Protein profile

KP13_16520

Alanyl-tRNA synthetase

Genome: KpKP13

Gene: alaS ANJ86586.1 Structure source: AlphaFold + ColabFold UniProt A0A0H3GUA1
Export view
Amino acids 875
Annotations 14
Features 48
PDB binders 7
Druggability 0.183

Overview

Basic information about this protein and its source genome.

Accession
KP13_16520
Assembly
Klebsiella pneumoniae subsp. pneumoniae Kp13, complete sequence
Gene
alaS ANJ86586.1
Status
annotated
Amino acids
875
Structure source
AlphaFold + ColabFold
EC
6.1.1.7
GO
GO:0006419 The process of coupling alanine to alanyl-tRNA, catalyzed by alanyl-tRNA synthetase. The alanyl-tRNA synthetase is a class-II synthetases. The activated amino acid is transferred to the 3'-OH group of an alanine accetping tRNA. GO:0004812 Catalysis of the formation of aminoacyl-tRNA from ATP, amino acid, and tRNA with the release of diphosphate and AMP. GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. GO:0003676 Binding to a nucleic acid. GO:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. GO:0043039 The chemical reactions and pathways by which the various amino acids become bonded to their corresponding tRNAs. The most common route for synthesis of aminoacyl tRNA is by the formation of an ester bond between the 3'-hydroxyl group of the most 3' adenosine of the tRNA and the alpha carboxylic acid group of an amino acid, usually catalyzed by the cognate aminoacyl-tRNA ligase. A given aminoacyl-tRNA ligase aminoacylates all species of an isoaccepting group of tRNA molecules.

Target profile

Computed evidence for target prioritization.

Human off-target
hit
Human identity (%)
58.14
Human E-value
1.88e-10
Gut microbiome off-target
hit
Essential (DEG)
Y
DEG identity (%)
91.2
DEG E-value
0.0
Localization
Cytoplasmic
ColabFold pLDDT
90.34

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 0.183
Structure A0A0H3GUA1
Pocket Pocket 1
P2Rank 0.936
Structure A0A0H3GUA1
Pocket Pocket 1
ColabFold model
FPocket 0.71 · Pocket 1
P2Rank 0.935 · Pocket 1
Core conservation Conserved core gene
Roary core
CoreCruncher core
Gut microbiome 316 / 4744 genomes with a hit
Normalized 0.067

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 13 GO

Enzyme Commission (EC)

1

Gene Ontology (GO)

13
  • GO:0006419 The process of coupling alanine to alanyl-tRNA, catalyzed by alanyl-tRNA synthetase. The alanyl-tRNA synthetase is a class-II synthetases. The activated amino acid is transferred to the 3'-OH group of an alanine accetping tRNA.
  • GO:0004812 Catalysis of the formation of aminoacyl-tRNA from ATP, amino acid, and tRNA with the release of diphosphate and AMP.
  • GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
  • GO:0003676 Binding to a nucleic acid.
  • GO:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
  • GO:0043039 The chemical reactions and pathways by which the various amino acids become bonded to their corresponding tRNAs. The most common route for synthesis of aminoacyl tRNA is by the formation of an ester bond between the 3'-hydroxyl group of the most 3' adenosine of the tRNA and the alpha carboxylic acid group of an amino acid, usually catalyzed by the cognate aminoacyl-tRNA ligase. A given aminoacyl-tRNA ligase aminoacylates all species of an isoaccepting group of tRNA molecules.
  • GO:0004813 Catalysis of the reaction: ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl-tRNA(Ala).
  • GO:0000166 Binding to a nucleotide, any compound consisting of a nucleoside that is esterified with (ortho)phosphate or an oligophosphate at any hydroxyl group on the ribose or deoxyribose.
  • GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
  • GO:0002161 The hydrolysis of an incorrectly aminoacylated tRNA.
  • GO:0000049 Binding to a transfer RNA.
  • GO:0008270 Binding to a zinc ion (Zn).
  • GO:0045892 Any process that stops, prevents, or reduces the frequency, rate or extent of cellular DNA-templated transcription.

Sequence Features

Domain/signature hits from InterPro and related databases.

48 records
Show feature table
Start End DB Term Name
2 252 Gene3D G3DSA:3.30.930.10 Bira Bifunctional Protein; Domain 2
2 252 InterPro IPR045864 Class II Aminoacyl-tRNA synthetase/Biotinyl protein ligase (BPL) and lipoyl protein ligase (LPL)
1 875 Hamap MF_00036_B Alanine--tRNA ligase [alaS].
1 875 InterPro IPR023033 Alanine-tRNA ligase, eukaryota/bacteria
5 251 CDD cd00673 AlaRS_core
462 552 Gene3D G3DSA:2.40.30.130 -
346 366 Coils Coil Coil
563 698 Gene3D G3DSA:3.30.980.10 -
2 252 FunFam G3DSA:3.30.930.10:FF:000004 Alanine--tRNA ligase
732 766 Coils Coil Coil
763 873 Gene3D G3DSA:3.10.310.40 -
368 388 Coils Coil Coil
764 871 FunFam G3DSA:3.10.310.40:FF:000001 Alanine--tRNA ligase
452 552 FunFam G3DSA:2.40.30.130:FF:000001 Alanine--tRNA ligase
7 854 NCBIfam TIGR00344 alanine--tRNA ligase
7 854 InterPro IPR002318 Alanine-tRNA ligase, class IIc
700 762 Gene3D G3DSA:6.10.250.550 -
552 708 SUPERFAMILY SSF55186 ThrRS/AlaRS common domain
552 708 InterPro IPR018163 Threonyl/alanyl tRNA synthetase, class II-like, putative editing domain superfamily
624 677 Gene3D G3DSA:3.30.54.20 -
733 871 Pfam PF02272 DHHA1 domain
733 871 InterPro IPR003156 DHHA1 domain
7 556 Pfam PF01411 tRNA synthetases class II (A)
7 556 InterPro IPR018164 Alanyl-tRNA synthetase, class IIc, N-terminal
4 255 SUPERFAMILY SSF55681 Class II aaRS and biotin synthetases
4 255 InterPro IPR045864 Class II Aminoacyl-tRNA synthetase/Biotinyl protein ligase (BPL) and lipoyl protein ligase (LPL)
653 696 Pfam PF07973 Threonyl and Alanyl tRNA synthetase second additional domain
653 696 InterPro IPR012947 Threonyl/alanyl tRNA synthetase, SAD
455 551 SUPERFAMILY SSF50447 Translation proteins
455 551 InterPro IPR009000 Translation protein, beta-barrel domain superfamily
553 711 FunFam G3DSA:3.30.980.10:FF:000004 Alanine--tRNA ligase, cytoplasmic
4 870 PANTHER PTHR11777 ALANYL-TRNA SYNTHETASE
306 319 PRINTS PR00980 Alanyl-tRNA synthetase signature
306 319 InterPro IPR002318 Alanine-tRNA ligase, class IIc
236 249 PRINTS PR00980 Alanyl-tRNA synthetase signature
236 249 InterPro IPR002318 Alanine-tRNA ligase, class IIc
76 87 PRINTS PR00980 Alanyl-tRNA synthetase signature
76 87 InterPro IPR002318 Alanine-tRNA ligase, class IIc
209 220 PRINTS PR00980 Alanyl-tRNA synthetase signature
209 220 InterPro IPR002318 Alanine-tRNA ligase, class IIc
282 298 PRINTS PR00980 Alanyl-tRNA synthetase signature
282 298 InterPro IPR002318 Alanine-tRNA ligase, class IIc
256 465 SUPERFAMILY SSF101353 Putative anticodon-binding domain of alanyl-tRNA synthetase (AlaRS)
256 465 InterPro IPR018162 Alanine-tRNA ligase, class IIc, anti-codon-binding domain superfamily
653 696 SMART SM00863 tRNA_SAD_4
624 677 FunFam G3DSA:3.30.54.20:FF:000001 Alanine--tRNA ligase
3 709 ProSiteProfiles PS50860 Alanyl-transfer RNA synthetases family profile.
3 709 InterPro IPR018165 Alanyl-tRNA synthetase, class IIc, core 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 + 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_A0A0H3GUA1
AlphaFold — — full sequence — Viewing
ColabFold KP13_16520
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 24.93 0.902
2 11.49 0.613
3 2.71 0.081
4 2.33 0.06
5 1.76 0.032

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.

57 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
5AL
3HXY
P00957 418.3 Da LogP -1.96 TPSA 218.2 1 viol. ✓ Clean C[C@@H](C(=O)O[P@](=O)(O)OC[C@@H]1[C@H]([C@H]([…
A5A
3HXZ
P00957 417.4 Da LogP -3.25 TPSA 217.8 1 viol. ✓ Clean C[C@@H](C(=O)NS(=O)(=O)OC[C@@H]1[C@H]([C@H]([C@…
ACP
3HXY
P00957 505.2 Da LogP -1.52 TPSA 269.9 3 viol. ✓ Clean c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)…
G5A
3HY0
P00957 403.4 Da LogP -3.64 TPSA 217.8 1 viol. ✓ Clean c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)…
HED
3HXY
P00957 154.3 Da LogP 0.35 TPSA 40.5 ✓ Ro5 ✓ Clean C(CSSCCO)O
MDN
3HXY
P00957 176.0 Da LogP -0.70 TPSA 115.1 ✓ Ro5 ✓ Clean C(P(=O)(O)O)P(=O)(O)O
SSA
3HXW
P00957 433.4 Da LogP -4.28 TPSA 238.0 2 viol. ✓ Clean c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)…

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.