Protein profile

PA0743

NAD-dependent L-serine dehydrogenase

Genome: NC_002516.2

Gene: PA0743 Structure source: Experimental + AlphaFold UniProt Q9I5I6
Export view
Amino acids 298
Annotations 9
Features 20
PDB binders 8
Druggability 0.807

Overview

Basic information about this protein and its source genome.

Accession
PA0743
Assembly
Pseudomonas aeruginosa PAO1, complete genome
Gene
PA0743
Status
annotated
Amino acids
298
Structure source
Experimental + AlphaFold
EC
1.1.1.387
GO
GO:0008442 Catalysis of the reaction: 3-hydroxy-2-methylpropanoate + NAD+ = 2-methyl-3-oxopropanoate + NADH + H+. 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: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: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. GO:0009083 The chemical reactions and pathways resulting in the breakdown of amino acids containing a branched carbon skeleton, comprising isoleucine, leucine and valine. GO:0006565 The chemical reactions and pathways resulting in the breakdown of L-serine.

Target profile

Computed evidence for target prioritization.

Human off-target
hit
Human identity (%)
44.509
Human E-value
9.38e-45
Gut microbiome off-target
hit
Essential (DEG)
N
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 0.807
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:0008442 Catalysis of the reaction: 3-hydroxy-2-methylpropanoate + NAD+ = 2-methyl-3-oxopropanoate + NADH + H+.
  • 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: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: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.
  • GO:0009083 The chemical reactions and pathways resulting in the breakdown of amino acids containing a branched carbon skeleton, comprising isoleucine, leucine and valine.
  • GO:0006565 The chemical reactions and pathways resulting in the breakdown of L-serine.
  • GO:0051289 The formation of a protein homotetramer, a macromolecular structure consisting of four noncovalently associated identical subunits.
  • 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.

20 records
Show feature table
Start End DB Term Name
1 298 PIRSF PIRSF000103 HIBADH
1 298 InterPro IPR015815 3-hydroxyisobutyrate dehydrogenase-related
165 297 FunFam G3DSA:1.10.1040.10:FF:000006 3-hydroxyisobutyrate dehydrogenase
1 164 FunFam G3DSA:3.40.50.720:FF:000071 2-hydroxy-3-oxopropionate reductase
165 291 Pfam PF14833 NAD-binding of NADP-dependent 3-hydroxyisobutyrate dehydrogenase
165 291 InterPro IPR029154 3-hydroxyisobutyrate dehydrogenase-like, NAD-binding domain
6 292 NCBIfam TIGR01692 3-hydroxyisobutyrate dehydrogenase
6 292 InterPro IPR011548 3-hydroxyisobutyrate dehydrogenase
164 293 SUPERFAMILY SSF48179 6-phosphogluconate dehydrogenase C-terminal domain-like
164 293 InterPro IPR008927 6-phosphogluconate dehydrogenase-like, C-terminal domain superfamily
1 293 PANTHER PTHR22981 3-HYDROXYISOBUTYRATE DEHYDROGENASE-RELATED
3 162 Pfam PF03446 NAD binding domain of 6-phosphogluconate dehydrogenase
3 162 InterPro IPR006115 6-phosphogluconate dehydrogenase, NADP-binding
1 162 SUPERFAMILY SSF51735 NAD(P)-binding Rossmann-fold domains
1 162 InterPro IPR036291 NAD(P)-binding domain superfamily
1 163 Gene3D G3DSA:3.40.50.720 -
6 19 ProSitePatterns PS00895 3-hydroxyisobutyrate dehydrogenase signature.
6 19 InterPro IPR002204 3-hydroxyisobutyrate dehydrogenase-related, conserved site
164 298 Gene3D G3DSA:1.10.1040.10 -
164 298 InterPro IPR013328 6-phosphogluconate dehydrogenase, domain 2

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

2 + 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 3OBB
X-ray 2.20 Å A
100.0% 1-298
PDBe RCSB PDBj File
Viewing
PDB 3Q3C
X-ray 2.30 Å A
100.0% 1-298
PDBe RCSB PDBj File
Loaded
AlphaFold PA0743
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 0.807
4 0.492

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 30.54 0.935
2 2.02 0.044
3 1.93 0.039
4 1.02 0.006

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.

58 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
3OH
5Y8O
P9WNY5 90.1 Da LogP -0.55 TPSA 57.5 ✓ Ro5 ✓ Clean C(CO)C(=O)O
9ON
5Y8L
P9WNY5 146.1 Da LogP 0.57 TPSA 74.6 ✓ Ro5 ✓ Clean C[C@@H](CCC(=O)O)C(=O)O
AKR
5Y8M
P9WNY5 72.1 Da LogP 0.26 TPSA 37.3 ✓ Ro5 ✓ Clean C=CC(=O)O
BO3
6SM7
P0A9V8 61.8 Da LogP -2.05 TPSA 60.7 ✓ Ro5 ✓ Clean B(O)(O)O
HIU
5Y8M
P9WNY5 104.1 Da LogP -0.30 TPSA 57.5 ✓ Ro5 ✓ Clean C[C@H](CO)C(=O)O
HUI
5Y8L
P9WNY5 104.1 Da LogP -0.30 TPSA 57.5 ✓ Ro5 ✓ Clean C[C@@H](CO)C(=O)O
LLQ
6SMY
P0A9V8 156.2 Da LogP -1.77 TPSA 94.8 ✓ Ro5 ✓ Clean C([C@@H](CS(=O)(=O)O)O)O
TLA
5XVH
A3MU08 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.