Protein profile

PA3656

30S ribosomal protein S2

Genome: NC_002516.2

Gene: PA3656 rpsB Structure source: AlphaFold UniProt O82850
Amino acids 246
Annotations 5
Features 31
PDB binders 2
Druggability 0.356

Overview

Basic information about this protein and its source genome.

Accession
PA3656
Gene
PA3656 rpsB
Status
annotated
Amino acids
246
Structure source
AlphaFold
GO
GO:0022627 The small subunit of a ribosome located in the cytosol. 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:0015935 The smaller of the two subunits of a 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 (%)
29.596
Human E-value
1.7000000000000002e-22
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 0.356
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:0022627 The small subunit of a ribosome located in the cytosol.
  • 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:0015935 The smaller of the two subunits of a 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.

31 records
Show feature table
Start End DB Term Name
6 231 SUPERFAMILY SSF52313 Ribosomal protein S2
6 231 InterPro IPR023591 Ribosomal protein S2, flavodoxin-like domain superfamily
2 240 PANTHER PTHR12534 30S RIBOSOMAL PROTEIN S2 PROKARYOTIC AND ORGANELLAR
2 240 InterPro IPR005706 Ribosomal protein S2, bacteria/mitochondria/plastid
175 186 PRINTS PR00395 Ribosomal protein S2 signature
175 186 InterPro IPR001865 Ribosomal protein S2
37 46 PRINTS PR00395 Ribosomal protein S2 signature
37 46 InterPro IPR001865 Ribosomal protein S2
87 104 PRINTS PR00395 Ribosomal protein S2 signature
87 104 InterPro IPR001865 Ribosomal protein S2
6 24 PRINTS PR00395 Ribosomal protein S2 signature
6 24 InterPro IPR001865 Ribosomal protein S2
158 175 PRINTS PR00395 Ribosomal protein S2 signature
158 175 InterPro IPR001865 Ribosomal protein S2
196 210 PRINTS PR00395 Ribosomal protein S2 signature
196 210 InterPro IPR001865 Ribosomal protein S2
102 151 FunFam G3DSA:1.10.287.610:FF:000001 30S ribosomal protein S2
158 182 ProSitePatterns PS00963 Ribosomal protein S2 signature 2.
158 182 InterPro IPR018130 Ribosomal protein S2, conserved site
9 224 Pfam PF00318 Ribosomal protein S2
9 224 InterPro IPR001865 Ribosomal protein S2
6 17 ProSitePatterns PS00962 Ribosomal protein S2 signature 1.
6 17 InterPro IPR018130 Ribosomal protein S2, conserved site
2 225 Hamap MF_00291_B 30S ribosomal protein S2 [rpsB].
2 225 InterPro IPR005706 Ribosomal protein S2, bacteria/mitochondria/plastid
105 150 Gene3D G3DSA:1.10.287.610 Helix hairpin bin
4 226 NCBIfam TIGR01011 30S ribosomal protein S2
4 226 InterPro IPR005706 Ribosomal protein S2, bacteria/mitochondria/plastid
9 223 CDD cd01425 RPS2
9 223 InterPro IPR001865 Ribosomal protein S2
7 245 Gene3D G3DSA:3.40.50.10490 -

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

Loading 3D structure...

Legend High Medium Low

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 PA3656
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
3 0.356

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.

52 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
TAC P80371 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 P80371 [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.