Protein profile

KP13_00760

50S ribosomal protein L24

Genome: KpKP13

Gene: AHE42375.1 rplX Structure source: AlphaFold + ColabFold UniProt A0A0H3GU18
Amino acids 104
Annotations 7
Features 20
PDB binders 4
Druggability 0.788

Overview

Basic information about this protein and its source genome.

Accession
KP13_00760
Gene
AHE42375.1 rplX
Status
annotated
Amino acids
104
Structure source
AlphaFold + ColabFold
GO
GO:0003723 Binding to an RNA molecule or a portion thereof. 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: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:0003735 The action of a molecule that contributes to the structural integrity of the ribosome. GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. GO:1990904 A macromolecular complex that contains both RNA and protein molecules.

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 (%)
100.0
DEG E-value
3.71e-70
Localization
Cytoplasmic
ColabFold pLDDT
91.25

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 0.788
Structure A0A0H3GU18
Pocket Pocket 2
P2Rank
Structure A0A0H3GU18
Pocket No pockets
ColabFold model
FPocket 0.701 · Pocket 2
Core conservation Conserved core gene
Roary core
CoreCruncher core
Gut microbiome 618 / 4744 genomes with a hit
Normalized 0.13

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

7 GO

Gene Ontology (GO)

7
  • GO:0003723 Binding to an RNA molecule or a portion thereof.
  • 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: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:0003735 The action of a molecule that contributes to the structural integrity of the ribosome.
  • GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
  • GO:1990904 A macromolecular complex that contains both RNA and protein molecules.
  • GO:0019843 Binding to a ribosomal RNA.

Sequence Features

Domain/signature hits from InterPro and related databases.

20 records
Show feature table
Start End DB Term Name
4 31 SMART SM00739 kow_9
4 31 InterPro IPR005824 KOW
4 100 SUPERFAMILY SSF50104 Translation proteins SH3-like domain
4 100 InterPro IPR008991 Translation protein SH3-like domain superfamily
8 25 ProSitePatterns PS01108 Ribosomal protein L24 signature.
8 25 InterPro IPR005825 Ribosomal protein L24/L26, conserved site
2 102 FunFam G3DSA:2.30.30.30:FF:000004 50S ribosomal protein L24
3 103 NCBIfam TIGR01079 50S ribosomal protein L24
3 103 InterPro IPR003256 Ribosomal protein L24
3 97 Hamap MF_01326_B 50S ribosomal protein L24 [rplX].
3 97 InterPro IPR003256 Ribosomal protein L24
2 104 Gene3D G3DSA:2.30.30.30 -
2 104 InterPro IPR014722 Ribosomal protein L2, domain 2
39 103 Pfam PF17136 Ribosomal proteins 50S L24/mitochondrial 39S L24
39 103 InterPro IPR003256 Ribosomal protein L24
8 36 Pfam PF00467 KOW motif
8 36 InterPro IPR005824 KOW
3 103 PANTHER PTHR12903 MITOCHONDRIAL RIBOSOMAL PROTEIN L24
8 72 CDD cd06089 KOW_RPL26
8 72 InterPro IPR041988 Ribosomal protein L26/L24, KOW 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

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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_A0A0H3GU18
AlphaFold full sequence Viewing
ColabFold KP13_00760
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
2 0.788

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.

54 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
NMY P60624 614.7 Da LogP -8.90 TPSA 353.1 3 viol. ✓ Clean C1[C@H]([C@@H]([C@H]([C@@H]([C@H]1N)O[C@@H]2[C@…
PAR P60624 615.6 Da LogP -8.86 TPSA 347.3 3 viol. ✓ Clean C1[C@H]([C@@H]([C@H]([C@@H]([C@H]1N)O[C@@H]2[C@…
PEV P60624 720.0 Da LogP 11.28 TPSA 134.4 2 viol. ✓ Clean CCCCCCCCCCCCCCCCCC(=O)O[C@@H](COC(=O)CCCCCCCCCC…
PGV P60624 749.0 Da LogP 10.45 TPSA 148.8 2 viol. ✓ Clean CCCCCCCCCCCCCCCC(=O)OC[C@H](CO[P@](=O)(O)OC[C@H…

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.