Protein profile
PA3159
UDP-N-acetyl-d-glucosamine 6-dehydrogenase
Genome: NC_002516.2
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.
Sequence
Primary amino-acid sequence viewer.
Functional Annotations
Enzyme classification and Gene Ontology terms linked to this protein.
Enzyme Commission (EC)
1Gene 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.
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.
Loading 3D structure...
Structural evidence
0 + 1Experimental 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.
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 | 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…
|
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
|
| ZINC12959005 | 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)(O)…
|
| ZINC12959016 | 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)(O…
|
| 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)(…
|
| ZINC25726233 | 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)(O)…
|
| ZINC3861755 | 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)(…
|
| ZINC3875255 | 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)(…
|
| ZINC3875256 | 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)…
|
| ZINC3875257 | 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)(…
|
| ZINC3875258 | 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)…
|
| ZINC88466482 | 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
|
| ZINC35636069 | 0.724 | 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 | 0.724 | 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 | 0.724 | 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 | 0.724 | 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 | 0.724 | 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 | 0.724 | 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 | 0.724 | 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 | 0.724 | 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 | 0.724 | 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…
|
| ZINC102211562 | 0.698 | 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 | 0.698 | 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 | 0.698 | 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 | 0.698 | 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]…
|
| 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
|
| 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
|
| ZINC12503831 | 0.655 | 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 | 0.655 | 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 | 0.655 | 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 | 0.655 | 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 | 0.655 | 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 | 0.655 | 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 | 0.655 | 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 | 0.655 | 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 | 0.655 | 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 | 0.655 | 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 | 0.655 | 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 | 0.655 | 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 | 0.655 | 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…
|
| ZINC98175528 | 0.640 | 240.5 Da LogP 2.61 TPSA 50.2 | ✓ Ro5 | ✓ Clean |
O=C(O)c1cccc(C(Cl)(Cl)Cl)n1
|
| ZINC108477652 | 0.631 | 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)(O)…
|
| ZINC145753022 | 0.631 | 483.2 Da LogP -2.53 TPSA 270.2 | 2 viol. | ✓ Clean |
N[C@@H]1[C@H](O)[C@H](CO[P@@](=O)(O)O[P@@](=O)(…
|
| ZINC220143873 | 0.631 | 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)(…
|
| ZINC31519946 | 0.631 | 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)(O)…
|
| ZINC78695900 | 0.631 | 483.2 Da LogP -2.53 TPSA 270.2 | 2 viol. | ✓ Clean |
N[C@@H]1[C@H](O)[C@H](CO[P@@](=O)(O)O[P@@](=O)(…
|
| ZINC90614026 | 0.631 | 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)(…
|
| 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
|
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.