Protein profile

PA4256

50S ribosomal protein L16

Genome: NC_002516.2

Gene: PA4256 rplP Structure source: AlphaFold UniProt Q9HWE2
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Amino acids 137
Annotations 6
Features 27
PDB binders 8
Druggability 0.804

Overview

Basic information about this protein and its source genome.

Accession
PA4256
Assembly
Pseudomonas aeruginosa PAO1, complete genome
Gene
PA4256 rplP
Status
annotated
Amino acids
137
Structure source
AlphaFold
GO
GO:0022625 The large subunit of a ribosome located in the cytosol. 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: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 (%)
36.364
Human E-value
7.06e-06
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 0.804
Structure –
Pocket –

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:0022625 The large subunit of a ribosome located in the cytosol.
  • 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: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.

27 records
Show feature table
Start End DB Term Name
1 137 FunFam G3DSA:3.90.1170.10:FF:000001 50S ribosomal protein L16
4 135 PANTHER PTHR12220 50S/60S RIBOSOMAL PROTEIN L16
4 135 InterPro IPR000114 Ribosomal protein L16
23 112 CDD cd01433 Ribosomal_L16_L10e
23 112 InterPro IPR016180 Ribosomal protein L10e/L16
82 93 ProSitePatterns PS00701 Ribosomal protein L16 signature 2.
82 93 InterPro IPR020798 Ribosomal protein L16, conserved site
88 117 PRINTS PR00060 Ribosomal protein L16 signature
88 117 InterPro IPR000114 Ribosomal protein L16
42 53 PRINTS PR00060 Ribosomal protein L16 signature
42 53 InterPro IPR000114 Ribosomal protein L16
24 36 PRINTS PR00060 Ribosomal protein L16 signature
24 36 InterPro IPR000114 Ribosomal protein L16
58 87 PRINTS PR00060 Ribosomal protein L16 signature
58 87 InterPro IPR000114 Ribosomal protein L16
4 132 Pfam PF00252 Ribosomal protein L16p/L10e
4 132 InterPro IPR016180 Ribosomal protein L10e/L16
59 70 ProSitePatterns PS00586 Ribosomal protein L16 signature 1.
59 70 InterPro IPR020798 Ribosomal protein L16, conserved site
1 134 Hamap MF_01342 50S ribosomal protein L16 [rplP].
1 134 InterPro IPR000114 Ribosomal protein L16
1 134 SUPERFAMILY SSF54686 Ribosomal protein L16p/L10e
1 134 InterPro IPR036920 Ribosomal protein L10e/L16 superfamily
1 137 Gene3D G3DSA:3.90.1170.10 Ribosomal protein L10e/L16
1 137 InterPro IPR036920 Ribosomal protein L10e/L16 superfamily
2 126 NCBIfam TIGR01164 50S ribosomal protein L16
2 126 InterPro IPR000114 Ribosomal protein L16

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 + 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 PA4256
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
1 0.804
2 0.305
3 0.245

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.

58 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
1MG
6YSR
P0ADY7 377.3 Da LogP -2.56 TPSA 195.2 1 viol. ✓ Clean CN1C(=O)c2c(n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)…
2MA
6YST
P0ADY7 361.3 Da LogP -1.55 TPSA 186.1 ✓ Ro5 ✓ Clean Cc1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3…
2MG
6YSR
P0ADY7 377.3 Da LogP -2.11 TPSA 192.0 1 viol. ✓ Clean CNC1=Nc2c(ncn2[C@H]3[C@@H]([C@@H]([C@H](O3)COP(…
6UQ
5KCR
P0ADY7 1406.3 Da LogP 0.84 TPSA 388.0 3 viol. ✓ Clean Cc1c(c(c(c(c1Cl)O)Cl)OC)C(=O)O[C@@H]2[C@H](O[C@…
EVN
5KCS
P0ADY7 1631.4 Da LogP 1.26 TPSA 479.1 3 viol. ✓ Clean Cc1cc(cc(c1C(=O)O[C@@H]2CO[C@]3([C@H]4[C@H]2OCO…
FSD
6CZR
P60489 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…
OHX
4V8E
P60489 286.4 Da LogP -3.55 TPSA 156.1 1 viol. ✓ Clean N[Os](N)(N)(N)(N)N
PSU
6YSR
P0ADY7 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…

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.