Overview
Basic information about this protein and its source genome.
- Accession
- KP13_07875
- Gene
- ANJ86563.1 rpmB
- Status
- annotated
- Amino acids
- 78
- Structure source
- AlphaFold + ColabFold
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
- 1.9499999999999998e-54
- Localization
- Cytoplasmic
- ColabFold pLDDT
- 92.34
Selected Druggability evidence
AlphaFold / UniProt modelSelected 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.
Functional Annotations
Enzyme classification and Gene Ontology terms linked to this protein.
Gene Ontology (GO)
3- 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.
Sequence Features
Domain/signature hits from InterPro and related databases.
Show feature table
| Start | End | DB | Term | Name |
|---|---|---|---|---|
| 3 | 62 | Pfam | PF00830 | Ribosomal L28 family |
| 3 | 62 | InterPro | IPR026569 | Ribosomal protein L28/L24 |
| 2 | 78 | Gene3D | G3DSA:2.30.170.40 | Ribosomal protein L28/L24 |
| 2 | 78 | InterPro | IPR037147 | Ribosomal protein L28/L24 superfamily |
| 1 | 57 | NCBIfam | TIGR00009 | 50S ribosomal protein L28 |
| 1 | 57 | InterPro | IPR001383 | Ribosomal protein L28 |
| 1 | 67 | Hamap | MF_00373 | 50S ribosomal protein L28 [rpmB]. |
| 1 | 67 | InterPro | IPR001383 | Ribosomal protein L28 |
| 2 | 77 | SUPERFAMILY | SSF143800 | L28p-like |
| 2 | 77 | InterPro | IPR034704 | L28p-like |
| 2 | 78 | FunFam | G3DSA:2.30.170.40:FF:000001 | 50S ribosomal protein L28 |
| 1 | 70 | PANTHER | PTHR13528 | 39S RIBOSOMAL PROTEIN L28, MITOCHONDRIAL |
| 1 | 70 | InterPro | IPR026569 | Ribosomal protein L28/L24 |
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 + 2Experimental PDB entries and predicted models. Click Switch to display a different structure in the viewer.
| Entry | Method | Resolution | Chain | Coverage | Links | Status |
|---|---|---|---|---|---|---|
|
AlphaFold
AF_A6TFM8
|
AlphaFold | — | — | full sequence | — | Viewing |
|
ColabFold
KP13_07875
|
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 | 0.723 | ||||||
| 4 | 0.331 |
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 | 0.551 | ||||||
| 2 | 0.478 |
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.
No PDB ligands found through similar proteins.
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).
| Ligand | UniProt (homolog) | pchembl | MW · LogP · TPSA | Lipinski | PAINS | SMILES |
|---|---|---|---|---|---|---|
| FCN | P0A7M2 | — | 138.1 Da LogP -0.09 TPSA 70.1 | ✓ Ro5 | ✓ Clean |
C[C@H]1[C@H](O1)P(=O)(O)O
|
| FOM | P0A7M2 | — | 183.1 Da LogP -0.60 TPSA 98.1 | ✓ Ro5 | ✓ Clean |
C(CN(C=O)O)CP(=O)(O)O
|
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.