Protein profile

KP13_05506

Glutamyl-tRNA(Gln) amidotransferase subunit A

Genome: KpKP13

Gene: gatA AHE44512.1 Structure source: AlphaFold + ColabFold UniProt A0A1V8B7W3
Amino acids 465
Annotations 4
Features 10
PDB binders 3
Druggability 0.8

Overview

Basic information about this protein and its source genome.

Accession
KP13_05506
Gene
gatA AHE44512.1
Status
annotated
Amino acids
465
Structure source
AlphaFold + ColabFold

Target profile

Computed evidence for target prioritization.

Human off-target
hit
Human identity (%)
38.71
Human E-value
3.29e-13
Gut microbiome off-target
hit
Essential (DEG)
N
DEG identity (%)
0.0
Localization
Cytoplasmic
ColabFold pLDDT
97.07

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 0.8
Structure A0A1V8B7W3
Pocket Pocket 7
P2Rank 0.221
Structure A0A1V8B7W3
Pocket Pocket 1
ColabFold model
FPocket 0.579 · Pocket 5
P2Rank 0.242 · Pocket 1
Core conservation Conserved core gene
Roary core
CoreCruncher core
Gut microbiome 52 / 4744 genomes with a hit
Normalized 0.011

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 3 GO

Enzyme Commission (EC)

1

Gene Ontology (GO)

3
  • 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:0016787 Catalysis of the hydrolysis of various bonds, e.g. C-O, C-N, C-C, phosphoric anhydride bonds, etc.
  • GO:0016874 Catalysis of the joining of two molecules, or two groups within a single molecule, using the energy from the hydrolysis of ATP, a similar triphosphate, or a pH gradient.

Sequence Features

Domain/signature hits from InterPro and related databases.

10 records
Show feature table
Start End DB Term Name
7 456 Gene3D G3DSA:3.90.1300.10 Amidase signature (AS) domain
7 456 InterPro IPR036928 Amidase signature (AS) superfamily
8 456 NCBIfam TIGR02715 AtzE family amidohydrolase
8 456 InterPro IPR014087 1-carboxybiuret hydrolase, AtzE subunit
1 453 SUPERFAMILY SSF75304 Amidase signature (AS) enzymes
1 453 InterPro IPR036928 Amidase signature (AS) superfamily
4 452 PANTHER PTHR11895 TRANSAMIDASE
4 452 InterPro IPR000120 Amidase
28 444 Pfam PF01425 Amidase
28 444 InterPro IPR023631 Amidase signature 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...

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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_A0A1V8B7W3
AlphaFold full sequence Viewing
ColabFold KP13_05506
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
7 0.8
8 0.425

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 3.39 0.121

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.

53 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
ACA P13398 131.2 Da LogP 0.59 TPSA 63.3 ✓ Ro5 ✓ Clean C(CCC(=O)O)CCN
GJY Q7XJJ7 344.5 Da LogP 7.38 TPSA 26.3 1 viol. ✓ Clean CC/C=C\C/C=C\C/C=C\CCCCCCCC[P@](=O)(OC)F
UNU Q7DKE4 121.1 Da LogP 0.79 TPSA 43.1 ✓ Ro5 ✓ Clean c1ccc(cc1)C(=O)N

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.