Protein profile

KP13_02422

50S ribosomal protein L19

Genome: KpKP13

Gene: AHE43142.1 rplS Structure source: AlphaFold + ColabFold UniProt A0A0H3GWE5
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Amino acids 115
Annotations 4
Features 22
PDB binders 1
Druggability 0.72

Overview

Basic information about this protein and its source genome.

Accession
KP13_02422
Assembly
Klebsiella pneumoniae subsp. pneumoniae Kp13, complete sequence
Gene
AHE43142.1 rplS
Status
annotated
Amino acids
115
Structure source
AlphaFold + ColabFold
GO
GO:0003735 The action of a molecule that contributes to the structural integrity of the ribosome. GO:0005840 An intracellular organelle, about 200 A in diameter, consisting of RNA and protein. It is the site of protein biosynthesis resulting from translation of messenger RNA (mRNA). It consists of two subunits, one large and one small, each containing only protein and RNA. Both the ribosome and its subunits are characterized by their sedimentation coefficients, expressed in Svedberg units (symbol: S). Hence, the prokaryotic ribosome (70S) comprises a large (50S) subunit and a small (30S) subunit, while the eukaryotic ribosome (80S) comprises a large (60S) subunit and a small (40S) subunit. Two sites on the ribosomal large subunit are involved in translation, namely the aminoacyl site (A site) and peptidyl site (P site). Ribosomes from prokaryotes, eukaryotes, mitochondria, and chloroplasts have characteristically distinct ribosomal proteins. GO:0006412 The cellular metabolic process in which a protein is formed, using the sequence of a mature mRNA or circRNA molecule to specify the sequence of amino acids in a polypeptide chain. Translation is mediated by the ribosome, and begins with the formation of a ternary complex between aminoacylated initiator methionine tRNA, GTP, and initiation factor 2, which subsequently associates with the small subunit of the ribosome and an mRNA or circRNA. Translation ends with the release of a polypeptide chain from the ribosome. GO:0022625 The large subunit of a ribosome located in the cytosol.

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 (%)
98.261
DEG E-value
2.77e-80
Localization
Cytoplasmic
ColabFold pLDDT
92.43

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 0.72
Structure A0A0H3GWE5
Pocket Pocket 3
P2Rank 0.036
Structure A0A0H3GWE5
Pocket Pocket 1
ColabFold model
FPocket 0.552 · Pocket 2
P2Rank 0.014 · Pocket 1
Core conservation Conserved core gene
Roary core
CoreCruncher core
Gut microbiome 2399 / 4744 genomes with a hit
Normalized 0.506

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

4 GO

Gene Ontology (GO)

4
  • GO:0003735 The action of a molecule that contributes to the structural integrity of the ribosome.
  • GO:0005840 An intracellular organelle, about 200 A in diameter, consisting of RNA and protein. It is the site of protein biosynthesis resulting from translation of messenger RNA (mRNA). It consists of two subunits, one large and one small, each containing only protein and RNA. Both the ribosome and its subunits are characterized by their sedimentation coefficients, expressed in Svedberg units (symbol: S). Hence, the prokaryotic ribosome (70S) comprises a large (50S) subunit and a small (30S) subunit, while the eukaryotic ribosome (80S) comprises a large (60S) subunit and a small (40S) subunit. Two sites on the ribosomal large subunit are involved in translation, namely the aminoacyl site (A site) and peptidyl site (P site). Ribosomes from prokaryotes, eukaryotes, mitochondria, and chloroplasts have characteristically distinct ribosomal proteins.
  • GO:0006412 The cellular metabolic process in which a protein is formed, using the sequence of a mature mRNA or circRNA molecule to specify the sequence of amino acids in a polypeptide chain. Translation is mediated by the ribosome, and begins with the formation of a ternary complex between aminoacylated initiator methionine tRNA, GTP, and initiation factor 2, which subsequently associates with the small subunit of the ribosome and an mRNA or circRNA. Translation ends with the release of a polypeptide chain from the ribosome.
  • GO:0022625 The large subunit of a ribosome located in the cytosol.

Sequence Features

Domain/signature hits from InterPro and related databases.

22 records
Show feature table
Start End DB Term Name
2 114 Hamap MF_00402 50S ribosomal protein L19 [rplS].
2 114 InterPro IPR001857 Ribosomal protein L19
1 115 Gene3D G3DSA:2.30.30.790 -
1 115 InterPro IPR038657 Ribosomal protein L19 superfamily
1 115 FunFam G3DSA:2.30.30.790:FF:000001 50S ribosomal protein L19
3 113 Pfam PF01245 Ribosomal protein L19
3 113 InterPro IPR001857 Ribosomal protein L19
1 115 PIRSF PIRSF002191 Ribosomal_L19
1 115 InterPro IPR001857 Ribosomal protein L19
86 101 ProSitePatterns PS01015 Ribosomal protein L19 signature.
86 101 InterPro IPR018257 Ribosomal protein L19, conserved site
34 63 PRINTS PR00061 Ribosomal protein L19 signature
34 63 InterPro IPR001857 Ribosomal protein L19
88 113 PRINTS PR00061 Ribosomal protein L19 signature
88 113 InterPro IPR001857 Ribosomal protein L19
4 33 PRINTS PR00061 Ribosomal protein L19 signature
4 33 InterPro IPR001857 Ribosomal protein L19
3 113 NCBIfam TIGR01024 50S ribosomal protein L19
2 114 SUPERFAMILY SSF50104 Translation proteins SH3-like domain
2 114 InterPro IPR008991 Translation protein SH3-like domain superfamily
3 112 PANTHER PTHR15680 RIBOSOMAL PROTEIN L19
3 112 InterPro IPR001857 Ribosomal protein L19

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_A0A0H3GWE5
AlphaFold — — full sequence — Viewing
ColabFold KP13_02422
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
3 0.72

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 1.18 0.01

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.

1 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
OHX
4V8E
P60490 286.4 Da LogP -3.55 TPSA 156.1 1 viol. ✓ Clean N[Os](N)(N)(N)(N)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.