Protein profile

KP13_01226

50S ribosomal protein L9

Genome: KpKP13

Gene: AHE46708.1 rplI Structure source: AlphaFold + ColabFold UniProt A0A0H3GLI4
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Amino acids 149
Annotations 5
Features 22
PDB binders 3
Druggability 0.276

Overview

Basic information about this protein and its source genome.

Accession
KP13_01226
Assembly
Klebsiella pneumoniae subsp. pneumoniae Kp13, complete sequence
Gene
AHE46708.1 rplI
Status
annotated
Amino acids
149
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:1990904 A macromolecular complex that contains both RNA and protein molecules. GO:0019843 Binding to a ribosomal RNA.

Target profile

Computed evidence for target prioritization.

Human off-target
hit
Human identity (%)
43.137
Human E-value
3.11e-06
Gut microbiome off-target
hit
Essential (DEG)
Y
DEG identity (%)
93.289
DEG E-value
9.29e-98
Localization
Cytoplasmic
ColabFold pLDDT
88.48

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 0.276
Structure A0A0H3GLI4
Pocket Pocket 2
P2Rank
Structure A0A0H3GLI4
Pocket No pockets
ColabFold model
FPocket 0.248 · Pocket 1
Core conservation Conserved core gene
Roary core
CoreCruncher core
Gut microbiome 209 / 4744 genomes with a hit
Normalized 0.044

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

5 GO

Gene Ontology (GO)

5
  • 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: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.

22 records
Show feature table
Start End DB Term Name
1 149 Hamap MF_00503 50S ribosomal protein L9 [rplI].
1 149 InterPro IPR020594 Ribosomal protein L9, bacteria/chloroplast
44 64 Coils Coil Coil
1 149 NCBIfam TIGR00158 50S ribosomal protein L9
1 50 Gene3D G3DSA:3.40.5.10 -
1 50 InterPro IPR036935 Ribosomal protein L9, N-terminal domain superfamily
60 149 SUPERFAMILY SSF55653 Ribosomal protein L9 C-domain
60 149 InterPro IPR036791 Ribosomal protein L9, C-terminal domain superfamily
13 40 ProSitePatterns PS00651 Ribosomal protein L9 signature.
13 40 InterPro IPR020070 Ribosomal protein L9, N-terminal
61 149 Gene3D G3DSA:3.10.430.100 -
61 149 InterPro IPR036791 Ribosomal protein L9, C-terminal domain superfamily
64 148 Pfam PF03948 Ribosomal protein L9, C-terminal domain
64 148 InterPro IPR020069 Ribosomal protein L9, C-terminal
1 57 SUPERFAMILY SSF55658 L9 N-domain-like
1 57 InterPro IPR009027 Ribosomal protein L9/RNase H1, N-terminal
1 45 Pfam PF01281 Ribosomal protein L9, N-terminal domain
1 45 InterPro IPR020070 Ribosomal protein L9, N-terminal
1 147 PANTHER PTHR21368 50S RIBOSOMAL PROTEIN L9
1 147 InterPro IPR000244 Ribosomal protein L9
1 50 FunFam G3DSA:3.40.5.10:FF:000001 50S ribosomal protein L9
61 149 FunFam G3DSA:3.10.430.100:FF:000001 50S ribosomal protein L9

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_A0A0H3GLI4
AlphaFold — — full sequence — Viewing
ColabFold KP13_01226
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 0.276

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
5MU
5J4C
Q5SLQ1 338.2 Da LogP -2.43 TPSA 171.3 ✓ Ro5 ✓ Clean CC1=CN(C(=O)NC1=O)[C@H]2[C@@H]([C@@H]([C@H](O2)…
A
5J4C
Q5SLQ1 347.2 Da LogP -1.86 TPSA 186.1 ✓ Ro5 ✓ Clean c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)…
PSU
5J4C
Q5SLQ1 324.2 Da LogP -2.67 TPSA 182.2 1 viol. ✓ Clean C1=C(C(=O)NC(=O)N1)[C@H]2[C@@H]([C@@H]([C@H](O2…

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.