Protein profile

KP13_03362

Aminotransferase

Genome: KpKP13

Gene: AHE45741.1 Structure source: AlphaFold + ColabFold UniProt A0A0H3GPY3
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Amino acids 386
Annotations 5
Features 11
PDB binders 8
Druggability 0.165

Overview

Basic information about this protein and its source genome.

Accession
KP13_03362
Assembly
Klebsiella pneumoniae subsp. pneumoniae Kp13, complete sequence
Gene
AHE45741.1
Status
annotated
Amino acids
386
Structure source
AlphaFold + ColabFold
GO
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: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. 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: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.

Target profile

Computed evidence for target prioritization.

Human off-target
hit
Human identity (%)
34.247
Human E-value
7.54e-35
Gut microbiome off-target
hit
Essential (DEG)
N
DEG identity (%)
0.0
Localization
Unknown
ColabFold pLDDT
97.22

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 0.165
Structure A0A0H3GPY3
Pocket Pocket 9
P2Rank 0.83
Structure A0A0H3GPY3
Pocket Pocket 1
ColabFold model
FPocket 0.598 · Pocket 1
P2Rank 0.836 · Pocket 1
Core conservation Conserved core gene
Roary core
CoreCruncher core
Gut microbiome 116 / 4744 genomes with a hit
Normalized 0.024

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:0030170 Binding to pyridoxal 5' phosphate, 3-hydroxy-5-(hydroxymethyl)-2-methyl4-pyridine carboxaldehyde 5' phosphate, the biologically active form of vitamin B6.
  • 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.
  • 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: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.

Sequence Features

Domain/signature hits from InterPro and related databases.

11 records
Show feature table
Start End DB Term Name
11 384 PANTHER PTHR43807 FI04487P
10 385 SUPERFAMILY SSF53383 PLP-dependent transferases
10 385 InterPro IPR015424 Pyridoxal phosphate-dependent transferase
45 284 Gene3D G3DSA:3.40.640.10 -
45 284 InterPro IPR015421 Pyridoxal phosphate-dependent transferase, major domain
62 283 FunFam G3DSA:3.40.640.10:FF:000033 Aspartate aminotransferase
22 383 Gene3D G3DSA:3.90.1150.10 Aspartate Aminotransferase, domain 1
22 383 InterPro IPR015422 Pyridoxal phosphate-dependent transferase, small domain
33 373 CDD cd00609 AAT_like
32 382 Pfam PF00155 Aminotransferase class I and II
32 382 InterPro IPR004839 Aminotransferase, class I/classII

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_A0A0H3GPY3
AlphaFold — — full sequence — Viewing
ColabFold KP13_03362
ColabFold — — full sequence — Loaded
Pocket details FPocket · P2Rank — toggle visibility and zoom from here, or open full viewer

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 14.44 0.723
2 1.7 0.03
3 1.36 0.016
4 1.31 0.014
5 0.78 0.002

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.