Protein profile

PA3155

UDP-2-acetamido-2-deoxy-3-oxo-D-glucuronate aminotransferase

Genome: NC_002516.2

Gene: PA3155 wbpE Structure source: Experimental + AlphaFold UniProt Q9HZ76
Export view
Amino acids 359
Annotations 9
Features 15
PDB binders 9
Druggability 0.786

Overview

Basic information about this protein and its source genome.

Accession
PA3155
Assembly
Pseudomonas aeruginosa PAO1, complete genome
Gene
PA3155 wbpE
Status
annotated
Amino acids
359
Structure source
Experimental + AlphaFold
EC
2.6.1.98
GO
GO:0030170 Binding to pyridoxal 5' phosphate, 3-hydroxy-5-(hydroxymethyl)-2-methyl4-pyridine carboxaldehyde 5' phosphate, the biologically active form of vitamin B6. GO:0008483 Catalysis of the transfer of an amino group to an acceptor, usually a 2-oxo acid. 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:0009103 The chemical reactions and pathways resulting in the formation of lipopolysaccharides, any of a group of related, structurally complex components of the outer membrane of Gram-negative bacteria. 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.

Target profile

Computed evidence for target prioritization.

Human off-target
No hit
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 0.786
Structure –
Pocket –

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 8 GO

Enzyme Commission (EC)

1

Gene Ontology (GO)

8
  • GO:0030170 Binding to pyridoxal 5' phosphate, 3-hydroxy-5-(hydroxymethyl)-2-methyl4-pyridine carboxaldehyde 5' phosphate, the biologically active form of vitamin B6.
  • GO:0008483 Catalysis of the transfer of an amino group to an acceptor, usually a 2-oxo acid.
  • 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:0009103 The chemical reactions and pathways resulting in the formation of lipopolysaccharides, any of a group of related, structurally complex components of the outer membrane of Gram-negative bacteria.
  • 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:0006065 The chemical reactions and pathways resulting in the formation of UDP-glucuronate, a substance composed of glucuronic acid in glycosidic linkage with uridine diphosphate.
  • GO:0003824 Catalysis of a biochemical reaction at physiological temperatures. In biologically catalyzed reactions, the reactants are known as substrates, and the catalysts are naturally occurring macromolecular substances known as enzymes. Enzymes possess specific binding sites for substrates, and are usually composed wholly or largely of protein, but RNA that has catalytic activity (ribozyme) is often also regarded as enzymatic.

Sequence Features

Domain/signature hits from InterPro and related databases.

15 records
Show feature table
Start End DB Term Name
22 357 CDD cd00616 AHBA_syn
22 357 InterPro IPR000653 DegT/DnrJ/EryC1/StrS aminotransferase
1 244 Gene3D G3DSA:3.40.640.10 -
1 244 InterPro IPR015421 Pyridoxal phosphate-dependent transferase, major domain
1 244 FunFam G3DSA:3.40.640.10:FF:000089 Aminotransferase, DegT/DnrJ/EryC1/StrS family
1 359 PIRSF PIRSF000390 PLP_StrS
1 359 InterPro IPR000653 DegT/DnrJ/EryC1/StrS aminotransferase
15 358 SUPERFAMILY SSF53383 PLP-dependent transferases
15 358 InterPro IPR015424 Pyridoxal phosphate-dependent transferase
14 357 Pfam PF01041 DegT/DnrJ/EryC1/StrS aminotransferase family
14 357 InterPro IPR000653 DegT/DnrJ/EryC1/StrS aminotransferase
9 358 PANTHER PTHR30244 TRANSAMINASE
9 358 InterPro IPR000653 DegT/DnrJ/EryC1/StrS aminotransferase
245 359 Gene3D G3DSA:3.90.1150.10 Aspartate Aminotransferase, domain 1
245 359 InterPro IPR015422 Pyridoxal phosphate-dependent transferase, small domain

3D Structure

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

3D visualization script Full viewer

Loading 3D structure...

Legend High Medium Low

Structural evidence

6 + 1

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

Entry Method Resolution Chain Coverage Links Status
PDB 3NYT
X-ray 1.30 Å A
100.0% 1-359
PDBe RCSB PDBj File
Viewing
PDB 3NYS
X-ray 1.45 Å A
100.0% 1-359
PDBe RCSB PDBj File
Loaded
PDB 3NU8
X-ray 1.50 Å A,B
100.0% 1-359
PDBe RCSB PDBj File
Loaded
PDB 3NYU
X-ray 1.50 Å A,B,C,D
100.0% 1-359
PDBe RCSB PDBj File
Loaded
PDB 3NUB
X-ray 1.90 Å A,B
100.0% 1-359
PDBe RCSB PDBj File
Loaded
PDB 3NU7
X-ray 1.95 Å A,B
100.0% 1-359
PDBe RCSB PDBj File
Loaded
AlphaFold PA3155
AlphaFold — — 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 0.786

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 18.84 0.831
2 6.57 0.333
3 1.61 0.026

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.

59 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.

Show only:
Ligand Source crystal MW · LogP · TPSA Lipinski PAINS SMILES
PMP
3NU7 1.95 Å Open crystal
248.2 Da LogP 0.16 TPSA 125.9 ✓ Ro5 ✓ Clean Cc1c(c(c(cn1)COP(=O)(O)O)CN)O
UD0
3NUB 1.90 Å Open crystal
849.5 Da LogP -3.41 TPSA 414.9 3 viol. ✓ Clean Cc1c(c(c(cn1)COP(=O)(O)O)/C=N/[C@@H]2[C@H]([C@H…
ULP
3NYT 1.30 Å Open crystal
849.5 Da LogP -3.41 TPSA 414.9 3 viol. ✓ Clean Cc1c(c(c(cn1)COP(=O)(O)O)/C=N/[C@@H]2[C@H]([C@H…

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.