Protein profile

PA3736

homoserine dehydrogenase

Genome: NC_002516.2

Gene: PA3736 hom Structure source: AlphaFold UniProt P29365
Export view
Amino acids 434
Annotations 9
Features 24
PDB binders 7
Druggability 0.707

Overview

Basic information about this protein and its source genome.

Accession
PA3736
Assembly
Pseudomonas aeruginosa PAO1, complete genome
Gene
PA3736 hom
Status
annotated
Amino acids
434
Structure source
AlphaFold
EC
1.1.1.3
GO
GO:0004412 Catalysis of the reaction: L-homoserine + NADP+ = L-aspartate-4-semialdehyde + NADPH + H+. GO:0046872 Binding to a metal ion. GO:0070403 Binding to the oxidized form, NAD, of nicotinamide adenine dinucleotide, a coenzyme involved in many redox and biosynthetic reactions. GO:0050661 Binding to nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions; binding may be to either the oxidized form, NADP+, or the reduced form, NADPH. GO:0009086 OBSOLETE. The chemical reactions and pathways resulting in the de novo formation of L-methionine (2-amino-4-(methylthio)butanoic acid), a sulfur-containing, essential amino acid found in peptide linkage in proteins. GO:0009088 The chemical reactions and pathways resulting in the formation of L-threonine (2-amino-3-hydroxybutyric acid), a polar, uncharged, essential amino acid found in peptide linkage in proteins.

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 0.707
Structure –
Pocket –

Sequence

Primary amino-acid sequence viewer.

MKPVKVGICGLGTVGGGTFNVLERNAEEIARRAGRGIEVAQIAARRPNPKCDTGATPITADIFDVACNPEIDVVVELIGGYTLAHELVLKAIENGKHVVTANKALIAVHGNEIFAKAREKGVIVAFEAAVAGGIPVIKAIREGLSANRINWLAGIINGTGNFILSEMREKGRTFPDVLAEAQALGYAEADPTFDVEGIDAAHKLTILASIAFGIPLQFDKAYTEGISKLTSADVNYADALGYRIKHLGVARRTESGFELRVHPTLIPSDRLIANVNGVMNAVMVNGDAVGSTLYYGAGAGMEPTASSVVADLVDVVRAMTSDPENRVPHLAFQPDALSDHPILPIEACESAYYLRIQAKDHPGVLAQVATILSERGINIESIMQKEAEEQDGLVPMILVTHRVIEQRINDAIAALEALEGVSGPVVRIRVEQLN

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:0004412 Catalysis of the reaction: L-homoserine + NADP+ = L-aspartate-4-semialdehyde + NADPH + H+.
  • GO:0046872 Binding to a metal ion.
  • GO:0070403 Binding to the oxidized form, NAD, of nicotinamide adenine dinucleotide, a coenzyme involved in many redox and biosynthetic reactions.
  • GO:0050661 Binding to nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions; binding may be to either the oxidized form, NADP+, or the reduced form, NADPH.
  • GO:0009086 OBSOLETE. The chemical reactions and pathways resulting in the de novo formation of L-methionine (2-amino-4-(methylthio)butanoic acid), a sulfur-containing, essential amino acid found in peptide linkage in proteins.
  • GO:0009088 The chemical reactions and pathways resulting in the formation of L-threonine (2-amino-3-hydroxybutyric acid), a polar, uncharged, essential amino acid found in peptide linkage in proteins.
  • 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.

24 records
Show feature table
Start End DB Term Name
134 302 FunFam G3DSA:3.30.360.10:FF:000005 Homoserine dehydrogenase
347 422 FunFam G3DSA:3.30.70.260:FF:000030 Homoserine dehydrogenase
352 431 CDD cd04881 ACT_HSDH-Hom
10 127 Pfam PF03447 Homoserine dehydrogenase, NAD binding domain
10 127 InterPro IPR005106 Aspartate/homoserine dehydrogenase, NAD-binding
1 321 PANTHER PTHR43331 HOMOSERINE DEHYDROGENASE
135 313 Pfam PF00742 Homoserine dehydrogenase
135 313 InterPro IPR001342 Homoserine dehydrogenase, catalytic
353 429 ProSiteProfiles PS51671 ACT domain profile.
353 429 InterPro IPR002912 ACT domain
350 420 SUPERFAMILY SSF55021 ACT-like
350 420 InterPro IPR045865 ACT-like domain
181 203 ProSitePatterns PS01042 Homoserine dehydrogenase signature.
181 203 InterPro IPR019811 Homoserine dehydrogenase, conserved site
134 346 Gene3D G3DSA:3.30.360.10 Dihydrodipicolinate Reductase; domain 2
347 422 Gene3D G3DSA:3.30.70.260 -
4 338 Gene3D G3DSA:3.40.50.720 -
1 433 PIRSF PIRSF000098 Homoser_dh
1 433 InterPro IPR016204 Homoserine dehydrogenase
352 419 Pfam PF01842 ACT domain
352 419 InterPro IPR002912 ACT domain
1 156 SUPERFAMILY SSF51735 NAD(P)-binding Rossmann-fold domains
1 156 InterPro IPR036291 NAD(P)-binding domain superfamily
135 300 SUPERFAMILY SSF55347 Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal 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

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 PA3736
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 0.707

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
178
1TVE
P31116 302.4 Da LogP 5.50 TPSA 40.5 1 viol. ✓ Clean CC(C)c1cc(ccc1O)Sc2ccc(c(c2)C(C)C)O
80F
5X9D
F9VNG5 784.6 Da LogP -3.56 TPSA 380.9 3 viol. ✓ Clean c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)…
CXS
6A0R
Q5SL04 221.3 Da LogP 1.19 TPSA 66.4 ✓ Ro5 ✓ Clean C1CCC(CC1)NCCCS(=O)(=O)O
HSE
4XB2
O58802 119.1 Da LogP -1.22 TPSA 83.5 ✓ Ro5 ✓ Clean C(CO)[C@@H](C(=O)O)N
NDA
1EBU
P31116 649.4 Da LogP -3.29 TPSA 304.0 3 viol. ✓ Clean c1cc(c[n+](c1)[C@H]2[C@@H]([C@@H]([C@H](O2)CO[P…
NHO
1Q7G
P31116 809.6 Da LogP -4.61 TPSA 418.9 3 viol. ✓ Clean c1c[n+](cc(c1[C@@H](C(=O)C[C@@H](C(=O)O)N)O)C(=…
TLA
5X9D
F9VNG5 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.