Protein profile

VK055_0716

aspartate-semialdehyde dehydrogenase

Genome: KpATCC43816

Gene: asd AIK79339.1 Structure source: AlphaFold + ColabFold UniProt A0A0H3GTQ2
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Amino acids 352
Annotations 13
Features 17
PDB binders 4
Druggability 0.838

Overview

Basic information about this protein and its source genome.

Accession
VK055_0716
Assembly
Klebsiella pneumoniae subsp. pneumoniae strain ATCC 43816 KPPR1, complete genome
Gene
asd AIK79339.1
Status
annotated
Amino acids
352
Structure source
AlphaFold + ColabFold
EC
1.2.1.11
GO
GO:0016620 Catalysis of an oxidation-reduction (redox) reaction in which an aldehyde or ketone (oxo) group acts as a hydrogen or electron donor and reduces NAD or NADP. GO:0009097 OBSOLETE. The chemical reactions and pathways resulting in the formation of isoleucine, (2R*,3R*)-2-amino-3-methylpentanoic acid. 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: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:0009089 OBSOLETE. The chemical reactions and pathways resulting in the formation of lysine, via the intermediate diaminopimelate. GO:0046983 The formation of a protein dimer, a macromolecular structure consists of two noncovalently associated identical or nonidentical subunits.

Target profile

Computed evidence for target prioritization.

Human off-target
No hit
Human identity (%)
0.0
Gut microbiome off-target
hit
Essential (DEG)
Y
DEG identity (%)
54.571
DEG E-value
1.04e-133
Localization
Cytoplasmic
ColabFold pLDDT
97.1

Selected Druggability evidence

AlphaFold / UniProt model

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 0.838
Structure A0A0H3GTQ2
Pocket Pocket 1
P2Rank 0.76
Structure A0A0H3GTQ2
Pocket Pocket 1
ColabFold model
FPocket 0.124 · Pocket 19
P2Rank 0.352 · Pocket 1
Core conservation Accessory gene
Roary core
CoreCruncher accessory
Gut microbiome 191 / 4744 genomes with a hit
Normalized 0.04

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 12 GO

Enzyme Commission (EC)

1

Gene Ontology (GO)

12
  • GO:0016620 Catalysis of an oxidation-reduction (redox) reaction in which an aldehyde or ketone (oxo) group acts as a hydrogen or electron donor and reduces NAD or NADP.
  • GO:0009097 OBSOLETE. The chemical reactions and pathways resulting in the formation of isoleucine, (2R*,3R*)-2-amino-3-methylpentanoic acid.
  • 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: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:0009089 OBSOLETE. The chemical reactions and pathways resulting in the formation of lysine, via the intermediate diaminopimelate.
  • GO:0046983 The formation of a protein dimer, a macromolecular structure consists of two noncovalently associated identical or nonidentical subunits.
  • 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:0004073 Catalysis of the reaction: L-aspartate 4-semialdehyde + NADP+ + phosphate = 4-phospho-L-aspartate + H+ + NADPH.
  • 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:0006520 The chemical reactions and pathways involving amino acids, carboxylic acids containing one or more amino groups.
  • GO:0008652 The chemical reactions and pathways resulting in the formation of amino acids, organic acids containing one or more amino substituents.
  • GO:0019877 OBSOLETE. The chemical reactions and pathways resulting in the formation of diaminopimelate, both as an intermediate in lysine biosynthesis and as a component (as meso-diaminopimelate) of the peptidoglycan of Gram-negative bacterial cell walls.

Sequence Features

Domain/signature hits from InterPro and related databases.

17 records
Show feature table
Start End DB Term Name
116 333 Gene3D G3DSA:3.30.360.10 Dihydrodipicolinate Reductase; domain 2
114 336 SUPERFAMILY SSF55347 Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain
1 349 NCBIfam TIGR01745 aspartate-semialdehyde dehydrogenase
1 349 InterPro IPR011534 Aspartate-semialdehyde dehydrogenase, gamma-type
2 349 PANTHER PTHR46278 DEHYDROGENASE, PUTATIVE-RELATED
1 102 SMART SM00859 Semialdhyde_dh_3
1 102 InterPro IPR000534 Semialdehyde dehydrogenase, NAD-binding
1 352 PIRSF PIRSF000148 ASA_dh
1 338 Gene3D G3DSA:3.40.50.720 -
11 101 Pfam PF01118 Semialdehyde dehydrogenase, NAD binding domain
11 101 InterPro IPR000534 Semialdehyde dehydrogenase, NAD-binding
1 127 SUPERFAMILY SSF51735 NAD(P)-binding Rossmann-fold domains
1 127 InterPro IPR036291 NAD(P)-binding domain superfamily
242 256 ProSitePatterns PS01103 Aspartate-semialdehyde dehydrogenase signature.
242 256 InterPro IPR000319 Aspartate-semialdehyde dehydrogenase, conserved site
124 335 Pfam PF02774 Semialdehyde dehydrogenase, dimerisation domain
124 335 InterPro IPR012280 Semialdehyde dehydrogenase, dimerisation 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

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Structural evidence

0 + 2

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

Entry Method Resolution Chain Coverage Links Status
AlphaFold AF_A0A0H3GTQ2
AlphaFold — — full sequence — Viewing
ColabFold VK055_0716
ColabFold — — 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 0.838
18 0.599
8 0.244

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 10.83 0.581
2 1.16 0.009
3 0.99 0.005
4 0.83 0.003
5 0.66 0.001

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.

55 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
4NO
4R5M
Q9KQG2 247.1 Da LogP 0.10 TPSA 138.0 ✓ Ro5 ✓ Clean c1cc(c(cc1[N+](=O)[O-])P(=O)(O)O)C(=O)O
CAC
1PQU
P44801 137.0 Da LogP -0.52 TPSA 40.1 ✓ Ro5 ✓ Clean C[As](=O)(C)[O-]
HSE
1PQP
P44801 119.1 Da LogP -1.22 TPSA 83.5 ✓ Ro5 ✓ Clean C(CO)[C@@H](C(=O)O)N
PEJ
1TB4
P44801 190.9 Da LogP -7.75 TPSA 92.2 ✓ Ro5 ✓ Clean [O-]I(=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.