Protein profile

PA4262

50S ribosomal protein L4

Genome: NC_002516.2

Gene: rplD PA4262 Structure source: AlphaFold UniProt Q9HWD6
Amino acids 200
Annotations 5
Features 14
PDB binders 7
Druggability 0.666

Overview

Basic information about this protein and its source genome.

Accession
PA4262
Gene
rplD PA4262
Status
annotated
Amino acids
200
Structure source
AlphaFold
GO
GO:1990904 A macromolecular complex that contains both RNA and protein molecules. 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:0019843 Binding to a ribosomal RNA. 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.

Target profile

Computed evidence for target prioritization.

Human off-target
hit
Human identity (%)
57.143
Human E-value
4.25e-14
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 0.666
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:1990904 A macromolecular complex that contains both RNA and protein molecules.
  • 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:0019843 Binding to a ribosomal RNA.
  • 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.

Sequence Features

Domain/signature hits from InterPro and related databases.

14 records
Show feature table
Start End DB Term Name
6 199 SUPERFAMILY SSF52166 Ribosomal protein L4
6 199 InterPro IPR023574 Ribosomal protein L4 domain superfamily
11 197 NCBIfam TIGR03953 50S ribosomal protein L4
11 197 InterPro IPR013005 50S ribosomal protein uL4
11 197 Pfam PF00573 Ribosomal protein L4/L1 family
11 197 InterPro IPR002136 Ribosomal protein L4/L1e
6 200 Hamap MF_01328_B 50S ribosomal protein L4 [rplD].
6 200 InterPro IPR013005 50S ribosomal protein uL4
7 198 PANTHER PTHR10746 50S RIBOSOMAL PROTEIN L4
7 198 InterPro IPR013005 50S ribosomal protein uL4
2 199 Gene3D G3DSA:3.40.1370.10 -
2 199 InterPro IPR023574 Ribosomal protein L4 domain superfamily
1 200 FunFam G3DSA:3.40.1370.10:FF:000001 50S ribosomal protein L4
42 65 MobiDBLite mobidb-lite consensus disorder prediction

3D Structure

Selected loaded structure. Experimental PDB entries may cover only a portion of the sequence; predicted models typically cover the full protein.

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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 PA4262
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 0.666
1 0.552
4 0.484

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.

57 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
5MU Q5SHN9 338.2 Da LogP -2.43 TPSA 171.3 ✓ Ro5 ✓ Clean CC1=CN(C(=O)NC1=O)[C@H]2[C@@H]([C@@H]([C@H](O2)…
FSD Q5SHN9 618.7 Da LogP -0.38 TPSA 210.7 3 viol. ✓ Clean C[C@@H]1[C@H](CC[C@@H](O1)N2C=CC(=NC2=O)NC(=O)c…
LUJ Q5SHN9 641.7 Da LogP -6.81 TPSA 327.1 3 viol. ✓ Clean CCC[C@@H]1[C@H](O[C@@H]([C@@H]([C@H]1O)N)O[C@@H…
O Q2FW07 18.0 Da LogP -0.82 TPSA 31.5 ✓ Ro5 ✓ Clean O
OHX Q5SHN9 286.4 Da LogP -3.55 TPSA 156.1 1 viol. ✓ Clean N[Os](N)(N)(N)(N)N
PSU Q5SHN9 324.2 Da LogP -2.67 TPSA 182.2 1 viol. ✓ Clean C1=C(C(=O)NC(=O)N1)[C@H]2[C@@H]([C@@H]([C@H](O2…
SPD Q2FW07 145.2 Da LogP -0.34 TPSA 64.1 ✓ Ro5 ✓ Clean C(CCNCCCN)CN

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.