Protein profile

KP13_12202

50S ribosomal protein L11

Genome: KpKP13

Gene: ANJ86642.1 Structure source: AlphaFold + ColabFold UniProt A0A0H3GGN5
Export view
Amino acids 142
Annotations 5
Features 26
PDB binders 0
Druggability 0.52

Overview

Basic information about this protein and its source genome.

Accession
KP13_12202
Assembly
Klebsiella pneumoniae subsp. pneumoniae Kp13, complete sequence
Gene
ANJ86642.1
Status
annotated
Amino acids
142
Structure source
AlphaFold + ColabFold
GO
GO:0003735 The action of a molecule that contributes to the structural integrity of 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. 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:0022625 The large subunit of a ribosome located in the cytosol. GO:0070180 Binding to large ribosomal subunit RNA (LSU rRNA), a constituent of the large ribosomal subunit. In S. cerevisiae, this is the 25S rRNA.

Target profile

Computed evidence for target prioritization.

Human off-target
hit
Human identity (%)
46.552
Human E-value
3.95e-14
Gut microbiome off-target
hit
Essential (DEG)
Y
DEG identity (%)
99.296
DEG E-value
5e-101
Localization
Cytoplasmic
ColabFold pLDDT
82.27

Selected Druggability evidence

AlphaFold / UniProt model

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 0.52
Structure A0A0H3GGN5
Pocket Pocket 5
P2Rank 0.004
Structure A0A0H3GGN5
Pocket Pocket 1
ColabFold model
FPocket 0.471 · Pocket 6
Core conservation Conserved core gene
Roary core
CoreCruncher core
Gut microbiome 3860 / 4744 genomes with a hit
Normalized 0.814

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:0003735 The action of a molecule that contributes to the structural integrity of 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.
  • 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:0022625 The large subunit of a ribosome located in the cytosol.
  • GO:0070180 Binding to large ribosomal subunit RNA (LSU rRNA), a constituent of the large ribosomal subunit. In S. cerevisiae, this is the 25S rRNA.

Sequence Features

Domain/signature hits from InterPro and related databases.

26 records
Show feature table
Start End DB Term Name
9 141 SMART SM00649 rl11c
9 141 InterPro IPR000911 Ribosomal protein L11/L12
72 140 Pfam PF00298 Ribosomal protein L11, RNA binding domain
72 140 InterPro IPR020783 Ribosomal protein L11, C-terminal
3 142 NCBIfam TIGR01632 50S ribosomal protein L11
3 142 InterPro IPR006519 Ribosomal protein L11, bacterial-type
5 142 Hamap MF_00736 50S ribosomal protein L11 [rplK].
5 142 InterPro IPR000911 Ribosomal protein L11/L12
3 73 SUPERFAMILY SSF54747 Ribosomal L11/L12e N-terminal domain
3 73 InterPro IPR036796 Ribosomal protein L11/L12, N-terminal domain superfamily
68 141 SUPERFAMILY SSF46906 Ribosomal protein L11, C-terminal domain
68 141 InterPro IPR036769 Ribosomal protein L11, C-terminal domain superfamily
2 70 FunFam G3DSA:3.30.1550.10:FF:000001 50S ribosomal protein L11
9 67 Pfam PF03946 Ribosomal protein L11, N-terminal domain
9 67 InterPro IPR020784 Ribosomal protein L11, N-terminal
71 142 FunFam G3DSA:1.10.10.250:FF:000001 50S ribosomal protein L11
9 140 CDD cd00349 Ribosomal_L11
9 140 InterPro IPR000911 Ribosomal protein L11/L12
2 69 Gene3D G3DSA:3.30.1550.10 -
2 69 InterPro IPR036796 Ribosomal protein L11/L12, N-terminal domain superfamily
127 142 ProSitePatterns PS00359 Ribosomal protein L11 signature.
127 142 InterPro IPR020785 Ribosomal protein L11, conserved site
70 142 Gene3D G3DSA:1.10.10.250 -
70 142 InterPro IPR036769 Ribosomal protein L11, C-terminal domain superfamily
3 140 PANTHER PTHR11661 60S RIBOSOMAL PROTEIN L12
3 140 InterPro IPR000911 Ribosomal protein L11/L12

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 + 2

Experimental PDB entries and predicted models. Click Switch to display a different structure in the viewer.

Entry Method Resolution Chain Coverage Links Status
AlphaFold AF_A0A0H3GGN5
AlphaFold — — full sequence — Viewing
ColabFold KP13_12202
ColabFold — — full sequence — Loaded
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
5 0.52
6 0.301
2 0.238

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.

17 records

Proposed virtual-screening candidates from ZINC. Score = Tanimoto similarity to a known binder (0–1; higher = more similar).

Show only:
Ligand Tanimoto MW · LogP · TPSA Lipinski PAINS SMILES
ZINC1532902 0.700 206.2 Da LogP -0.86 TPSA 132.1 ✓ Ro5 ✓ Clean O=C(O)CC[C@@](O)(CC(=O)O)C(=O)O
ZINC2018106 0.700 206.2 Da LogP -0.86 TPSA 132.1 ✓ Ro5 ✓ Clean O=C(O)CC[C@](O)(CC(=O)O)C(=O)O
ZINC3593496 0.652 206.2 Da LogP -1.16 TPSA 121.1 ✓ Ro5 ✓ Clean COC(=O)C[C@@](O)(CC(=O)O)C(=O)O
ZINC3593497 0.652 206.2 Da LogP -1.16 TPSA 121.1 ✓ Ro5 ✓ Clean COC(=O)C[C@](O)(CC(=O)O)C(=O)O
ZINC14686440 0.625 436.4 Da LogP -2.64 TPSA 247.9 1 viol. ✓ Clean O=C(O)C[C@](O)(CC(=O)NCCCCNC(=O)C[C@@](O)(CC(=O…
ZINC14686442 0.625 436.4 Da LogP -2.64 TPSA 247.9 1 viol. ✓ Clean O=C(O)C[C@@](O)(CC(=O)NCCCCNC(=O)C[C@](O)(CC(=O…
ZINC14686444 0.625 436.4 Da LogP -2.64 TPSA 247.9 1 viol. ✓ Clean O=C(O)C[C@@](O)(CC(=O)NCCCCNC(=O)C[C@@](O)(CC(=…
ZINC13398039 0.577 234.2 Da LogP -0.38 TPSA 121.1 ✓ Ro5 ✓ Clean CC(C)OC(=O)C[C@](O)(CC(=O)O)C(=O)O
ZINC2528012 0.577 234.2 Da LogP -0.38 TPSA 121.1 ✓ Ro5 ✓ Clean CC(C)OC(=O)C[C@@](O)(CC(=O)O)C(=O)O
ZINC146315135 0.560 204.2 Da LogP 0.86 TPSA 94.8 ✓ Ro5 ✓ Clean CCCCC[C@@](O)(CC(=O)O)C(=O)O
ZINC146315336 0.560 204.2 Da LogP 0.86 TPSA 94.8 ✓ Ro5 ✓ Clean CCCCC[C@](O)(CC(=O)O)C(=O)O
ZINC1850353 0.556 206.1 Da LogP -0.86 TPSA 132.1 ✓ Ro5 ✓ Clean O=C(O)CC(O)(CC(=O)O)CC(=O)O
ZINC13398014 0.522 220.2 Da LogP -1.07 TPSA 110.1 ✓ Ro5 ✓ Clean COC(=O)CC(O)(CC(=O)OC)C(=O)O
ZINC3861629 0.522 206.1 Da LogP -1.16 TPSA 121.1 ✓ Ro5 ✓ Clean COC(=O)C(O)(CC(=O)O)CC(=O)O
ZINC100969993 0.500 359.5 Da LogP 2.70 TPSA 123.9 ✓ Ro5 ✓ Clean CCCCCCCCCCCCNC(=O)C[C@](O)(CC(=O)O)C(=O)O
ZINC100969996 0.500 359.5 Da LogP 2.70 TPSA 123.9 ✓ Ro5 ✓ Clean CCCCCCCCCCCCNC(=O)C[C@@](O)(CC(=O)O)C(=O)O
ZINC1711854 0.500 248.2 Da LogP -0.13 TPSA 149.2 ✓ Ro5 ✓ Clean O=C(O)CC(CC(=O)O)(CC(=O)O)CC(=O)O

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.