Protein profile

PA3159

UDP-N-acetyl-d-glucosamine 6-dehydrogenase

Genome: NC_002516.2

Gene: wbpA PA3159 Structure source: AlphaFold UniProt G3XD94
Amino acids 436
Annotations 11
Features 26
PDB binders 4
Druggability 0.275

Overview

Basic information about this protein and its source genome.

Accession
PA3159
Gene
wbpA PA3159
Status
annotated
Amino acids
436
Structure source
AlphaFold

Target profile

Computed evidence for target prioritization.

Human off-target
hit
Human identity (%)
22.791
Human E-value
3.17e-13
Gut microbiome off-target
hit
Essential (DEG)
Y
Localization
Cytoplasmic

Selected Druggability evidence

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 0.275
Structure
Pocket

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)

1

Gene Ontology (GO)

10
  • GO:0016020 A lipid bilayer along with all the proteins and protein complexes embedded in it and attached to it.
  • 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.
  • GO:0003954 Catalysis of the reaction: NADH + H+ + acceptor = NAD+ + reduced acceptor.
  • GO:0016491 Catalysis of an oxidation-reduction (redox) reaction, a reversible chemical reaction in which the oxidation state of an atom or atoms within a molecule is altered. One substrate acts as a hydrogen or electron donor and becomes oxidized, while the other acts as hydrogen or electron acceptor and becomes reduced.
  • 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:0047004 Catalysis of the reaction: H2O + 2 NAD+ + UDP-N-acetyl-alpha-D-glucosamine = 3 H+ + 2 NADH + UDP-N-acetyl-2-amino-2-deoxy-D-glucuronate.
  • GO:0071555 A process that results in the assembly, arrangement of constituent parts, or disassembly of the cell wall, the rigid or semi-rigid envelope lying outside the cell membrane of plant, fungal and most prokaryotic cells, maintaining their shape and protecting them from osmotic lysis.
  • GO:0009243 The chemical reactions and pathways resulting in the formation of the O side chain of a lipopolysaccharide, which determines the antigenic specificity of the organism. It is made up of about 50 repeating units of a branched tetrasaccharide.
  • 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: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.

Sequence Features

Domain/signature hits from InterPro and related databases.

26 records
Show feature table
Start End DB Term Name
18 192 Pfam PF03721 UDP-glucose/GDP-mannose dehydrogenase family, NAD binding domain
18 192 InterPro IPR001732 UDP-glucose/GDP-mannose dehydrogenase, N-terminal
9 432 PANTHER PTHR43491 UDP-N-ACETYL-D-MANNOSAMINE DEHYDROGENASE
9 432 InterPro IPR028359 UDP-N-acetyl-D-mannosamine/glucosamine dehydrogenase
3 209 Gene3D G3DSA:3.40.50.720 -
211 433 Gene3D G3DSA:3.40.50.720 -
17 435 PIRSF PIRSF000124 UDPglc_GDPman_dh
17 435 InterPro IPR017476 UDP-glucose/GDP-mannose dehydrogenase
18 206 SUPERFAMILY SSF51735 NAD(P)-binding Rossmann-fold domains
18 206 InterPro IPR036291 NAD(P)-binding domain superfamily
212 305 SUPERFAMILY SSF48179 6-phosphogluconate dehydrogenase C-terminal domain-like
212 305 InterPro IPR008927 6-phosphogluconate dehydrogenase-like, C-terminal domain superfamily
317 427 SUPERFAMILY SSF52413 UDP-glucose/GDP-mannose dehydrogenase C-terminal domain
317 427 InterPro IPR036220 UDP-glucose/GDP-mannose dehydrogenase, C-terminal domain superfamily
6 435 PIRSF PIRSF500136 UDP_ManNAc_DH
6 435 InterPro IPR028359 UDP-N-acetyl-D-mannosamine/glucosamine dehydrogenase
13 32 TMHMM TMhelix Region of a membrane-bound protein predicted to be embedded in the membrane.
330 428 SMART SM00984 UDPG_MGDP_dh_C_a_2_a
330 428 InterPro IPR014027 UDP-glucose/GDP-mannose dehydrogenase, C-terminal
18 423 NCBIfam TIGR03026 nucleotide sugar dehydrogenase
18 423 InterPro IPR017476 UDP-glucose/GDP-mannose dehydrogenase
330 424 Pfam PF03720 UDP-glucose/GDP-mannose dehydrogenase family, UDP binding domain
330 424 InterPro IPR014027 UDP-glucose/GDP-mannose dehydrogenase, C-terminal
211 434 FunFam G3DSA:3.40.50.720:FF:000727 UDP-N-acetyl-D-glucosamine dehydrogenase
213 303 Pfam PF00984 UDP-glucose/GDP-mannose dehydrogenase family, central domain
213 303 InterPro IPR014026 UDP-glucose/GDP-mannose dehydrogenase, dimerisation

3D Structure

Selected loaded structure. Experimental PDB entries may cover only a portion of the sequence; predicted models typically cover the full protein.

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Structural evidence

0 + 1

Experimental PDB entries and predicted models. Click Switch to display a different structure in the viewer.

Entry Method Resolution Chain Coverage Links Status
AlphaFold PA3159
AlphaFold full sequence Viewing
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 0.275
3 0.251

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

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.

Show only:
Ligand Source crystal UniProt (homolog) MW · LogP · TPSA Lipinski PAINS SMILES
PDC P95708 167.1 Da LogP 0.48 TPSA 87.5 ✓ Ro5 ✓ Clean c1cc(nc(c1)C(=O)O)C(=O)O
SAJ 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 C9E261 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 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…

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.