Protein profile

PA4588

glutamate dehydrogenase

Genome: NC_002516.2

Gene: gdhA PA4588 Structure source: AlphaFold UniProt Q9HVJ7
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Amino acids 445
Annotations 7
Features 32
PDB binders 7
Druggability 0.667

Overview

Basic information about this protein and its source genome.

Accession
PA4588
Assembly
Pseudomonas aeruginosa PAO1, complete genome
Gene
gdhA PA4588
Status
annotated
Amino acids
445
Structure source
AlphaFold
GO
GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. GO:0004354 Catalysis of the reaction: L-glutamate + NADP+ + H2O = 2-oxoglutarate + NH4+ + NADPH + H+. GO:0000166 Binding to a nucleotide, any compound consisting of a nucleoside that is esterified with (ortho)phosphate or an oligophosphate at any hydroxyl group on the ribose or deoxyribose. GO:0006537 OBSOLETE. The chemical reactions and pathways resulting in the formation of glutamate, the anion of 2-aminopentanedioic acid. GO:0016639 Catalysis of an oxidation-reduction (redox) reaction in which a CH-NH2 group acts as a hydrogen or electron donor and reduces NAD+ or NADP. GO:0006520 The chemical reactions and pathways involving amino acids, carboxylic acids containing one or more amino groups.

Target profile

Computed evidence for target prioritization.

Human off-target
hit
Human identity (%)
33.0
Human E-value
8.78e-09
Gut microbiome off-target
hit
Essential (DEG)
Y
Localization
Unknown

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 0.667
Structure –
Pocket –

Sequence

Primary amino-acid sequence viewer.

MTQSVDAFLERLKRRDPDQPEFHQAVEEVLRSLWPFLEANPHYLEAGIIERIVEPERAILFRVPWVDDQGRVRVNRGYRVQMSSAIGPYKGGLRFHPSVNLGVLKFLAFEQVFKNSLTTLPMGGGKGGSDFDPKGKSDAEVMRFCQSFMSELYRHVGADLDVPAGDIGVGAREIGYLFGQYKRLSNQFTSVLTGKGLSYGGSLIRPEATGFGCVYFAQEMLKDRGRGFDGQRVAISGSGNVAQYAARKVMEMGGKVISLSDSEGTLYAEAGLSDEQWEYLMELKNVRRGRIREMAEQFSLQFLEGRRPWGLACDIALPCATQNELDAEDARRLLANGCVCVAEGANMPSTLEAVDLFLEAGILYAPGKASNAGGVAVSGLEMSQNAMRLRWSEGEVDTKLHGIMQSIHHACLLYGEEQGRVNYVKGANIAGFVKVADAMLAQGVV

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

7 GO

Gene Ontology (GO)

7
  • GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
  • GO:0004354 Catalysis of the reaction: L-glutamate + NADP+ + H2O = 2-oxoglutarate + NH4+ + NADPH + H+.
  • GO:0000166 Binding to a nucleotide, any compound consisting of a nucleoside that is esterified with (ortho)phosphate or an oligophosphate at any hydroxyl group on the ribose or deoxyribose.
  • GO:0006537 OBSOLETE. The chemical reactions and pathways resulting in the formation of glutamate, the anion of 2-aminopentanedioic acid.
  • GO:0016639 Catalysis of an oxidation-reduction (redox) reaction in which a CH-NH2 group acts as a hydrogen or electron donor and reduces NAD+ or NADP.
  • GO:0006520 The chemical reactions and pathways involving amino acids, carboxylic acids containing one or more amino groups.
  • 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.

Sequence Features

Domain/signature hits from InterPro and related databases.

32 records
Show feature table
Start End DB Term Name
55 182 Pfam PF02812 Glu/Leu/Phe/Val dehydrogenase, dimerisation domain
55 182 InterPro IPR006097 Glutamate/phenylalanine/leucine/valine/L-tryptophan dehydrogenase, dimerisation domain
53 188 Gene3D G3DSA:3.40.50.10860 Leucine Dehydrogenase, chain A, domain 1
377 445 FunFam G3DSA:1.10.285.10:FF:000001 Glutamate dehydrogenase
53 188 FunFam G3DSA:3.40.50.10860:FF:000002 Glutamate dehydrogenase
370 381 PRINTS PR00082 Glutamate/leucine/phenylalanine/valine dehydrogenase signature
370 381 InterPro IPR006095 Glutamate/phenylalanine/leucine/valine/L-tryptophan dehydrogenase
233 253 PRINTS PR00082 Glutamate/leucine/phenylalanine/valine dehydrogenase signature
233 253 InterPro IPR006095 Glutamate/phenylalanine/leucine/valine/L-tryptophan dehydrogenase
112 126 PRINTS PR00082 Glutamate/leucine/phenylalanine/valine dehydrogenase signature
112 126 InterPro IPR006095 Glutamate/phenylalanine/leucine/valine/L-tryptophan dehydrogenase
191 213 PRINTS PR00082 Glutamate/leucine/phenylalanine/valine dehydrogenase signature
191 213 InterPro IPR006095 Glutamate/phenylalanine/leucine/valine/L-tryptophan dehydrogenase
207 372 FunFam G3DSA:3.40.50.720:FF:000030 Glutamate dehydrogenase
380 445 Gene3D G3DSA:1.10.285.10 Glutamate Dehydrogenase, chain A, domain 3
200 443 Pfam PF00208 Glutamate/Leucine/Phenylalanine/Valine dehydrogenase
200 443 InterPro IPR006096 Glutamate/phenylalanine/leucine/valine/L-tryptophan dehydrogenase, C-terminal
20 445 PIRSF PIRSF000185 Glu_DH
20 445 InterPro IPR014362 Glutamate dehydrogenase
2 445 PANTHER PTHR43571 NADP-SPECIFIC GLUTAMATE DEHYDROGENASE 1-RELATED
200 444 SUPERFAMILY SSF51735 NAD(P)-binding Rossmann-fold domains
200 444 InterPro IPR036291 NAD(P)-binding domain superfamily
207 371 Gene3D G3DSA:3.40.50.720 -
193 444 CDD cd05313 NAD_bind_2_Glu_DH
193 444 InterPro IPR033922 NAD(P) binding domain of glutamate dehydrogenase
4 194 SUPERFAMILY SSF53223 Aminoacid dehydrogenase-like, N-terminal domain
4 194 InterPro IPR046346 Aminoacid dehydrogenase-like, N-terminal domain superfamily
8 379 Gene3D G3DSA:1.10.285.10 Glutamate Dehydrogenase, chain A, domain 3
202 443 SMART SM00839 ELFV_dehydrog_3
202 443 InterPro IPR006096 Glutamate/phenylalanine/leucine/valine/L-tryptophan dehydrogenase, C-terminal
120 133 ProSitePatterns PS00074 Glu / Leu / Phe / Val dehydrogenases active site.
120 133 InterPro IPR033524 Leu/Phe/Val dehydrogenases active site

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 PA4588
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 0.667

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.

57 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
8G0
5XW0
B6V7E4 166.1 Da LogP 1.08 TPSA 74.6 ✓ Ro5 ✓ Clean c1cc(cc(c1)C(=O)O)C(=O)O
A2R
7ECR
T2D1F5 639.3 Da LogP -3.17 TPSA 338.0 3 viol. ✓ Clean c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)…
AKG
5XVV
B6V7E4 146.1 Da LogP -0.50 TPSA 91.7 ✓ Ro5 ✓ Clean C(CC(=O)O)C(=O)C(=O)O
MLI
7ECS
T2D1F5 102.0 Da LogP -3.12 TPSA 80.3 ✓ Ro5 ✓ Clean C(C(=O)[O-])C(=O)[O-]
NH4
3AOG
Q72IC1 18.0 Da LogP 0.38 TPSA 36.5 ✓ Ro5 ✓ Clean [NH4+]
SIN
7ECR
T2D1F5 118.1 Da LogP -0.06 TPSA 74.6 ✓ Ro5 ✓ Clean C(CC(=O)O)C(=O)O
TLA
7ECT
T2D1F5 150.1 Da LogP -2.12 TPSA 115.1 ✓ Ro5 ✓ Clean [C@@H]([C@H](C(=O)O)O)(C(=O)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.