Target candidate with partial support; inspect missing evidence before prioritizing.
4 signalsStrengths
Risks / watch
How to read this page
PDB: experimentally determined structures from the Protein Data Bank. These are the strongest structural evidence, but may cover only part of the protein.
AlphaFold DB model: a precomputed predicted structure downloaded from AlphaFold Database/UniProt, not an experiment performed here.
ColabFold model: a predicted structure generated for this workspace; interpret it with coverage and confidence.
pLDDT: confidence score for predicted structures. High values support local geometry; low values mean the region should not drive pocket interpretation.
FPocket / P2Rank: software tools that predict possible ligand-binding pockets on a 3D structure. They are useful screening signals, not experimental validation.
Druggability: a pocket-based estimate of whether a small molecule could bind productively. It does not mean a drug already exists.
PDB ligand: a compound observed in an experimental structure. Direct same-protein records are stronger than homolog-transferred records.
ChEMBL: a public database of measured compound bioactivity. Direct entries are stronger than entries transferred from similar proteins.
ZINC: a purchasable-compound database. Here it marks proposed candidates from chemical similarity, not measured binders.
LigQ / LigQ_2: an internal TPW pipeline step that gathers PDB, ChEMBL, and ZINC ligand evidence for each protein.
Off-target: sequence similarity to proteins we prefer not to hit, such as human proteins or beneficial gut microbiome proteins.
DEG: Database of Essential Genes. A match suggests the protein resembles genes known to be essential in other organisms.
Roary / CoreCruncher: pan-genome tools used to decide whether a gene is core across analyzed strains or accessory/strain-specific.
EC / GO: functional annotations: EC describes enzyme reactions; GO describes biological process, molecular function, or cellular component.
KEGG pathway: a curated metabolic route label used here to group reactions imported from the metabolic model.
Chokepoint: a metabolic reaction that is the only producer or consumer of a metabolite in the imported model.
Overview
Basic information about this protein and its source genome.
- Accession
- PA4267
- Gene
- rpsG PA4267
- Status
- annotated
- Amino acids
- 156
- 3D evidence
- AlphaFold DB model
Target profile
Computed evidence for target prioritization.
- Human off-target
- Hit
- Human identity (%)
- 31.757
- Human E-value
- 5.94e-07
- Gut microbiome off-target
- Hit
- Essential (DEG)
- Y
- Localization
- Cytoplasmic
Selected pocket evidence
The selected pocket score is the FPocket value used for ranking after applying the curated structure priority. It estimates small-molecule pocket quality; it is not experimental binding evidence. The 3D viewer may show a different loaded structure, so visible pockets can differ.
Sequence
Primary amino-acid sequence viewer.
MPRRRVAAKREVLADPKYGSQILAKFMNHVMESGKKAVAERIVYGALDKVKERGKADPLETFEKALDAIAPLVEVKSRRVGGATYQVPVEVRPSRRNALAMRWLVDFARKRGEKSMALRLAGELLDAAEGKGAAVKKREDVHRMAEANKAFSHYRF
Functional Annotations
Enzyme classification and Gene Ontology terms linked to this protein.
Gene Ontology (GO)
9- GO:0022627 The small subunit of a ribosome located in the cytosol.
- 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:0003729 Binding to messenger RNA (mRNA), an intermediate molecule between DNA and protein. mRNA includes UTR and coding sequences, but does not contain introns.
- 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:0015935 The smaller of the two subunits of a ribosome.
- GO:0003723 Binding to an RNA molecule or a portion thereof.
Sequence Features
Domain/signature hits from InterPro and related databases.
Show feature table
| Start | End | DB | Term | Name |
|---|---|---|---|---|
| 20 | 46 | ProSitePatterns | PS00052 | Ribosomal protein S7 signature. |
| 20 | 46 | InterPro | IPR020606 | Ribosomal protein S7, conserved site |
| 6 | 149 | SUPERFAMILY | SSF47973 | Ribosomal protein S7 |
| 6 | 149 | InterPro | IPR036823 | Ribosomal protein S7 domain superfamily |
| 1 | 149 | Pfam | PF00177 | Ribosomal protein S7p/S5e |
| 1 | 149 | InterPro | IPR023798 | Ribosomal protein S7 domain |
| 2 | 156 | PIRSF | PIRSF002122 | RPS7p_RPS7a_RPS5e_RPS7o |
| 2 | 156 | InterPro | IPR000235 | Ribosomal protein S5/S7 |
| 1 | 156 | Hamap | MF_00480_B | 30S ribosomal protein S7 [rpsG]. |
| 1 | 156 | InterPro | IPR005717 | Ribosomal protein S7, bacterial/organellar-type |
| 12 | 149 | CDD | cd14869 | uS7_Bacteria |
| 8 | 148 | PANTHER | PTHR11205 | RIBOSOMAL PROTEIN S7 |
| 8 | 148 | InterPro | IPR000235 | Ribosomal protein S5/S7 |
| 1 | 155 | FunFam | G3DSA:1.10.455.10:FF:000001 | 30S ribosomal protein S7 |
| 3 | 155 | NCBIfam | TIGR01029 | 30S ribosomal protein S7 |
| 3 | 155 | InterPro | IPR005717 | Ribosomal protein S7, bacterial/organellar-type |
| 1 | 155 | Gene3D | G3DSA:1.10.455.10 | Ribosomal protein S7 domain |
| 1 | 155 | InterPro | IPR036823 | Ribosomal protein S7 domain superfamily |
3D Structure
Selected loaded structure. Experimental PDB entries may cover only a portion of the sequence; AlphaFold DB and ColabFold models typically cover the full protein but remain computational predictions.
Loading 3D structure...
Structural evidence
0 + 1Experimental PDB entries plus predicted AlphaFold DB or ColabFold models. Click Switch to display a different loaded structure in the viewer.
| Entry | Method | Resolution | Chain | Coverage | Links | Status |
|---|---|---|---|---|---|---|
|
AlphaFold DB
PA4267
|
AlphaFold DB | — | — | full sequence | — | Viewing |
Pocket details Inspect a specific pocket, or open the full viewer
- Method
- -
- Score
- -
- Visible layer
- -
- Residues
- -
- Pocket properties
- -
Inspect mode shows the specific pocket/cavity and hides other active pocket layers. Use Surface when you need the wider residue environment.
Binding pockets · FPocket
Druggability: high ≥ 0.7 · medium 0.4–0.69 · low < 0.4
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.
Structural and bioactivity evidence are both available for this target.
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 |
|---|---|---|---|---|---|---|
| PAR RCSB PDB | P17291 | 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 RCSB PDB | P17291 | 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 RCSB PDB | P17291 | 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 RCSB PDB | P17291 | — | — | — |
[O][W]1234O[W]567(O[W]89%10(O5[P]5%11O%12[W]%13…
|
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 |
|---|---|---|---|---|---|---|
| DWT ChEMBL | P46782 | 7.30 | 503.5 Da LogP 5.75 TPSA 97.6 | 2 viol. | ✓ Clean |
Cc1ccc(cc1Nc2c3cn(nc3nc(n2)c4cccnc4)C)C(=O)Nc5c…
|
| DXH ChEMBL | P46782 | 6.75 | 503.5 Da LogP 5.75 TPSA 97.6 | 2 viol. | ✓ Clean |
Cc1ccc(cc1Nc2c3cnn(c3nc(n2)c4cccnc4)C)C(=O)Nc5c…
|
| CHEMBL4129274 ChEMBL | Q9Y2R9 | — | 851.5 Da LogP 4.76 TPSA 183.3 | 3 viol. | Alert |
C=CC(=O)Nc1ccccc1Nc1nc(Nc2ccc(N3CCN(CCOCCOCCOCC…
|
Proposed virtual-screening candidates from ZINC. Score = Tanimoto similarity to a known binder (0–1; higher = more similar).
| Ligand | Tanimoto | MW · LogP · TPSA | Lipinski | PAINS | SMILES |
|---|---|---|---|---|---|
| ZINC11525121 ZINC | 1.000 | 444.4 Da LogP -0.21 TPSA 181.6 | 1 viol. | ✓ Clean |
CN(C)[C@@H]1C(O)=C(C(N)=O)C(=O)[C@]2(O)C(O)=C3C…
|
| ZINC18202167 ZINC | 1.000 | 444.4 Da LogP -0.21 TPSA 181.6 | 1 viol. | ✓ Clean |
CN(C)[C@@H]1C(O)=C(C(N)=O)C(=O)[C@@]2(O)C(O)=C3…
|
| ZINC20410403 ZINC | 1.000 | 444.4 Da LogP -0.21 TPSA 181.6 | 1 viol. | ✓ Clean |
CN(C)[C@@H]1C(O)=C(C(N)=O)C(=O)[C@@]2(O)C(O)=C3…
|
| ZINC21984166 ZINC | 1.000 | 444.4 Da LogP -0.21 TPSA 181.6 | 1 viol. | ✓ Clean |
CN(C)[C@@H]1C(O)=C(C(N)=O)C(=O)[C@@]2(O)C(O)=C3…
|
| ZINC239173596 ZINC | 1.000 | 444.4 Da LogP -0.21 TPSA 181.6 | 1 viol. | ✓ Clean |
CN(C)[C@@H]1C(O)=C(C(N)=O)C(=O)[C@]2(O)C(O)=C3C…
|
| ZINC4059755 ZINC | 1.000 | 444.4 Da LogP -0.21 TPSA 181.6 | 1 viol. | ✓ Clean |
CN(C)[C@@H]1C(O)=C(C(N)=O)C(=O)[C@]2(O)C(O)=C3C…
|
| ZINC4215819 ZINC | 1.000 | 444.4 Da LogP -0.21 TPSA 181.6 | 1 viol. | ✓ Clean |
CN(C)[C@H]1C(O)=C(C(N)=O)C(=O)[C@@]2(O)C(O)=C3C…
|
| ZINC43771554 ZINC | 1.000 | 444.4 Da LogP -0.21 TPSA 181.6 | 1 viol. | ✓ Clean |
CN(C)[C@@H]1C(O)=C(C(N)=O)C(=O)[C@]2(O)C(O)=C3C…
|
| ZINC4807269 ZINC | 1.000 | 444.4 Da LogP -0.21 TPSA 181.6 | 1 viol. | ✓ Clean |
CN(C)[C@@H]1C(O)=C(C(N)=O)C(=O)[C@@]2(O)C(O)=C3…
|
| ZINC575338663 ZINC | 1.000 | 444.4 Da LogP -0.21 TPSA 181.6 | 1 viol. | ✓ Clean |
CN(C)[C@H]1C(O)=C(C(N)=O)C(=O)[C@]2(O)C(O)=C3C(…
|
| ZINC84441937 ZINC | 1.000 | 444.4 Da LogP -0.21 TPSA 181.6 | 1 viol. | ✓ Clean |
CN(C)[C@@H]1C(O)=C(C(N)=O)C(=O)[C@@]2(O)C(O)=C3…
|
| ZINC100052153 ZINC | 0.905 | 454.5 Da LogP -6.65 TPSA 262.4 | 2 viol. | ✓ Clean |
NC[C@H]1O[C@H](O[C@@H]2[C@@H](N)C[C@@H](N)[C@H]…
|
| ZINC100223147 ZINC | 0.905 | 454.5 Da LogP -6.65 TPSA 262.4 | 2 viol. | ✓ Clean |
NC[C@@H]1O[C@@H](O[C@@H]2[C@@H](O[C@@H]3O[C@H](…
|
| ZINC103649633 ZINC | 0.905 | 454.5 Da LogP -6.65 TPSA 262.4 | 2 viol. | ✓ Clean |
NC[C@H]1O[C@H](O[C@@H]2[C@@H](N)C[C@@H](N)[C@H]…
|
| ZINC242575106 ZINC | 0.905 | 454.5 Da LogP -6.65 TPSA 262.4 | 2 viol. | ✓ Clean |
NC[C@@H]1O[C@H](O[C@H]2[C@@H](O[C@@H]3O[C@H](CO…
|
| ZINC242575107 ZINC | 0.905 | 454.5 Da LogP -6.65 TPSA 262.4 | 2 viol. | ✓ Clean |
NC[C@@H]1O[C@H](O[C@H]2[C@@H](O[C@@H]3O[C@H](CO…
|
| ZINC242575108 ZINC | 0.905 | 454.5 Da LogP -6.65 TPSA 262.4 | 2 viol. | ✓ Clean |
NC[C@@H]1O[C@H](O[C@H]2[C@@H](O[C@@H]3O[C@H](CO…
|
| ZINC242575109 ZINC | 0.905 | 454.5 Da LogP -6.65 TPSA 262.4 | 2 viol. | ✓ Clean |
NC[C@@H]1O[C@H](O[C@H]2[C@@H](O[C@@H]3O[C@H](CO…
|
| ZINC43664294 ZINC | 0.905 | 454.5 Da LogP -6.65 TPSA 262.4 | 2 viol. | ✓ Clean |
NC[C@@H]1O[C@H](O[C@H]2[C@@H](O[C@H]3O[C@@H](CO…
|
| ZINC43664297 ZINC | 0.905 | 454.5 Da LogP -6.65 TPSA 262.4 | 2 viol. | ✓ Clean |
NC[C@@H]1O[C@H](O[C@H]2[C@@H](O[C@H]3O[C@@H](CO…
|
| ZINC43664300 ZINC | 0.905 | 454.5 Da LogP -6.65 TPSA 262.4 | 2 viol. | ✓ Clean |
NC[C@@H]1O[C@H](O[C@H]2[C@@H](O[C@H]3O[C@@H](CO…
|
| ZINC43664303 ZINC | 0.905 | 454.5 Da LogP -6.65 TPSA 262.4 | 2 viol. | ✓ Clean |
NC[C@@H]1O[C@H](O[C@H]2[C@@H](O[C@H]3O[C@@H](CO…
|
| ZINC53255716 ZINC | 0.905 | 454.5 Da LogP -6.65 TPSA 262.4 | 2 viol. | ✓ Clean |
NC[C@H]1O[C@H](O[C@@H]2[C@@H](N)C[C@@H](N)[C@H]…
|
| ZINC56874669 ZINC | 0.905 | 454.5 Da LogP -6.65 TPSA 262.4 | 2 viol. | ✓ Clean |
NC[C@H]1O[C@H](O[C@@H]2[C@@H](N)C[C@@H](N)[C@H]…
|
| ZINC60184027 ZINC | 0.810 | 455.5 Da LogP -6.62 TPSA 256.6 | 2 viol. | ✓ Clean |
N[C@H]1C[C@@H](N)[C@H](O)[C@@H](O[C@@H]2O[C@H](…
|
| ZINC28630683 ZINC | 0.800 | 444.4 Da LogP 0.84 TPSA 182.6 | 1 viol. | ✓ Clean |
CN(C)[C@@H]1C(O)=C(C(=N)O)C(=O)[C@]2(O)C(O)=C3C…
|
| ZINC35051264 ZINC | 0.800 | 444.4 Da LogP 0.84 TPSA 182.6 | 1 viol. | ✓ Clean |
CN(C)[C@@H]1C(O)=C(C(=N)O)C(=O)[C@]2(O)C(O)=C3C…
|
| ZINC71769623 ZINC | 0.793 | 417.4 Da LogP -0.78 TPSA 198.6 | 1 viol. | ✓ Clean |
C[C@@]1(O)c2cccc(O)c2C(=O)C2=C(O)[C@]3(O)C(=O)C…
|
| ZINC71769624 ZINC | 0.793 | 417.4 Da LogP -0.78 TPSA 198.6 | 1 viol. | ✓ Clean |
C[C@@]1(O)c2cccc(O)c2C(=O)C2=C(O)[C@]3(O)C(=O)C…
|
| ZINC71769638 ZINC | 0.793 | 416.4 Da LogP -0.82 TPSA 204.4 | 1 viol. | ✓ Clean |
C[C@@]1(O)c2cccc(O)c2C(=O)C2=C(O)[C@]3(O)C(=O)C…
|
| ZINC14768423 ZINC | 0.762 | 478.9 Da LogP 0.44 TPSA 181.6 | 1 viol. | ✓ Clean |
CN(C)[C@@H]1C(O)=C(C(N)=O)C(=O)[C@]2(O)C(O)=C3C…
|
| ZINC19701767 ZINC | 0.762 | 478.9 Da LogP 0.44 TPSA 181.6 | 1 viol. | ✓ Clean |
CN(C)[C@@H]1C(O)=C(C(N)=O)C(=O)[C@@]2(O)C(O)=C3…
|
| ZINC19701769 ZINC | 0.762 | 478.9 Da LogP 0.44 TPSA 181.6 | 1 viol. | ✓ Clean |
CN(C)[C@@H]1C(O)=C(C(N)=O)C(=O)[C@@]2(O)C(O)=C3…
|
| ZINC22054932 ZINC | 0.762 | 478.9 Da LogP 0.44 TPSA 181.6 | 1 viol. | ✓ Clean |
CN(C)[C@H]1C(O)=C(C(N)=O)C(=O)[C@@]2(O)C(O)=C3C…
|
| ZINC34800280 ZINC | 0.762 | 478.9 Da LogP 0.44 TPSA 181.6 | 1 viol. | ✓ Clean |
CN(C)[C@@H]1C(O)=C(C(N)=O)C(=O)[C@@]2(O)C(O)=C3…
|
| ZINC35024403 ZINC | 0.762 | 478.9 Da LogP 0.44 TPSA 181.6 | 1 viol. | ✓ Clean |
CN(C)[C@@H]1C(O)=C(C(N)=O)C(=O)[C@]2(O)C(O)=C3C…
|
| ZINC43769566 ZINC | 0.762 | 478.9 Da LogP 0.44 TPSA 181.6 | 1 viol. | ✓ Clean |
CN(C)[C@@H]1C(O)=C(C(N)=O)C(=O)[C@]2(O)C(O)=C3C…
|
| ZINC44019569 ZINC | 0.762 | 478.9 Da LogP 0.44 TPSA 181.6 | 1 viol. | ✓ Clean |
CN(C)[C@H]1C(O)=C(C(N)=O)C(=O)[C@]2(O)C(O)=C3C(…
|
| ZINC44830179 ZINC | 0.762 | 478.9 Da LogP 0.44 TPSA 181.6 | 1 viol. | ✓ Clean |
CN(C)[C@@H]1C(O)=C(C(N)=O)C(=O)[C@]2(O)C(O)=C3C…
|
| ZINC71789581 ZINC | 0.762 | 478.9 Da LogP 0.44 TPSA 181.6 | 1 viol. | ✓ Clean |
CN(C)[C@@H]1C(O)=C(C(N)=O)C(=O)[C@]2(O)C(O)=C3C…
|
| ZINC86860183 ZINC | 0.762 | 478.9 Da LogP 0.44 TPSA 181.6 | 1 viol. | ✓ Clean |
CN(C)[C@H]1C(O)=C(C(N)=O)C(=O)[C@]2(O)C(O)=C3C(…
|
| ZINC13736610 ZINC | 0.754 | 459.5 Da LogP -0.07 TPSA 178.4 | 1 viol. | ✓ Clean |
C[C@@]1(O)c2cccc(O)c2C(=O)C2=C(O)[C@]3(O)C(=O)C…
|
| ZINC256001609 ZINC | 0.739 | 483.5 Da LogP -7.33 TPSA 288.4 | 2 viol. | ✓ Clean |
NC[C@@H]1O[C@H](O[C@@H]2[C@H](N)C[C@H](N)[C@H](…
|
| ZINC256001610 ZINC | 0.739 | 483.5 Da LogP -7.33 TPSA 288.4 | 2 viol. | ✓ Clean |
NC[C@@H]1O[C@H](O[C@@H]2[C@H](N)C[C@H](N)[C@H](…
|
| ZINC256001611 ZINC | 0.739 | 483.5 Da LogP -7.33 TPSA 288.4 | 2 viol. | ✓ Clean |
NC[C@@H]1O[C@H](O[C@@H]2[C@H](N)C[C@H](N)[C@H](…
|
| ZINC256001612 ZINC | 0.739 | 483.5 Da LogP -7.33 TPSA 288.4 | 2 viol. | ✓ Clean |
NC[C@@H]1O[C@H](O[C@@H]2[C@H](N)C[C@H](N)[C@H](…
|
| ZINC53132258 ZINC | 0.739 | 483.5 Da LogP -7.33 TPSA 288.4 | 2 viol. | ✓ Clean |
NC[C@H]1O[C@H](O[C@@H]2[C@@H](N)C[C@@H](N)[C@H]…
|
| ZINC77301567 ZINC | 0.739 | 483.5 Da LogP -7.33 TPSA 288.4 | 2 viol. | ✓ Clean |
NC[C@H]1O[C@H](O[C@H]2[C@H](N)C[C@H](N)[C@@H](O…
|
| ZINC2382315467 ZINC | 0.698 | 430.4 Da LogP -0.39 TPSA 181.6 | 1 viol. | ✓ Clean |
CN(C)[C@@H]1C(O)=C(C(N)=O)C(=O)[C@]2(O)C(O)=C3C…
|
| ZINC4215546 ZINC | 0.698 | 430.4 Da LogP -0.39 TPSA 181.6 | 1 viol. | ✓ Clean |
CN(C)[C@@H]1C(O)=C(C(N)=O)C(=O)[C@@]2(O)C(O)=C3…
|
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.