Protein profile

PA3181

2-dehydro-3-deoxy-phosphogluconate aldolase

Genome: NC_002516.2

Gene: eda PA3181 Structure source: AlphaFold UniProt O68283
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Amino acids 220
Annotations 6
Features 15
PDB binders 4
Druggability 0.337

Overview

Basic information about this protein and its source genome.

Accession
PA3181
Assembly
Pseudomonas aeruginosa PAO1, complete genome
Gene
eda PA3181
Status
annotated
Amino acids
220
Structure source
AlphaFold
EC
4.1.2.14
GO
GO:0106009 Catalysis of the reaction:(4S)-4-hydroxy-2-oxoglutarate = pyruvate + glyoxylate. Specific for the (4S) enantiomer of 4-hydroxy-2-oxoglutarate. GO:0008675 Catalysis of the reaction: 2-dehydro-3-deoxy-D-gluconate 6-phosphate = pyruvate + D-glyceraldehyde 3-phosphate. GO:0016832 Catalysis of the cleavage of a C-C bond in a molecule containing a hydroxyl group and a carbonyl group to form two smaller molecules, each being an aldehyde or a ketone. GO:0009255 A pathway that converts a carbohydrate to pyruvate and glyceraldehyde-3 phosphate by producing 6-phosphogluconate and then dehydrating it. GO:0016829 Catalysis of the cleavage of C-C, C-O, C-N and other bonds by other means than by hydrolysis or oxidation, or conversely adding a group to a double bond. They differ from other enzymes in that two substrates are involved in one reaction direction, but only one in the other direction. When acting on the single substrate, a molecule is eliminated and this generates either a new double bond or a new ring.

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 0.337
Structure –
Pocket –

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 5 GO

Enzyme Commission (EC)

1

Gene Ontology (GO)

5
  • GO:0106009 Catalysis of the reaction:(4S)-4-hydroxy-2-oxoglutarate = pyruvate + glyoxylate. Specific for the (4S) enantiomer of 4-hydroxy-2-oxoglutarate.
  • GO:0008675 Catalysis of the reaction: 2-dehydro-3-deoxy-D-gluconate 6-phosphate = pyruvate + D-glyceraldehyde 3-phosphate.
  • GO:0016832 Catalysis of the cleavage of a C-C bond in a molecule containing a hydroxyl group and a carbonyl group to form two smaller molecules, each being an aldehyde or a ketone.
  • GO:0009255 A pathway that converts a carbohydrate to pyruvate and glyceraldehyde-3 phosphate by producing 6-phosphogluconate and then dehydrating it.
  • GO:0016829 Catalysis of the cleavage of C-C, C-O, C-N and other bonds by other means than by hydrolysis or oxidation, or conversely adding a group to a double bond. They differ from other enzymes in that two substrates are involved in one reaction direction, but only one in the other direction. When acting on the single substrate, a molecule is eliminated and this generates either a new double bond or a new ring.

Sequence Features

Domain/signature hits from InterPro and related databases.

15 records
Show feature table
Start End DB Term Name
43 52 ProSitePatterns PS00159 KDPG and KHG aldolases active site.
43 52 InterPro IPR031337 KDPG/KHG aldolase, active site 1
5 218 PANTHER PTHR30246 2-KETO-3-DEOXY-6-PHOSPHOGLUCONATE ALDOLASE
5 218 InterPro IPR000887 KDPG/KHG aldolase
16 206 CDD cd00452 KDPG_aldolase
16 206 InterPro IPR000887 KDPG/KHG aldolase
131 144 ProSitePatterns PS00160 KDPG and KHG aldolases Schiff-base forming residue.
131 144 InterPro IPR031338 KDPG/KHG aldolase, active site 2
1 214 Gene3D G3DSA:3.20.20.70 Aldolase class I
1 214 InterPro IPR013785 Aldolase-type TIM barrel
11 206 Pfam PF01081 KDPG and KHG aldolase
11 206 InterPro IPR000887 KDPG/KHG aldolase
12 213 NCBIfam TIGR01182 bifunctional 4-hydroxy-2-oxoglutarate aldolase/2-dehydro-3-deoxy-phosphogluconate aldolase
12 213 InterPro IPR000887 KDPG/KHG aldolase
10 213 SUPERFAMILY SSF51569 Aldolase

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 PA3181
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
2 0.337
1 0.292
6 0.246

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.

52 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
3PG
5XSF
Q00384 186.1 Da LogP -1.46 TPSA 124.3 ✓ Ro5 ✓ Clean C([C@H](C(=O)O)O)OP(=O)(O)O
3PY
5XSF
Q00384 104.1 Da LogP -1.37 TPSA 74.6 ✓ Ro5 ✓ Clean C(C(=O)C(=O)O)O
PVO
6OVI
Q5ZYF2 106.1 Da LogP -1.23 TPSA 77.8 ✓ Ro5 ✓ Clean CC(C(=O)O)(O)O
PYR
3VCR
D2YW47 88.1 Da LogP -0.34 TPSA 54.4 ✓ Ro5 ✓ Clean CC(=O)C(=O)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.