Protein profile

KP13_02354

L-fucose isomerase

Genome: KpKP13

Gene: fucI AHE42924.1 Structure source: AlphaFold + ColabFold UniProt A0A0H3GWX4

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Amino acids 591

Annotations 11

Features 24

PDB binders 1

Druggability 0.48

Overview

Basic information about this protein and its source genome.

Accession: KP13_02354
Assembly: Klebsiella pneumoniae subsp. pneumoniae Kp13, complete sequence
Gene: fucI AHE42924.1
Status: annotated
Amino acids: 591
Structure source: AlphaFold + ColabFold

5.3.1.25

GO:0030145 Binding to a manganese ion (Mn). GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. GO:0008736 Catalysis of the reaction: L-fucose = L-fuculose. GO:0019317 OBSOLETE. The chemical reactions and pathways resulting in the breakdown of fucose (6-deoxygalactose). GO:0016861 Catalysis of an oxidation-reduction (redox) reaction in which the hydrogen donor and acceptor, which is an aldose or a ketose, are the same molecule, and no oxidized product appears. GO:0005996 The chemical reactions and pathways involving monosaccharides, the simplest carbohydrates. They are polyhydric alcohols containing either an aldehyde or a keto group and between three to ten or more carbon atoms. They form the constitutional repeating units of oligo- and polysaccharides.

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 (%): 68.664
DEG E-value: 0.0
Localization: Cytoplasmic
ColabFold pLDDT: 98.11

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 0.48

Structure A0A0H3GWX4

Pocket Pocket 33

P2Rank 0.511

Structure A0A0H3GWX4

Pocket Pocket 1

ColabFold model

FPocket 0.675 · Pocket 2

P2Rank 0.465 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 778 / 4744 genomes with a hit

Normalized 0.164

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 10 GO

Enzyme Commission (EC)

5.3.1.25

Gene Ontology (GO)

GO:0030145 Binding to a manganese ion (Mn).
GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
GO:0008736 Catalysis of the reaction: L-fucose = L-fuculose.
GO:0019317 OBSOLETE. The chemical reactions and pathways resulting in the breakdown of fucose (6-deoxygalactose).
GO:0016861 Catalysis of an oxidation-reduction (redox) reaction in which the hydrogen donor and acceptor, which is an aldose or a ketose, are the same molecule, and no oxidized product appears.
GO:0005996 The chemical reactions and pathways involving monosaccharides, the simplest carbohydrates. They are polyhydric alcohols containing either an aldehyde or a keto group and between three to ten or more carbon atoms. They form the constitutional repeating units of oligo- and polysaccharides.
GO:0006004 The chemical reactions and pathways involving fucose, or 6-deoxygalactose, which has two enantiomers, D-fucose and L-fucose.
GO:0008790 Catalysis of the reaction: D-arabinose = D-ribulose.
GO:0019571 The chemical reactions and pathways resulting in the breakdown of D-arabinose, the D-enantiomer of arabino-pentose.
GO:0042355 The chemical reactions and pathways resulting in the breakdown of L-fucose (6-deoxy-Lgalactose).

Sequence Features

Domain/signature hits from InterPro and related databases.

24 records

Show feature table

Start	End	DB	Term	Name
3	591	Hamap	MF_01254	L-fucose isomerase [fucI].
3	591	InterPro	IPR005763	L-fucose isomerase
1	175	Gene3D	G3DSA:3.40.50.1070	-
1	175	InterPro	IPR038391	L-fucose isomerase, domain 1 superfamily
175	354	Pfam	PF07882	L-fucose isomerase, second N-terminal domain
175	354	InterPro	IPR012889	L-fucose isomerase, N-terminal-2
341	591	FunFam	G3DSA:3.20.14.10:FF:000001	L-fucose isomerase
7	174	Pfam	PF07881	L-fucose isomerase, first N-terminal domain
7	174	InterPro	IPR012888	L-fucose isomerase, N-terminal-1
176	340	Gene3D	G3DSA:3.40.275.10	-
176	340	InterPro	IPR038392	L-fucose isomerase, domain 2 superfamily
356	590	SUPERFAMILY	SSF50443	FucI/AraA C-terminal domain-like
356	590	InterPro	IPR004216	L-fucose/L-arabinose isomerase, C-terminal
176	340	FunFam	G3DSA:3.40.275.10:FF:000001	L-fucose isomerase
5	590	NCBIfam	TIGR01089	L-fucose isomerase
5	590	InterPro	IPR005763	L-fucose isomerase
341	591	Gene3D	G3DSA:3.20.14.10	-
341	591	InterPro	IPR038393	L-fucose isomerase, domain 3 superfamily
2	355	SUPERFAMILY	SSF53743	FucI/AraA N-terminal and middle domains
2	355	InterPro	IPR009015	L-fucose isomerase, N-terminal/central domain superfamily
5	590	PANTHER	PTHR37840	L-FUCOSE ISOMERASE
1	175	FunFam	G3DSA:3.40.50.1070:FF:000001	L-fucose isomerase
390	554	Pfam	PF02952	L-fucose isomerase, C-terminal domain
390	554	InterPro	IPR015888	L-fucose isomerase, C-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_A0A0H3GWX4	AlphaFold	—	—	full sequence	—	Viewing
ColabFold KP13_02354	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
33				0.48
3				0.024
29				0.024
2				0.001

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	11.07	0.511
2	3.53	0.104
3	3.06	0.081
4	2.46	0.055
5	1.98	0.035

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
2				0.675

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	6.16	0.307
2	1.69	0.029
3	1.63	0.027
4	1.62	0.026
5	1.32	0.014

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.

38 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
FOC	1FUI	P69922	166.2 Da LogP -2.56 TPSA 101.2	✓ Ro5	✓ Clean	`C[C@@H]([C@H]([C@H]([C@@H](CO)O)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
ZINC100055463	0.647	212.2 Da LogP -4.22 TPSA 141.6	1 viol.	✓ Clean	`OC[C@H](O)[C@@H](O)[C@H](O)[C@H](O)[C@H](O)CO`
ZINC100064885	0.647	212.2 Da LogP -4.22 TPSA 141.6	1 viol.	✓ Clean	`OC[C@H](O)[C@@H](O)[C@@H](O)[C@H](O)[C@H](O)CO`
ZINC17780060	0.647	212.2 Da LogP -4.22 TPSA 141.6	1 viol.	✓ Clean	`OC[C@@H](O)[C@H](O)C(O)[C@H](O)[C@H](O)CO`
ZINC17952732	0.647	212.2 Da LogP -4.22 TPSA 141.6	1 viol.	✓ Clean	`OC[C@H](O)[C@@H](O)C(O)[C@H](O)[C@H](O)CO`
ZINC18042331	0.647	242.2 Da LogP -4.86 TPSA 161.8	1 viol.	✓ Clean	`OC[C@H](O)[C@H](O)[C@H](O)[C@H](O)[C@H](O)[C@H]…`
ZINC18120313	0.647	212.2 Da LogP -4.22 TPSA 141.6	1 viol.	✓ Clean	`OC[C@H](O)[C@H](O)C(O)[C@H](O)[C@H](O)CO`
ZINC3979006	0.647	212.2 Da LogP -4.22 TPSA 141.6	1 viol.	✓ Clean	`OC[C@@H](O)[C@@H](O)C(O)[C@H](O)[C@H](O)CO`
ZINC4403103	0.647	242.2 Da LogP -4.86 TPSA 161.8	1 viol.	✓ Clean	`OC[C@@H](O)[C@H](O)[C@H](O)[C@H](O)[C@H](O)[C@H…`
ZINC4403105	0.647	242.2 Da LogP -4.86 TPSA 161.8	1 viol.	✓ Clean	`OC[C@H](O)[C@@H](O)[C@H](O)[C@H](O)[C@H](O)[C@H…`
ZINC4403107	0.647	242.2 Da LogP -4.86 TPSA 161.8	1 viol.	✓ Clean	`OC[C@@H](O)[C@@H](O)[C@H](O)[C@H](O)[C@H](O)[C@…`
ZINC9212412	0.647	212.2 Da LogP -4.22 TPSA 141.6	1 viol.	✓ Clean	`OC[C@H](O)[C@@H](O)C(O)[C@H](O)[C@@H](O)CO`
ZINC216185927	0.522	209.2 Da LogP -3.02 TPSA 104.4	✓ Ro5	✓ Clean	`CN(C)C[C@H](O)[C@H](O)[C@H](O)[C@@H](O)CO`
ZINC216185976	0.522	209.2 Da LogP -3.02 TPSA 104.4	✓ Ro5	✓ Clean	`CN(C)C[C@H](O)[C@H](O)[C@@H](O)[C@H](O)CO`
ZINC216186168	0.522	224.3 Da LogP -2.87 TPSA 101.2	✓ Ro5	✓ Clean	`C[N+](C)(C)C[C@H](O)[C@H](O)[C@H](O)[C@@H](O)CO`
ZINC216186206	0.522	224.3 Da LogP -2.87 TPSA 101.2	✓ Ro5	✓ Clean	`C[N+](C)(C)C[C@H](O)[C@H](O)[C@@H](O)[C@H](O)CO`
ZINC25624721	0.522	209.2 Da LogP -3.02 TPSA 104.4	✓ Ro5	✓ Clean	`CN(C)C[C@H](O)[C@H](O)[C@@H](O)[C@@H](O)CO`
ZINC25624980	0.522	224.3 Da LogP -2.87 TPSA 101.2	✓ Ro5	✓ Clean	`C[N+](C)(C)C[C@H](O)[C@H](O)[C@@H](O)[C@@H](O)CO`
ZINC4566610	0.522	209.2 Da LogP -3.02 TPSA 104.4	✓ Ro5	✓ Clean	`CN(C)C[C@H](O)[C@H](O)[C@H](O)[C@H](O)CO`
ZINC4566614	0.522	224.3 Da LogP -2.87 TPSA 101.2	✓ Ro5	✓ Clean	`C[N+](C)(C)C[C@H](O)[C@H](O)[C@H](O)[C@H](O)CO`
ZINC5066653	0.520	312.5 Da LogP 1.17 TPSA 80.9	✓ Ro5	✓ Clean	`CC(C)CSC(SCC(C)C)[C@H](O)[C@H](O)[C@H](O)CO`
ZINC5066655	0.520	312.5 Da LogP 1.17 TPSA 80.9	✓ Ro5	✓ Clean	`CC(C)CSC(SCC(C)C)[C@@H](O)[C@H](O)[C@H](O)CO`
ZINC5066658	0.520	312.5 Da LogP 1.17 TPSA 80.9	✓ Ro5	✓ Clean	`CC(C)CSC(SCC(C)C)[C@H](O)[C@@H](O)[C@H](O)CO`
ZINC5066661	0.520	312.5 Da LogP 1.17 TPSA 80.9	✓ Ro5	✓ Clean	`CC(C)CSC(SCC(C)C)[C@@H](O)[C@@H](O)[C@H](O)CO`
ZINC14944599	0.500	256.4 Da LogP -0.11 TPSA 80.9	✓ Ro5	✓ Clean	`CCSC(SCC)[C@H](O)[C@H](O)[C@@H](O)CO`
ZINC1868590	0.500	256.4 Da LogP -0.11 TPSA 80.9	✓ Ro5	✓ Clean	`CCSC(SCC)[C@H](O)[C@@H](O)[C@H](O)CO`
ZINC3137815	0.500	256.4 Da LogP -0.11 TPSA 80.9	✓ Ro5	✓ Clean	`CCSC(SCC)[C@H](O)[C@@H](O)[C@@H](O)CO`
ZINC3843093	0.500	256.4 Da LogP -0.11 TPSA 80.9	✓ Ro5	✓ Clean	`CCSC(SCC)[C@@H](O)[C@H](O)[C@H](O)CO`
ZINC4691943	0.500	256.4 Da LogP -0.11 TPSA 80.9	✓ Ro5	✓ Clean	`CCSC(SCC)[C@H](O)[C@H](O)[C@H](O)CO`
ZINC4691944	0.500	256.4 Da LogP -0.11 TPSA 80.9	✓ Ro5	✓ Clean	`CCSC(SCC)[C@@H](O)[C@@H](O)[C@H](O)CO`
ZINC5201837	0.500	345.3 Da LogP -6.55 TPSA 214.3	2 viol.	✓ Clean	`OC[C@@H](O)[C@@H](O)[C@@H](O)[C@@H](O)CNC[C@H](…`
ZINC5201838	0.500	345.3 Da LogP -6.55 TPSA 214.3	2 viol.	✓ Clean	`OC[C@@H](O)[C@@H](O)[C@@H](O)[C@@H](O)CNC[C@@H]…`
ZINC5201839	0.500	345.3 Da LogP -6.55 TPSA 214.3	2 viol.	✓ Clean	`OC[C@@H](O)[C@@H](O)[C@@H](O)[C@@H](O)CNC[C@H](…`
ZINC5201841	0.500	345.3 Da LogP -6.55 TPSA 214.3	2 viol.	✓ Clean	`OC[C@@H](O)[C@@H](O)[C@@H](O)[C@@H](O)CNC[C@@H]…`
ZINC5732420	0.500	212.2 Da LogP -3.61 TPSA 130.6	1 viol.	✓ Clean	`CO[C@H](O)[C@H](O)[C@H](O)[C@H](O)[C@H](O)CO`
ZINC5732422	0.500	212.2 Da LogP -3.61 TPSA 130.6	1 viol.	✓ Clean	`CO[C@@H](O)[C@H](O)[C@H](O)[C@H](O)[C@H](O)CO`
ZINC5732426	0.500	212.2 Da LogP -3.61 TPSA 130.6	1 viol.	✓ Clean	`CO[C@H](O)[C@@H](O)[C@H](O)[C@H](O)[C@H](O)CO`
ZINC5732428	0.500	212.2 Da LogP -3.61 TPSA 130.6	1 viol.	✓ Clean	`CO[C@@H](O)[C@@H](O)[C@H](O)[C@H](O)[C@H](O)CO`

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.