Overview
Basic information about this protein and its source genome.
- Accession
- PA4251
- Gene
- rplE PA4251
- Status
- annotated
- Amino acids
- 179
- Structure source
- AlphaFold
Target profile
Computed evidence for target prioritization.
- Human off-target
- hit
- Human identity (%)
- 34.351
- Human E-value
- 9.95e-13
- 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.
Sequence
Primary amino-acid sequence viewer.
MARLKEIYRKEIAPKLKEELQLANVMEVPRVTKITLNMGLGEAVGDKKIIENAVADLEKITGQKPVVTYARKSIAGFKIREGWPIGVKVTLRSDRMYEFLDRLLSISLPRVRDFRGLNAKSFDGRGNYSMGVKEQIIFPEIDYDKIDALRGLDITLTTTARTDDEGRALLRAFKFPFRN
Functional Annotations
Enzyme classification and Gene Ontology terms linked to this protein.
Gene Ontology (GO)
7- GO:0022625 The large subunit of a ribosome located in the cytosol.
- GO:0003723 Binding to an RNA molecule or a portion thereof.
- GO:0019843 Binding to a ribosomal RNA.
- GO:0003735 The action of a molecule that contributes to the structural integrity of the ribosome.
- GO:0000049 Binding to a transfer RNA.
- 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.
Show feature table
| Start | End | DB | Term | Name |
|---|---|---|---|---|
| 1 | 179 | Hamap | MF_01333_B | 50S ribosomal protein L5 [rplE]. |
| 1 | 179 | InterPro | IPR020930 | Ribosomal protein L5, bacterial-type |
| 1 | 179 | Gene3D | G3DSA:3.30.1440.10 | - |
| 1 | 179 | InterPro | IPR022803 | Ribosomal protein L5 domain superfamily |
| 24 | 80 | Pfam | PF00281 | Ribosomal protein L5 |
| 24 | 80 | InterPro | IPR031310 | Ribosomal protein L5, N-terminal |
| 1 | 179 | FunFam | G3DSA:3.30.1440.10:FF:000001 | 50S ribosomal protein L5 |
| 12 | 178 | PANTHER | PTHR11994 | 60S RIBOSOMAL PROTEIN L11-RELATED |
| 12 | 178 | InterPro | IPR002132 | Ribosomal protein L5 |
| 3 | 179 | SUPERFAMILY | SSF55282 | RL5-like |
| 3 | 179 | InterPro | IPR022803 | Ribosomal protein L5 domain superfamily |
| 1 | 179 | PIRSF | PIRSF002161 | RPL5p_RPL5a_RPL11e_RPL5o |
| 1 | 179 | InterPro | IPR002132 | Ribosomal protein L5 |
| 57 | 73 | ProSitePatterns | PS00358 | Ribosomal protein L5 signature. |
| 57 | 73 | InterPro | IPR020929 | Ribosomal protein L5, conserved site |
| 84 | 177 | Pfam | PF00673 | ribosomal L5P family C-terminus |
| 84 | 177 | InterPro | IPR031309 | Ribosomal protein L5, C-terminal |
3D Structure
Selected loaded structure. Experimental PDB entries may cover only a portion of the sequence; predicted models typically cover the full protein.
Loading 3D structure...
Structural evidence
0 + 1Experimental PDB entries and predicted models. Click Switch to display a different structure in the viewer.
| Entry | Method | Resolution | Chain | Coverage | Links | Status |
|---|---|---|---|---|---|---|
|
AlphaFold
PA4251
|
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 | 0.739 | ||||||
| 3 | 0.428 |
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.
Highest-confidence structural evidence: ligands co-crystallized with this exact protein. If the source PDB is loaded in TPW, use Open crystal to inspect it in the structure viewer.
No PDB structure with a co-crystallized ligand found for this exact protein.
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.
| Ligand | Source crystal | UniProt (homolog) | MW · LogP · TPSA | Lipinski | PAINS | SMILES |
|---|---|---|---|---|---|---|
| OHX | Q3E757 | 286.4 Da LogP -3.55 TPSA 156.1 | 1 viol. | ✓ Clean |
N[Os](N)(N)(N)(N)N
|
Experimental bioactivity from ChEMBL measured directly on this protein. Score = pchembl (−log Ki/IC₅₀; higher = more potent).
No ChEMBL bioactivity data found for this exact protein.
Bioactivity inferred from similar proteins in ChEMBL. Score = pchembl (−log Ki/IC₅₀; higher = more potent).
No ChEMBL hits found through similar proteins.
Proposed virtual-screening candidates from ZINC. Score = Tanimoto similarity to a known binder (0–1; higher = more similar).
No virtual-screening candidates for this protein.
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.