Protein profile

KP13_00768

50S ribosomal protein L15

Genome: KpKP13

Gene: rplO AHE42382.1 Structure source: AlphaFold + ColabFold UniProt A0A0H3GYA6
Amino acids 144
Annotations 6
Features 15
PDB binders 6
Druggability 0.304

Overview

Basic information about this protein and its source genome.

Accession
KP13_00768
Gene
rplO AHE42382.1
Status
annotated
Amino acids
144
Structure source
AlphaFold + ColabFold
GO
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:0015934 The larger of the two subunits of a ribosome. Two sites on the ribosomal large subunit are involved in translation, namely the aminoacyl site (A site) and peptidyl site (P site). 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:0022625 The large subunit of a ribosome located in the cytosol. GO:0019843 Binding to a ribosomal RNA.

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 (%)
95.139
DEG E-value
5.84e-93
Localization
Cytoplasmic
ColabFold pLDDT
86.57

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 0.304
Structure A0A0H3GYA6
Pocket Pocket 1
P2Rank
Structure A0A0H3GYA6
Pocket No pockets
ColabFold model
FPocket 0.493 · Pocket 3
Core conservation Conserved core gene
Roary core
CoreCruncher core
Gut microbiome 425 / 4744 genomes with a hit
Normalized 0.09

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

6 GO

Gene Ontology (GO)

6
  • 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:0015934 The larger of the two subunits of a ribosome. Two sites on the ribosomal large subunit are involved in translation, namely the aminoacyl site (A site) and peptidyl site (P site).
  • 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:0022625 The large subunit of a ribosome located in the cytosol.
  • GO:0019843 Binding to a ribosomal RNA.

Sequence Features

Domain/signature hits from InterPro and related databases.

15 records
Show feature table
Start End DB Term Name
2 143 NCBIfam TIGR01071 50S ribosomal protein L15
2 143 InterPro IPR005749 Ribosomal protein L15, bacterial-type
109 139 ProSitePatterns PS00475 Ribosomal protein L15 signature.
109 139 InterPro IPR001196 Ribosomal protein L15, conserved site
28 143 Pfam PF00828 Ribosomal proteins 50S-L15, 50S-L18e, 60S-L27A
28 143 InterPro IPR021131 Ribosomal protein L18e/L15P
4 143 SUPERFAMILY SSF52080 Ribosomal proteins L15p and L18e
4 143 InterPro IPR036227 Ribosomal L18e/L15P superfamily
1 54 MobiDBLite mobidb-lite consensus disorder prediction
75 144 FunFam G3DSA:3.100.10.10:FF:000003 50S ribosomal protein L15
3 144 Hamap MF_01341 50S ribosomal protein L15 [rplO].
3 144 InterPro IPR030878 Ribosomal protein L15
75 144 Gene3D G3DSA:3.100.10.10 -
1 142 PANTHER PTHR12934 50S RIBOSOMAL PROTEIN L15
1 142 InterPro IPR005749 Ribosomal protein L15, bacterial-type

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_A0A0H3GYA6
AlphaFold full sequence Viewing
ColabFold KP13_00768
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
1 0.304

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.

56 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
4D4 P02413 190.2 Da LogP -2.37 TPSA 145.4 1 viol. ✓ Clean [H]/N=C(/N)\NCC[C@H]([C@@H](C(=O)O)N)O
GUN P02413 151.1 Da LogP -0.77 TPSA 100.5 ✓ Ro5 ✓ Clean c1[nH]c2c(n1)C(=O)NC(=N2)N
MEQ P02413 160.2 Da LogP -1.08 TPSA 92.4 ✓ Ro5 ✓ Clean CNC(=O)CC[C@@H](C(=O)O)N
OHX Q5SHQ7 286.4 Da LogP -3.55 TPSA 156.1 1 viol. ✓ Clean N[Os](N)(N)(N)(N)N
PUT P02413 88.2 Da LogP -0.32 TPSA 52.0 ✓ Ro5 ✓ Clean C(CCN)CN
TAC P02413 444.4 Da LogP -0.21 TPSA 181.6 1 viol. ✓ Clean C[C@]1(c2cccc(c2C(=O)C3=C([C@]4([C@@H](C[C@@H]3…

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.