Protein profile

KP13_10184

30S ribosomal protein S8

Genome: KpKP13

Gene: ANJ86574.1 rpsH Structure source: AlphaFold + ColabFold UniProt A0A0H3GYB0
Amino acids 130
Annotations 6
Features 14
PDB binders 6
Druggability 0.267

Overview

Basic information about this protein and its source genome.

Accession
KP13_10184
Gene
ANJ86574.1 rpsH
Status
annotated
Amino acids
130
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:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. 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
No hit
Human identity (%)
0.0
Gut microbiome off-target
hit
Essential (DEG)
Y
DEG identity (%)
99.231
DEG E-value
1.56e-92
Localization
Cytoplasmic
ColabFold pLDDT
91.81

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 0.267
Structure A0A0H3GYB0
Pocket Pocket 8
P2Rank
Structure A0A0H3GYB0
Pocket No pockets
ColabFold model
FPocket 0.327 · Pocket 6
Core conservation Conserved core gene
Roary core
CoreCruncher core
Gut microbiome 2363 / 4744 genomes with a hit
Normalized 0.498

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: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:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
  • 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.

14 records
Show feature table
Start End DB Term Name
100 117 ProSitePatterns PS00053 Ribosomal protein S8 signature.
100 117 InterPro IPR000630 Ribosomal protein S8
73 130 FunFam G3DSA:3.30.1490.10:FF:000001 30S ribosomal protein S8
5 129 SUPERFAMILY SSF56047 Ribosomal protein S8
5 129 InterPro IPR035987 Ribosomal protein S8 superfamily
2 72 FunFam G3DSA:3.30.1370.30:FF:000003 30S ribosomal protein S8
2 130 Hamap MF_01302_B 30S ribosomal protein S8 [rpsH].
2 130 InterPro IPR000630 Ribosomal protein S8
1 129 PANTHER PTHR11758 40S RIBOSOMAL PROTEIN S15A
1 129 InterPro IPR000630 Ribosomal protein S8
2 72 Gene3D G3DSA:3.30.1370.30 -
73 130 Gene3D G3DSA:3.30.1490.10 -
5 129 Pfam PF00410 Ribosomal protein S8
5 129 InterPro IPR000630 Ribosomal protein S8

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_A0A0H3GYB0
AlphaFold full sequence Viewing
ColabFold KP13_10184
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
8 0.267
7 0.22

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
NMY P0DOY9 614.7 Da LogP -8.90 TPSA 353.1 3 viol. ✓ Clean C1[C@H]([C@@H]([C@H]([C@@H]([C@H]1N)O[C@@H]2[C@…
OHX P0DOY9 286.4 Da LogP -3.55 TPSA 156.1 1 viol. ✓ Clean N[Os](N)(N)(N)(N)N
PAR P0DOY9 615.6 Da LogP -8.86 TPSA 347.3 3 viol. ✓ Clean C1[C@H]([C@@H]([C@H]([C@@H]([C@H]1N)O[C@@H]2[C@…
PCY P0DOY9 558.6 Da LogP 0.75 TPSA 194.7 2 viol. ✓ Clean Cc1cccc(c1C(=O)OC[C@]2([C@H]([C@@H]([C@]([C@@]2…
TAC P0DOY9 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…
WO2 P0DOY9 [O][W]1234O[W]567(O[W]89%10(O5[P]5%11O%12[W]%13…

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.