Protein profile

PA3798

aminotransferase

Genome: NC_002516.2

Gene: PA3798 Structure source: AlphaFold UniProt Q9HXJ9
Export view
Amino acids 382
Annotations 5
Features 11
PDB binders 8
Druggability 0.862

Overview

Basic information about this protein and its source genome.

Accession
PA3798
Assembly
Pseudomonas aeruginosa PAO1, complete genome
Gene
PA3798
Status
annotated
Amino acids
382
Structure source
AlphaFold
GO
GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. GO:0016212 Catalysis of the reaction: 2-oxoglutarate + L-kynurenine = H2O + kynurenate + L-glutamate. The product 4-(2-aminophenyl)-2,4-dioxobutanoate is converted into kynurenate by a spontaneous reaction. Also acts on 3-hydroxykynurenine to form xanthurenate. GO:0030170 Binding to pyridoxal 5' phosphate, 3-hydroxy-5-(hydroxymethyl)-2-methyl4-pyridine carboxaldehyde 5' phosphate, the biologically active form of vitamin B6. GO:0003824 Catalysis of a biochemical reaction at physiological temperatures. In biologically catalyzed reactions, the reactants are known as substrates, and the catalysts are naturally occurring macromolecular substances known as enzymes. Enzymes possess specific binding sites for substrates, and are usually composed wholly or largely of protein, but RNA that has catalytic activity (ribozyme) is often also regarded as enzymatic. GO:0009058 A cellular process consisting of the biochemical pathways by which a living organism synthesizes chemical substances. This typically represents the energy-requiring part of metabolism in which simpler substances are transformed into more complex ones.

Target profile

Computed evidence for target prioritization.

Human off-target
hit
Human identity (%)
35.455
Human E-value
2.07e-42
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 0.862
Structure –
Pocket –

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

5 GO

Gene Ontology (GO)

5
  • GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
  • GO:0016212 Catalysis of the reaction: 2-oxoglutarate + L-kynurenine = H2O + kynurenate + L-glutamate. The product 4-(2-aminophenyl)-2,4-dioxobutanoate is converted into kynurenate by a spontaneous reaction. Also acts on 3-hydroxykynurenine to form xanthurenate.
  • GO:0030170 Binding to pyridoxal 5' phosphate, 3-hydroxy-5-(hydroxymethyl)-2-methyl4-pyridine carboxaldehyde 5' phosphate, the biologically active form of vitamin B6.
  • GO:0003824 Catalysis of a biochemical reaction at physiological temperatures. In biologically catalyzed reactions, the reactants are known as substrates, and the catalysts are naturally occurring macromolecular substances known as enzymes. Enzymes possess specific binding sites for substrates, and are usually composed wholly or largely of protein, but RNA that has catalytic activity (ribozyme) is often also regarded as enzymatic.
  • GO:0009058 A cellular process consisting of the biochemical pathways by which a living organism synthesizes chemical substances. This typically represents the energy-requiring part of metabolism in which simpler substances are transformed into more complex ones.

Sequence Features

Domain/signature hits from InterPro and related databases.

11 records
Show feature table
Start End DB Term Name
4 379 PANTHER PTHR43807 FI04487P
56 277 FunFam G3DSA:3.40.640.10:FF:000033 Aspartate aminotransferase
2 381 SUPERFAMILY SSF53383 PLP-dependent transferases
2 381 InterPro IPR015424 Pyridoxal phosphate-dependent transferase
27 379 Pfam PF00155 Aminotransferase class I and II
27 379 InterPro IPR004839 Aminotransferase, class I/classII
27 379 CDD cd00609 AAT_like
39 278 Gene3D G3DSA:3.40.640.10 -
39 278 InterPro IPR015421 Pyridoxal phosphate-dependent transferase, major domain
16 379 Gene3D G3DSA:3.90.1150.10 Aspartate Aminotransferase, domain 1
16 379 InterPro IPR015422 Pyridoxal phosphate-dependent transferase, small 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 PA3798
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 0.501
7 0.23

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.

61 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
C6P
2R5C
Q17CS8 352.3 Da LogP 0.18 TPSA 149.2 1 viol. ✓ Clean Cc1c(c(c(cn1)COP(=O)(O)O)CN[C@@H](CS)C(=O)O)O
HCI
1V2F
Q75WK2 150.2 Da LogP 1.70 TPSA 37.3 ✓ Ro5 ✓ Clean c1ccc(cc1)CCC(=O)O
IAC
3FVU
Q16773 175.2 Da LogP 1.79 TPSA 53.1 ✓ Ro5 ✓ Clean c1ccc2c(c1)c(c[nH]2)CC(=O)O
IK2
4WLJ
Q16773 322.2 Da LogP -0.19 TPSA 158.4 ✓ Ro5 ✓ Clean Cc1c(c(c(cn1)COP(=O)(O)O)CNOCC(=O)O)O
KMT
1V2E
Q75WK2 148.2 Da LogP 0.39 TPSA 54.4 ✓ Ro5 ✓ Clean CSCCC(=O)C(=O)O
KYN
3E2Z
Q71RI9 208.2 Da LogP 0.25 TPSA 106.4 ✓ Ro5 ✓ Clean c1ccc(c(c1)C(=O)C[C@@H](C(=O)O)N)N
PMP
3E2Y
Q71RI9 248.2 Da LogP 0.16 TPSA 125.9 ✓ Ro5 ✓ Clean Cc1c(c(c(cn1)COP(=O)(O)O)CN)O
QLP
2R5E
Q17CS8 377.3 Da LogP -0.49 TPSA 192.3 1 viol. ✓ Clean Cc1c(c(c(cn1)COP(=O)(O)O)CN[C@@H](CCC(=O)N)C(=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.