Protein profile

KP13_31518

3-dehydroquinate dehydratase

Genome: KpKP13

Gene: AHE42417.1 aroQ Structure source: AlphaFold + ColabFold UniProt A0A0H3GWB7

Export view

Amino acids 150

Annotations 6

Features 18

PDB binders 8

Druggability 0.649

Overview

Basic information about this protein and its source genome.

Accession: KP13_31518
Assembly: Klebsiella pneumoniae subsp. pneumoniae Kp13, complete sequence
Gene: AHE42417.1 aroQ
Status: annotated
Amino acids: 150
Structure source: AlphaFold + ColabFold

4.2.1.10

GO:0003855 Catalysis of the reaction: 3-dehydroquinate = 3-dehydroshikimate + H2O. GO:0008652 The chemical reactions and pathways resulting in the formation of amino acids, organic acids containing one or more amino substituents. GO:0009073 The chemical reactions and pathways resulting in the formation of aromatic amino acid family, amino acids with aromatic ring (phenylalanine, tyrosine, tryptophan). GO:0009423 The chemical reactions and pathways resulting in the formation of the unsymmetrical ether derived from phosphoenolpyruvate and 5-phosphoshikimic acid formed as an intermediate in the biosynthesis of aromatic amino acids and many other compounds. GO:0019631 The chemical reactions and pathways resulting in the breakdown of quinate, the anion of quinic acid.

Target profile

Computed evidence for target prioritization.

Human off-target: No hit
Human identity (%): 0.0
Gut microbiome off-target: hit
Essential (DEG): Y
DEG identity (%): 77.551
DEG E-value: 2.37e-71
Localization: Cytoplasmic
ColabFold pLDDT: 95.35

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 0.649

Structure A0A0H3GWB7

Pocket Pocket 1

P2Rank 0.649

Structure A0A0H3GWB7

Pocket Pocket 1

ColabFold model

FPocket 0.544 · Pocket 1

P2Rank 0.622 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 405 / 4744 genomes with a hit

Normalized 0.085

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 5 GO

Enzyme Commission (EC)

4.2.1.10

Gene Ontology (GO)

GO:0003855 Catalysis of the reaction: 3-dehydroquinate = 3-dehydroshikimate + H2O.
GO:0008652 The chemical reactions and pathways resulting in the formation of amino acids, organic acids containing one or more amino substituents.
GO:0009073 The chemical reactions and pathways resulting in the formation of aromatic amino acid family, amino acids with aromatic ring (phenylalanine, tyrosine, tryptophan).
GO:0009423 The chemical reactions and pathways resulting in the formation of the unsymmetrical ether derived from phosphoenolpyruvate and 5-phosphoshikimic acid formed as an intermediate in the biosynthesis of aromatic amino acids and many other compounds.
GO:0019631 The chemical reactions and pathways resulting in the breakdown of quinate, the anion of quinic acid.

Sequence Features

Domain/signature hits from InterPro and related databases.

18 records

Show feature table

Start	End	DB	Term	Name
3	149	PIRSF	PIRSF001399	DHQase_2
3	149	InterPro	IPR001874	Dehydroquinase, class II
6	145	CDD	cd00466	DHQase_II
6	145	InterPro	IPR001874	Dehydroquinase, class II
5	148	PANTHER	PTHR21272	CATABOLIC 3-DEHYDROQUINASE
5	148	InterPro	IPR001874	Dehydroquinase, class II
1	150	Hamap	MF_00169	3-dehydroquinate dehydratase [aroQ].
1	150	InterPro	IPR001874	Dehydroquinase, class II
10	27	ProSitePatterns	PS01029	Dehydroquinase class II signature.
10	27	InterPro	IPR018509	Dehydroquinase, class II, conserved site
7	142	Pfam	PF01220	Dehydroquinase class II
7	142	InterPro	IPR001874	Dehydroquinase, class II
6	145	NCBIfam	TIGR01088	3-dehydroquinate dehydratase, type II
1	150	Gene3D	G3DSA:3.40.50.9100	Dehydroquinase, class II
1	150	InterPro	IPR036441	Dehydroquinase, class II superfamily
35	55	Coils	Coil	Coil
6	148	SUPERFAMILY	SSF52304	Type II 3-dehydroquinate dehydratase
6	148	InterPro	IPR036441	Dehydroquinase, class II superfamily

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...

Legend High Medium Low

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_A0A0H3GWB7	AlphaFold	—	—	full sequence	—	Viewing
ColabFold KP13_31518	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				0.649

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				8.45	0.451
2				0.99	0.005

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				0.544

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				7.37	0.386
2				2.16	0.051

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.

42 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
CA2	2BT4	P15474	310.3 Da LogP 0.79 TPSA 107.2	✓ Ro5	✓ Clean	`c1ccc(cc1)OCCC[C@H]2C[C@](C[C@H]([C@@H]2O)O)(C(…`
DQA	5YDB	A3M692	190.2 Da LogP -2.11 TPSA 115.1	✓ Ro5	✓ Clean	`C1[C@H]([C@@H](C(=O)C[C@]1(C(=O)O)O)O)O`
FA1	1GU1	P15474	174.2 Da LogP -1.52 TPSA 98.0	✓ Ro5	✓ Clean	`C1[C@H]([C@@H](C=C[C@]1(C(=O)O)O)O)O`
FA3	1V1J	P15474	192.1 Da LogP -1.22 TPSA 98.0	✓ Ro5	✓ Clean	`C1[C@H]([C@@H](C(=C[C@]1(C(=O)O)O)F)O)O`
FLC	6SMF	Q5NPJ9	189.1 Da LogP -5.25 TPSA 140.6	✓ Ro5	✓ Clean	`C(C(=O)[O-])C(CC(=O)[O-])(C(=O)[O-])O`
RP4	2CJF	P15474	358.4 Da LogP 2.16 TPSA 98.0	✓ Ro5	✓ Clean	`c1ccc(cc1)Sc2cccc(c2)C3=C[C@](C[C@H]([C@@H]3O)O…`
TAR	6CV6	B2JVW0	150.1 Da LogP -2.12 TPSA 115.1	✓ Ro5	✓ Clean	`[C@H]([C@@H](C(=O)O)O)(C(=O)O)O`
TLA	6HSU	A1SZA3	150.1 Da LogP -2.12 TPSA 115.1	✓ Ro5	✓ Clean	`[C@@H]([C@H](C(=O)O)O)(C(=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).

Ligand	UniProt (homolog)	pchembl	MW · LogP · TPSA	Lipinski	PAINS	SMILES
CHEMBL1823559	P15474	8.24	317.3 Da LogP -0.41 TPSA 128.7	✓ Ro5	✓ Clean	`O=C(O)[C@]1(O)C=C(c2cn(-c3ccccc3)nn2)[C@@H](O)[…`
CHEMBL3221803	P15474	8.24	318.3 Da LogP -1.01 TPSA 141.6	✓ Ro5	✓ Clean	`O=C(O)[C@]1(O)C=C(c2cn(-c3cccnc3)nn2)[C@@H](O)[…`
CHEMBL3221799	P15474	7.54	335.3 Da LogP -0.27 TPSA 128.7	✓ Ro5	✓ Clean	`O=C(O)[C@]1(O)C=C(c2cn(-c3ccc(F)cc3)nn2)[C@@H](…`
CHEMBL3221802	P15474	7.32	333.3 Da LogP -0.70 TPSA 148.9	✓ Ro5	✓ Clean	`O=C(O)[C@]1(O)C=C(c2cn(-c3ccccc3O)nn2)[C@@H](O)…`
CHEMBL3221805	P15474	7.14	337.4 Da LogP -0.29 TPSA 128.7	✓ Ro5	✓ Clean	`O=C(O)[C@]1(O)C=C(c2cn(Cc3cccs3)nn2)[C@@H](O)[C…`
CHEMBL3221800	P15474	7.11	362.3 Da LogP -0.50 TPSA 171.8	✓ Ro5	✓ Clean	`O=C(O)[C@]1(O)C=C(c2cn(-c3cccc([N+](=O)[O-])c3)…`
CHEMBL3221804	P15474	6.66	321.3 Da LogP -0.76 TPSA 141.8	✓ Ro5	✓ Clean	`O=C(O)[C@]1(O)C=C(c2cn(Cc3ccco3)nn2)[C@@H](O)[C…`

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
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`
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`
ZINC473082484	0.548	310.3 Da LogP 2.54 TPSA 111.1	✓ Ro5	✓ Clean	`O=C(O)c1ccc(-c2cn(-c3cccc([N+](=O)[O-])c3)nn2)c…`
ZINC473083162	0.534	311.3 Da LogP 2.75 TPSA 117.0	✓ Ro5	✓ Clean	`O=[N+]([O-])c1cccc(-c2cn(-c3cccc([N+](=O)[O-])c…`
ZINC50213576	0.527	209.2 Da LogP 1.09 TPSA 68.0	✓ Ro5	✓ Clean	`O=C(O)c1cn(Cc2cccs2)nn1`
ZINC37291072	0.525	234.2 Da LogP 0.87 TPSA 111.1	✓ Ro5	✓ Clean	`O=C(O)c1cn(-c2cccc([N+](=O)[O-])c2)nn1`
ZINC473085275	0.525	311.3 Da LogP 2.75 TPSA 117.0	✓ Ro5	✓ Clean	`O=[N+]([O-])c1ccc(-c2cn(-c3cccc([N+](=O)[O-])c3…`
ZINC473081320	0.524	309.3 Da LogP 1.94 TPSA 116.9	✓ Ro5	✓ Clean	`NC(=O)c1cccc(-c2cn(-c3cccc([N+](=O)[O-])c3)nn2)…`
ZINC473081782	0.524	309.3 Da LogP 1.94 TPSA 116.9	✓ Ro5	✓ Clean	`NC(=O)c1ccc(-c2cn(-c3cccc([N+](=O)[O-])c3)nn2)c…`
ZINC408525852	0.509	241.3 Da LogP 3.05 TPSA 30.7	✓ Ro5	✓ Clean	`c1ccc(-c2cn(Cc3cccs3)nn2)cc1`
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`
ZINC473081680	0.500	266.3 Da LogP 2.84 TPSA 73.8	✓ Ro5	✓ Clean	`O=[N+]([O-])c1cccc(-c2cn(-c3ccccc3)nn2)c1`
ZINC473083741	0.500	309.3 Da LogP 1.94 TPSA 116.9	✓ Ro5	✓ Clean	`NC(=O)c1cccc(-n2cc(-c3cccc([N+](=O)[O-])c3)nn2)…`
ZINC52221032	0.500	220.2 Da LogP 0.67 TPSA 94.1	✓ Ro5	✓ Clean	`O=[N+]([O-])c1cccc(-n2cc(CO)nn2)c1`
ZINC75495318	0.500	310.3 Da LogP 2.54 TPSA 111.1	✓ Ro5	✓ Clean	`O=C(O)c1ccc(-n2cc(-c3cccc([N+](=O)[O-])c3)nn2)c…`

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.