Protein profile

KP13_01692

UDP-N-acetyl-D-mannosamine dehydrogenase

Genome: KpKP13

Gene: AHE47001.1 wecC Structure source: AlphaFold + ColabFold UniProt A0A0H3GLK6

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Amino acids 420

Annotations 7

Features 34

PDB binders 4

Druggability 0.618

Overview

Basic information about this protein and its source genome.

Accession: KP13_01692
Assembly: Klebsiella pneumoniae subsp. pneumoniae Kp13, complete sequence
Gene: AHE47001.1 wecC
Status: annotated
Amino acids: 420
Structure source: AlphaFold + ColabFold

1.1.1.336

GO:0089714 Catalysis of the reaction: UDP-N-acetyl-alpha-D-mannosamine + 2 NAD+ + H2O = UDP-N-acetyl-alpha-D-mannosaminuronate + 2 NADH + 2 H+. GO:0016628 Catalysis of an oxidation-reduction (redox) reaction in which a CH-CH group acts as a hydrogen or electron donor and reduces NAD or NADP. 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:0000271 The chemical reactions and pathways resulting in the formation of a polysaccharide, a polymer of many (typically more than 10) monosaccharide residues linked glycosidically. GO:0009246 The chemical reactions and pathways resulting in the formation of the enterobacterial common antigen, an acidic polysaccharide containing N-acetyl-D-glucosamine, N-acetyl-D-mannosaminouronic acid, and 4-acetamido-4,6-dideoxy-D-galactose. A major component of the cell wall outer membrane of Gram-negative bacteria. GO:0051287 Binding to nicotinamide adenine dinucleotide, a coenzyme involved in many redox and biosynthetic reactions; binding may be to either the oxidized form, NAD+, or the reduced form, NADH.

Target profile

Computed evidence for target prioritization.

Human off-target: hit
Human identity (%): 31.818
Human E-value: 8.65e-06
Gut microbiome off-target: hit
Essential (DEG): N
DEG identity (%): 0.0
Localization: Cytoplasmic
ColabFold pLDDT: 96.32

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 0.618

Structure A0A0H3GLK6

Pocket Pocket 2

P2Rank 0.773

Structure A0A0H3GLK6

Pocket Pocket 1

ColabFold model

FPocket 0.701 · Pocket 16

P2Rank 0.788 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 225 / 4744 genomes with a hit

Normalized 0.047

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)

1.1.1.336

Gene Ontology (GO)

GO:0089714 Catalysis of the reaction: UDP-N-acetyl-alpha-D-mannosamine + 2 NAD+ + H2O = UDP-N-acetyl-alpha-D-mannosaminuronate + 2 NADH + 2 H+.
GO:0016628 Catalysis of an oxidation-reduction (redox) reaction in which a CH-CH group acts as a hydrogen or electron donor and reduces NAD or NADP.
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:0000271 The chemical reactions and pathways resulting in the formation of a polysaccharide, a polymer of many (typically more than 10) monosaccharide residues linked glycosidically.
GO:0009246 The chemical reactions and pathways resulting in the formation of the enterobacterial common antigen, an acidic polysaccharide containing N-acetyl-D-glucosamine, N-acetyl-D-mannosaminouronic acid, and 4-acetamido-4,6-dideoxy-D-galactose. A major component of the cell wall outer membrane of Gram-negative bacteria.
GO:0051287 Binding to nicotinamide adenine dinucleotide, a coenzyme involved in many redox and biosynthetic reactions; binding may be to either the oxidized form, NAD+, or the reduced form, NADH.

Sequence Features

Domain/signature hits from InterPro and related databases.

34 records

Show feature table

Start	End	DB	Term	Name
206	293	Pfam	PF00984	UDP-glucose/GDP-mannose dehydrogenase family, central domain
206	293	InterPro	IPR014026	UDP-glucose/GDP-mannose dehydrogenase, dimerisation
1	202	FunFam	G3DSA:3.40.50.720:FF:000139	UDP-N-acetyl-D-mannosamine dehydrogenase
311	419	SUPERFAMILY	SSF52413	UDP-glucose/GDP-mannose dehydrogenase C-terminal domain
311	419	InterPro	IPR036220	UDP-glucose/GDP-mannose dehydrogenase, C-terminal domain superfamily
5	16	Phobius	SIGNAL_PEPTIDE_H_REGION	Hydrophobic region of a signal peptide.
206	235	Gene3D	G3DSA:1.20.5.100	-
324	420	SMART	SM00984	UDPG_MGDP_dh_C_a_2_a
324	420	InterPro	IPR014027	UDP-glucose/GDP-mannose dehydrogenase, C-terminal
238	420	Gene3D	G3DSA:3.40.50.720	-
5	198	SUPERFAMILY	SSF51735	NAD(P)-binding Rossmann-fold domains
5	198	InterPro	IPR036291	NAD(P)-binding domain superfamily
2	202	Gene3D	G3DSA:3.40.50.720	-
1	420	Hamap	MF_02029	UDP-N-acetyl-D-mannosamine dehydrogenase [wecC].
1	420	InterPro	IPR032891	UDP-N-acetyl-D-mannosamine dehydrogenase WecC
24	420	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
206	299	SUPERFAMILY	SSF48179	6-phosphogluconate dehydrogenase C-terminal domain-like
206	299	InterPro	IPR008927	6-phosphogluconate dehydrogenase-like, C-terminal domain superfamily
3	419	PANTHER	PTHR43491	UDP-N-ACETYL-D-MANNOSAMINE DEHYDROGENASE
3	419	InterPro	IPR028359	UDP-N-acetyl-D-mannosamine/glucosamine dehydrogenase
5	416	NCBIfam	TIGR03026	nucleotide sugar dehydrogenase
5	416	InterPro	IPR017476	UDP-glucose/GDP-mannose dehydrogenase
238	420	FunFam	G3DSA:3.40.50.720:FF:000235	UDP-N-acetyl-D-mannosamine dehydrogenase
4	419	PIRSF	PIRSF000124	UDPglc_GDPman_dh
4	419	InterPro	IPR017476	UDP-glucose/GDP-mannose dehydrogenase
324	419	Pfam	PF03720	UDP-glucose/GDP-mannose dehydrogenase family, UDP binding domain
324	419	InterPro	IPR014027	UDP-glucose/GDP-mannose dehydrogenase, C-terminal
5	189	Pfam	PF03721	UDP-glucose/GDP-mannose dehydrogenase family, NAD binding domain
5	189	InterPro	IPR001732	UDP-glucose/GDP-mannose dehydrogenase, N-terminal
1	23	Phobius	SIGNAL_PEPTIDE	Signal peptide region
17	23	Phobius	SIGNAL_PEPTIDE_C_REGION	C-terminal region of a signal peptide.
1	4	Phobius	SIGNAL_PEPTIDE_N_REGION	N-terminal region of a signal peptide.
1	420	PIRSF	PIRSF500136	UDP_ManNAc_DH
1	420	InterPro	IPR028359	UDP-N-acetyl-D-mannosamine/glucosamine dehydrogenase

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_A0A0H3GLK6	AlphaFold	—	—	full sequence	—	Viewing
ColabFold KP13_01692	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
2				0.618
11				0.557
21				0.007
5				0.0

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	19.36	0.773
2	15.1	0.663
3	6.48	0.274
4	5.82	0.235
5	3.93	0.126

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
16				0.701
13				0.522

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	11.88	0.629
2	5.7	0.275
3	4.52	0.193
4	4.11	0.166
5	2.08	0.047

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.

54 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
PDC	3OJO	P95708	167.1 Da LogP 0.48 TPSA 87.5	✓ Ro5	✓ Clean	`c1cc(nc(c1)C(=O)O)C(=O)O`
SAJ	4R16	O59284	621.3 Da LogP -4.56 TPSA 322.9	3 viol.	✓ Clean	`CC(=O)N[C@H]1[C@H]([C@@H]([C@H](O[C@@H]1OP(=O)(…`
UGA	3GG2	Q7MVC7	580.3 Da LogP -4.70 TPSA 314.1	3 viol.	✓ Clean	`C1=CN(C(=O)NC1=O)[C@H]2[C@@H]([C@@H]([C@H](O2)C…`
UPG	3VTF	A1RUM9	566.3 Da LogP -4.79 TPSA 297.0	3 viol.	✓ Clean	`C1=CN(C(=O)NC1=O)[C@H]2[C@@H]([C@@H]([C@H](O2)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
ZINC34049460	0.762	244.2 Da LogP 1.54 TPSA 100.4	✓ Ro5	✓ Clean	`O=C(O)c1cccc(-c2cccc(C(=O)O)n2)n1`
ZINC13548378	0.729	484.1 Da LogP -2.50 TPSA 264.4	2 viol.	✓ Clean	`O=c1ccn([C@@H]2O[C@H](CO[P@@](=O)(O)O[P@@](=O)(…`
ZINC21990496	0.727	321.3 Da LogP 2.60 TPSA 113.3	✓ Ro5	✓ Clean	`O=C(O)c1cccc(-c2cccc(-c3cccc(C(=O)O)n3)n2)n1`
ZINC331827	0.696	202.0 Da LogP 1.54 TPSA 50.2	✓ Ro5	✓ Clean	`O=C(O)c1cccc(Br)n1`
ZINC4352696	0.696	249.0 Da LogP 1.38 TPSA 50.2	✓ Ro5	✓ Clean	`O=C(O)c1cccc(I)n1`
ZINC12959005	0.694	484.1 Da LogP -2.50 TPSA 264.4	2 viol.	✓ Clean	`O=c1ccn([C@@H]2O[C@H](CO[P@](=O)(O)O[P@](=O)(O)…`
ZINC12959016	0.694	484.1 Da LogP -2.50 TPSA 264.4	2 viol.	✓ Clean	`O=c1ccn([C@@H]2O[C@@H](CO[P@](=O)(O)O[P@](=O)(O…`
ZINC25726233	0.694	484.1 Da LogP -2.50 TPSA 264.4	2 viol.	✓ Clean	`O=c1ccn([C@H]2O[C@@H](CO[P@](=O)(O)O[P@](=O)(O)…`
ZINC3861755	0.694	484.1 Da LogP -2.50 TPSA 264.4	2 viol.	✓ Clean	`O=c1ccn([C@@H]2O[C@H](CO[P@@](=O)(O)O[P@@](=O)(…`
ZINC3875255	0.694	484.1 Da LogP -2.50 TPSA 264.4	2 viol.	✓ Clean	`O=c1ccn([C@H]2O[C@@H](CO[P@@](=O)(O)O[P@@](=O)(…`
ZINC3875256	0.694	484.1 Da LogP -2.50 TPSA 264.4	2 viol.	✓ Clean	`O=c1ccn([C@@H]2O[C@@H](CO[P@@](=O)(O)O[P@@](=O)…`
ZINC3875257	0.694	484.1 Da LogP -2.50 TPSA 264.4	2 viol.	✓ Clean	`O=c1ccn([C@H]2O[C@@H](CO[P@@](=O)(O)O[P@@](=O)(…`
ZINC3875258	0.694	484.1 Da LogP -2.50 TPSA 264.4	2 viol.	✓ Clean	`O=c1ccn([C@@H]2O[C@@H](CO[P@@](=O)(O)O[P@@](=O)…`
ZINC88466482	0.694	484.1 Da LogP -2.50 TPSA 264.4	2 viol.	✓ Clean	`O=c1ccn([C@@H]2O[C@H](CO[P@@](=O)(O)O[P@@](=O)(…`
ZINC35636069	0.689	404.2 Da LogP -2.62 TPSA 217.8	1 viol.	✓ Clean	`O=c1ccn([C@@H]2O[C@H](CO[P@](=O)(O)OP(=O)(O)O)[…`
ZINC40655887	0.689	404.2 Da LogP -2.62 TPSA 217.8	1 viol.	✓ Clean	`O=c1ccn([C@@H]2O[C@H](CO[P@](=O)(O)OP(=O)(O)O)[…`
ZINC40655889	0.689	404.2 Da LogP -2.62 TPSA 217.8	1 viol.	✓ Clean	`O=c1ccn([C@@H]2O[C@H](CO[P@@](=O)(O)OP(=O)(O)O)…`
ZINC44460318	0.689	404.2 Da LogP -2.62 TPSA 217.8	1 viol.	✓ Clean	`O=c1ccn([C@H]2O[C@@H](CO[P@@](=O)(O)OP(=O)(O)O)…`
ZINC4490939	0.689	404.2 Da LogP -2.62 TPSA 217.8	1 viol.	✓ Clean	`O=c1ccn([C@@H]2O[C@H](CO[P@@](=O)(O)OP(=O)(O)O)…`
ZINC8585026	0.689	404.2 Da LogP -2.62 TPSA 217.8	1 viol.	✓ Clean	`O=c1ccn([C@H]2O[C@@H](CO[P@@](=O)(O)OP(=O)(O)O)…`
ZINC8585028	0.689	404.2 Da LogP -2.62 TPSA 217.8	1 viol.	✓ Clean	`O=c1ccn([C@@H]2O[C@@H](CO[P@@](=O)(O)OP(=O)(O)O…`
ZINC8585030	0.689	404.2 Da LogP -2.62 TPSA 217.8	1 viol.	✓ Clean	`O=c1ccn([C@H]2O[C@@H](CO[P@@](=O)(O)OP(=O)(O)O)…`
ZINC8585032	0.689	404.2 Da LogP -2.62 TPSA 217.8	1 viol.	✓ Clean	`O=c1ccn([C@@H]2O[C@@H](CO[P@@](=O)(O)OP(=O)(O)O…`
ZINC308666757	0.680	219.1 Da LogP 1.52 TPSA 67.3	✓ Ro5	✓ Clean	`O=C(O)c1cccc(C(=O)C(F)(F)F)n1`
ZINC102211562	0.667	490.3 Da LogP -1.89 TPSA 206.8	1 viol.	✓ Clean	`C[N+](C)(C)CCO[P@@](=O)(O)O[P@@](=O)(O)OC[C@H]1…`
ZINC110347779	0.667	490.3 Da LogP -1.89 TPSA 206.8	1 viol.	✓ Clean	`C[N+](C)(C)CCO[P@@](=O)(O)O[P@@](=O)(O)OC[C@@H]…`
ZINC110347782	0.667	490.3 Da LogP -1.89 TPSA 206.8	1 viol.	✓ Clean	`C[N+](C)(C)CCO[P@@](=O)(O)O[P@@](=O)(O)OC[C@@H]…`
ZINC97976147	0.667	490.3 Da LogP -1.89 TPSA 206.8	1 viol.	✓ Clean	`C[N+](C)(C)CCO[P@@](=O)(O)O[P@@](=O)(O)OC[C@@H]…`
ZINC98175528	0.640	240.5 Da LogP 2.61 TPSA 50.2	✓ Ro5	✓ Clean	`O=C(O)c1cccc(C(Cl)(Cl)Cl)n1`
ZINC34563915	0.630	222.2 Da LogP 1.26 TPSA 70.5	✓ Ro5	✓ Clean	`CCN(CC)C(=O)c1cccc(C(=O)O)n1`
ZINC36756657	0.630	220.2 Da LogP 1.02 TPSA 70.5	✓ Ro5	✓ Clean	`O=C(O)c1cccc(C(=O)N2CCCC2)n1`
ZINC12503831	0.623	324.2 Da LogP -2.73 TPSA 171.3	✓ Ro5	✓ Clean	`O=c1ccn([C@H]2O[C@H](COP(=O)(O)O)[C@H](O)[C@H]2…`
ZINC12503833	0.623	324.2 Da LogP -2.73 TPSA 171.3	✓ Ro5	✓ Clean	`O=c1ccn([C@H]2O[C@H](COP(=O)(O)O)[C@H](O)[C@@H]…`
ZINC13512000	0.623	324.2 Da LogP -2.73 TPSA 171.3	✓ Ro5	✓ Clean	`O=c1ccn([C@@H]2O[C@H](COP(=O)(O)O)[C@H](O)[C@H]…`
ZINC1532538	0.623	324.2 Da LogP -2.73 TPSA 171.3	✓ Ro5	✓ Clean	`O=c1ccn([C@H]2O[C@@H](COP(=O)(O)O)[C@H](O)[C@@H…`
ZINC2026984	0.623	324.2 Da LogP -2.73 TPSA 171.3	✓ Ro5	✓ Clean	`O=c1ccn([C@H]2O[C@@H](COP(=O)(O)O)[C@H](O)[C@H]…`
ZINC2123545	0.623	324.2 Da LogP -2.73 TPSA 171.3	✓ Ro5	✓ Clean	`O=c1ccn([C@@H]2O[C@H](COP(=O)(O)O)[C@@H](O)[C@H…`
ZINC2606131	0.623	324.2 Da LogP -2.73 TPSA 171.3	✓ Ro5	✓ Clean	`O=c1ccn([C@@H]2O[C@H](COP(=O)(O)O)[C@@H](O)[C@@…`
ZINC36377965	0.623	324.2 Da LogP -2.73 TPSA 171.3	✓ Ro5	✓ Clean	`O=c1ccn([C@@H]2O[C@H](COP(=O)(O)O)[C@H](O)[C@@H…`
ZINC3870257	0.623	324.2 Da LogP -2.73 TPSA 171.3	✓ Ro5	✓ Clean	`O=c1ccn([C@H]2O[C@@H](COP(=O)(O)O)[C@@H](O)[C@H…`
ZINC3870258	0.623	324.2 Da LogP -2.73 TPSA 171.3	✓ Ro5	✓ Clean	`O=c1ccn([C@@H]2O[C@@H](COP(=O)(O)O)[C@@H](O)[C@…`
ZINC3870259	0.623	324.2 Da LogP -2.73 TPSA 171.3	✓ Ro5	✓ Clean	`O=c1ccn([C@H]2O[C@@H](COP(=O)(O)O)[C@@H](O)[C@@…`
ZINC3870260	0.623	324.2 Da LogP -2.73 TPSA 171.3	✓ Ro5	✓ Clean	`O=c1ccn([C@@H]2O[C@@H](COP(=O)(O)O)[C@@H](O)[C@…`
ZINC9235501	0.623	324.2 Da LogP -2.73 TPSA 171.3	✓ Ro5	✓ Clean	`O=c1ccn([C@@H]2O[C@@H](COP(=O)(O)O)[C@H](O)[C@H…`
ZINC2566954	0.615	203.2 Da LogP 0.03 TPSA 104.6	✓ Ro5	✓ Clean	`O=C(O)c1cccc(S(=O)(=O)O)n1`
ZINC174780	0.607	209.2 Da LogP 1.34 TPSA 76.5	✓ Ro5	✓ Clean	`CC(C)OC(=O)c1cccc(C(=O)O)n1`
ZINC21161893	0.607	223.2 Da LogP 1.74 TPSA 76.5	✓ Ro5	✓ Clean	`CC(C)(C)OC(=O)c1cccc(C(=O)O)n1`
ZINC218535275	0.607	224.2 Da LogP -0.41 TPSA 116.6	✓ Ro5	✓ Clean	`O=C(O)CNC(=O)c1cccc(C(=O)O)n1`
ZINC36756666	0.607	208.2 Da LogP 0.92 TPSA 79.3	✓ Ro5	✓ Clean	`CC(C)NC(=O)c1cccc(C(=O)O)n1`
ZINC220143873	0.603	486.1 Da LogP -1.52 TPSA 244.1	2 viol.	✓ Clean	`O=c1ccn([C@@H]2O[C@H](CO[P@@](=O)(O)O[P@@](=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.