Protein profile

PA4932

50S ribosomal protein L9

Genome: NC_002516.2

Gene: PA4932 rplI Structure source: AlphaFold UniProt Q9HUN2
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Amino acids 148
Annotations 5
Features 21
PDB binders 3
Druggability 0.478

Overview

Basic information about this protein and its source genome.

Accession
PA4932
Assembly
Pseudomonas aeruginosa PAO1, complete genome
Gene
PA4932 rplI
Status
annotated
Amino acids
148
Structure source
AlphaFold
GO
GO:0022625 The large subunit of a ribosome located in the cytosol. GO:0019843 Binding to a ribosomal RNA. GO:0003735 The action of a molecule that contributes to the structural integrity of the ribosome. 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.

Target profile

Computed evidence for target prioritization.

Human off-target
hit
Human identity (%)
47.917
Human E-value
1.49e-06
Gut microbiome off-target
hit
Essential (DEG)
Y
Localization
Cytoplasmic

Selected Druggability evidence

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 0.478
Structure –
Pocket –

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:0022625 The large subunit of a ribosome located in the cytosol.
  • GO:0019843 Binding to a ribosomal RNA.
  • GO:0003735 The action of a molecule that contributes to the structural integrity of the ribosome.
  • 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.

Sequence Features

Domain/signature hits from InterPro and related databases.

21 records
Show feature table
Start End DB Term Name
44 75 Coils Coil Coil
1 50 Gene3D G3DSA:3.40.5.10 -
1 50 InterPro IPR036935 Ribosomal protein L9, N-terminal domain superfamily
1 148 Hamap MF_00503 50S ribosomal protein L9 [rplI].
1 148 InterPro IPR020594 Ribosomal protein L9, bacteria/chloroplast
1 148 NCBIfam TIGR00158 50S ribosomal protein L9
1 56 SUPERFAMILY SSF55658 L9 N-domain-like
1 56 InterPro IPR009027 Ribosomal protein L9/RNase H1, N-terminal
60 148 SUPERFAMILY SSF55653 Ribosomal protein L9 C-domain
60 148 InterPro IPR036791 Ribosomal protein L9, C-terminal domain superfamily
62 148 Gene3D G3DSA:3.10.430.100 -
62 148 InterPro IPR036791 Ribosomal protein L9, C-terminal domain superfamily
1 47 Pfam PF01281 Ribosomal protein L9, N-terminal domain
1 47 InterPro IPR020070 Ribosomal protein L9, N-terminal
64 147 Pfam PF03948 Ribosomal protein L9, C-terminal domain
64 147 InterPro IPR020069 Ribosomal protein L9, C-terminal
13 40 ProSitePatterns PS00651 Ribosomal protein L9 signature.
13 40 InterPro IPR020070 Ribosomal protein L9, N-terminal
1 50 FunFam G3DSA:3.40.5.10:FF:000001 50S ribosomal protein L9
1 147 PANTHER PTHR21368 50S RIBOSOMAL PROTEIN L9
1 147 InterPro IPR000244 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.

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Structural evidence

0 + 1

Experimental PDB entries and predicted models. Click Switch to display a different structure in the viewer.

Entry Method Resolution Chain Coverage Links Status
AlphaFold PA4932
AlphaFold — — full sequence — Viewing
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 0.478
2 0.271
5 0.218

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.