Protein profile

PA4260

50S ribosomal protein L2

Genome: NC_002516.2

Gene: rplB PA4260 Structure source: AlphaFold UniProt Q9HWD8
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Amino acids 273
Annotations 9
Features 32
PDB binders 4
Druggability 0.689

Overview

Basic information about this protein and its source genome.

Accession
PA4260
Assembly
Pseudomonas aeruginosa PAO1, complete genome
Gene
rplB PA4260
Status
annotated
Amino acids
273
Structure source
AlphaFold
GO
GO:0022625 The large subunit of a ribosome located in the cytosol. GO:0003723 Binding to an RNA molecule or a portion thereof. GO:0019843 Binding to a ribosomal RNA. GO:0003735 The action of a molecule that contributes to the structural integrity of the ribosome. GO:0016740 Catalysis of the transfer of a group, e.g. a methyl group, glycosyl group, acyl group, phosphorus-containing, or other groups, from one compound (generally regarded as the donor) to another compound (generally regarded as the acceptor). Transferase is the systematic name for any enzyme of EC class 2. GO:0002181 The chemical reactions and pathways resulting in the formation of a protein in the cytoplasm. This is a ribosome-mediated process in which the information in messenger RNA (mRNA) is used to specify the sequence of amino acids in the protein.

Target profile

Computed evidence for target prioritization.

Human off-target
hit
Human identity (%)
36.957
Human E-value
3.1000000000000004e-37
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 0.689
Structure –
Pocket –

Sequence

Primary amino-acid sequence viewer.

MAIVKCKPTSAGRRFVVKVVNQELHKGAPYAPLLEKKSKSGGRNNNGRITTRHIGGGHKQHYRLVDFRRNKDGIPAIVERVEYDPNRTAHIALLKYADGERRYIIAPKGVAAGDQLISGIGAPIKAGNSMPLRNIPVGSTVHGIELKPGKGAQIARSAGASAQLVAREGAYVTLRLRSGEMRKVLAECRATLGEVSNSEHSLRSLGKAGATRWRGVRPTVRGVAMNPVDHPHGGGEGRTSAGRHPVSPWGLQTKGKKTRSNKRTDNMIVRRRK

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

9 GO

Gene Ontology (GO)

9
  • GO:0022625 The large subunit of a ribosome located in the cytosol.
  • GO:0003723 Binding to an RNA molecule or a portion thereof.
  • GO:0019843 Binding to a ribosomal RNA.
  • GO:0003735 The action of a molecule that contributes to the structural integrity of the ribosome.
  • GO:0016740 Catalysis of the transfer of a group, e.g. a methyl group, glycosyl group, acyl group, phosphorus-containing, or other groups, from one compound (generally regarded as the donor) to another compound (generally regarded as the acceptor). Transferase is the systematic name for any enzyme of EC class 2.
  • GO:0002181 The chemical reactions and pathways resulting in the formation of a protein in the cytoplasm. This is a ribosome-mediated process in which the information in messenger RNA (mRNA) is used to specify the sequence of amino acids in the protein.
  • 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:0015934 The larger of the two subunits of a ribosome. Two sites on the ribosomal large subunit are involved in translation, namely the aminoacyl site (A site) and peptidyl site (P site).

Sequence Features

Domain/signature hits from InterPro and related databases.

32 records
Show feature table
Start End DB Term Name
196 273 FunFam G3DSA:4.10.950.10:FF:000001 50S ribosomal protein L2
125 250 Pfam PF03947 Ribosomal Proteins L2, C-terminal domain
125 250 InterPro IPR022669 Ribosomal protein L2, C-terminal
228 273 MobiDBLite mobidb-lite consensus disorder prediction
1 114 FunFam G3DSA:2.40.50.140:FF:000003 50S ribosomal protein L2
127 272 SUPERFAMILY SSF50104 Translation proteins SH3-like domain
127 272 InterPro IPR008991 Translation protein SH3-like domain superfamily
1 114 Gene3D G3DSA:2.40.50.140 -
1 114 InterPro IPR012340 Nucleic acid-binding, OB-fold
3 273 NCBIfam TIGR01171 50S ribosomal protein L2
3 273 InterPro IPR005880 Ribosomal protein L2, bacterial/organellar-type
42 117 Pfam PF00181 Ribosomal Proteins L2, RNA binding domain
42 117 InterPro IPR022666 Ribosomal Proteins L2, RNA binding domain
218 229 ProSitePatterns PS00467 Ribosomal protein L2 signature.
218 229 InterPro IPR022671 Ribosomal protein L2, conserved site
42 118 SMART SM01383 Ribosomal_L2_2
42 118 InterPro IPR002171 Ribosomal protein L2
124 252 SMART SM01382 Ribosomal_L2_C_2
124 252 InterPro IPR022669 Ribosomal protein L2, C-terminal
28 271 PANTHER PTHR13691 RIBOSOMAL PROTEIN L2
28 271 InterPro IPR002171 Ribosomal protein L2
2 125 SUPERFAMILY SSF50249 Nucleic acid-binding proteins
2 125 InterPro IPR012340 Nucleic acid-binding, OB-fold
197 273 Gene3D G3DSA:4.10.950.10 Ribosomal protein L2, domain 3
197 273 InterPro IPR014726 Ribosomal protein L2, domain 3
118 196 Gene3D G3DSA:2.30.30.30 -
118 196 InterPro IPR014722 Ribosomal protein L2, domain 2
118 195 FunFam G3DSA:2.30.30.30:FF:000001 50S ribosomal protein L2
12 273 PIRSF PIRSF002158 RPL2p_RPL2a_RPL8e_RPL2o
12 273 InterPro IPR002171 Ribosomal protein L2
1 273 Hamap MF_01320_B 50S ribosomal protein L2 [rplB].
1 273 InterPro IPR005880 Ribosomal protein L2, bacterial/organellar-type

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 PA4260
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
10 0.689
7 0.312
1 0.296
5 0.246

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.

54 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
8UZ
5NDW
P0CX45 483.5 Da LogP -7.33 TPSA 288.4 2 viol. ✓ Clean C1[C@H]([C@@H]([C@H]([C@@H]([C@H]1N)O[C@@H]2[C@…
LLL
5OBM
P0CX45 449.5 Da LogP -3.98 TPSA 213.7 2 viol. ✓ Clean C[C@@]1(CO[C@@H]([C@@H]([C@H]1NC)O)O[C@H]2[C@@H…
OHX
4V88
P0CX45 286.4 Da LogP -3.55 TPSA 156.1 1 viol. ✓ Clean N[Os](N)(N)(N)(N)N
PAR
5NDV
P0CX45 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@…

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.