@H](O)C(=O)O`
ZINC1532740	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@H](O)[C@@H](O)[C@H](O)C(=O)O`
ZINC1549593	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@H](O)[C@H](O)[C@@H](O)[C@@H](O)C(=O)O`
ZINC2013424	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@@H](O)[C@@H](O)[C@H](O)C(=O)O`
ZINC3581021	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@H](O)[C@@H](O)[C@@H](O)[C@@H](O)C(=O)O`
ZINC3860635	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@@H](O)[C@H](O)[C@H](O)C(=O)O`
ZINC5783661	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@@H](O)[C@H](O)[C@@H](O)C(=O)O`
ZINC6072527	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@@H](O)[C@@H](O)[C@@H](O)C(=O)O`
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`
ZINC3869233	0.630	266.0 Da LogP -1.34 TPSA 170.8	✓ Ro5	✓ Clean	`O=C(O)[C@H](COP(=O)(O)O)OP(=O)(O)O`
ZINC3869234	0.630	266.0 Da LogP -1.34 TPSA 170.8	✓ Ro5	✓ Clean	`O=C(O)[C@@H](COP(=O)(O)O)OP(=O)(O)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(=…`
ZINC1560405156	0.588	208.1 Da LogP -1.79 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)/C(O)=C(\O)[C@H](O)[C@H](O)C(=O)O`
ZINC1560405157	0.588	208.1 Da LogP -1.79 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)/C(O)=C(/O)[C@H](O)[C@H](O)C(=O)O`
ZINC13398039	0.577	234.2 Da LogP -0.38 TPSA 121.1	✓ Ro5	✓ Clean	`CC(C)OC(=O)C[C@](O)(CC(=O)O)C(=O)O`
ZINC2528012	0.577	234.2 Da LogP -0.38 TPSA 121.1	✓ Ro5	✓ Clean	`CC(C)OC(=O)C[C@@](O)(CC(=O)O)C(=O)O`
ZINC146315135	0.560	204.2 Da LogP 0.86 TPSA 94.8	✓ Ro5	✓ Clean	`CCCCC[C@@](O)(CC(=O)O)C(=O)O`
ZINC146315336	0.560	204.2 Da LogP 0.86 TPSA 94.8	✓ Ro5	✓ Clean	`CCCCC[C@](O)(CC(=O)O)C(=O)O`
ZINC1850353	0.556	206.1 Da LogP -0.86 TPSA 132.1	✓ Ro5	✓ Clean	`O=C(O)CC(O)(CC(=O)O)CC(=O)O`
ZINC13398014	0.522	220.2 Da LogP -1.07 TPSA 110.1	✓ Ro5	✓ Clean	`COC(=O)CC(O)(CC(=O)OC)C(=O)O`
ZINC3861629	0.522	206.1 Da LogP -1.16 TPSA 121.1	✓ Ro5	✓ Clean	`COC(=O)C(O)(CC(=O)O)CC(=O)O`
ZINC5575424	0.520	200.0 Da LogP -1.37 TPSA 141.4	✓ Ro5	✓ Clean	`O=C(O)C(OP(=O)(O)O)C(=O)O`
ZINC100969993	0.500	359.5 Da LogP 2.70 TPSA 123.9	✓ Ro5	✓ Clean	`CCCCCCCCCCCCNC(=O)C[C@](O)(CC(=O)O)C(=O)O`
ZINC100969996	0.500	359.5 Da LogP 2.70 TPSA 123.9	✓ Ro5	✓ Clean	`CCCCCCCCCCCCNC(=O)C[C@@](O)(CC(=O)O)C(=O)O`
ZINC1529331	0.500	206.1 Da LogP -2.21 TPSA 149.2	✓ Ro5	✓ Clean	`O=C(O)C(=O)[C@H](C(=O)O)[C@@H](O)C(=O)O`
ZINC1529332	0.500	206.1 Da LogP -2.21 TPSA 149.2	✓ Ro5	✓ Clean	`O=C(O)C(=O)[C@H](C(=O)O)[C@H](O)C(=O)O`
ZINC1529333	0.500	206.1 Da LogP -2.21 TPSA 149.2	✓ Ro5	✓ Clean	`O=C(O)C(=O)[C@@H](C(=O)O)[C@@H](O)C(=O)O`
ZINC1529334	0.500	206.1 Da LogP -2.21 TPSA 149.2	✓ Ro5	✓ Clean	`O=C(O)C(=O)[C@@H](C(=O)O)[C@H](O)C(=O)O`
ZINC1711854	0.500	248.2 Da LogP -0.13 TPSA 149.2	✓ Ro5	✓ Clean	`O=C(O)CC(CC(=O)O)(CC(=O)O)CC(=O)O`

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.