Target Pathogen

Overview

Basic information about this protein and its source genome.

Accession: KP13_04674
Assembly: Klebsiella pneumoniae subsp. pneumoniae Kp13, complete sequence
Gene: rplT AHE44066.1
Status: annotated
Amino acids: 118
Structure source: AlphaFold + ColabFold

GO

GO:0019843 Binding to a ribosomal 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. GO:0003735 The action of a molecule that contributes to the structural integrity of the ribosome.

Target profile

Computed evidence for target prioritization.

Human off-target: hit
Human identity (%): 40.351
Human E-value: 1.69e-07
Gut microbiome off-target: hit
Essential (DEG): Y
DEG identity (%): 100.0
DEG E-value: 1.68e-78
Localization: Cytoplasmic
ColabFold pLDDT: 94.84

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 0.132

Structure A6TAI4

Pocket Pocket 9

P2Rank

Structure A6TAI4

Pocket No pockets

ColabFold model

FPocket 0.241 · Pocket 5

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 3974 / 4744 genomes with a hit

Normalized 0.838

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

4 GO

Gene Ontology (GO)

4

GO:0019843 Binding to a ribosomal 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.
GO:0003735 The action of a molecule that contributes to the structural integrity of the ribosome.

Sequence Features

Domain/signature hits from InterPro and related databases.

24 records

Show feature table

Start	End	DB	Term	Name
3	117	SUPERFAMILY	SSF74731	Ribosomal protein L20
3	117	InterPro	IPR035566	Ribosomal protein L20, C-terminal
6	111	CDD	cd07026	Ribosomal_L20
6	111	InterPro	IPR005813	Ribosomal protein L20
3	109	Pfam	PF00453	Ribosomal protein L20
3	109	InterPro	IPR005813	Ribosomal protein L20
1	116	PANTHER	PTHR10986	39S RIBOSOMAL PROTEIN L20
1	116	InterPro	IPR005813	Ribosomal protein L20
1	114	NCBIfam	TIGR01032	50S ribosomal protein L20
1	114	InterPro	IPR005813	Ribosomal protein L20
2	115	Hamap	MF_00382	50S ribosomal protein L20 [rplT].
2	115	InterPro	IPR005813	Ribosomal protein L20
56	118	Gene3D	G3DSA:1.10.1900.20	Ribosomal protein L20
56	118	InterPro	IPR035566	Ribosomal protein L20, C-terminal
56	118	FunFam	G3DSA:1.10.1900.20:FF:000001	50S ribosomal protein L20
75	101	PRINTS	PR00062	Ribosomal protein L20 signature
75	101	InterPro	IPR005813	Ribosomal protein L20
42	71	PRINTS	PR00062	Ribosomal protein L20 signature
42	71	InterPro	IPR005813	Ribosomal protein L20
12	41	PRINTS	PR00062	Ribosomal protein L20 signature
12	41	InterPro	IPR005813	Ribosomal protein L20
3	55	Gene3D	G3DSA:6.10.160.10	-
54	70	ProSitePatterns	PS00937	Ribosomal protein L20 signature.
54	70	InterPro	IPR005813	Ribosomal protein L20

3D Structure

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

Loading 3D structure...

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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_A6TAI4	AlphaFold	—	—	full sequence	—	Viewing
ColabFold KP13_04674	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				0.241

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.

1 records

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
OHX	4V8E	P60491	286.4 Da LogP -3.55 TPSA 156.1	1 viol.	✓ Clean	`N[Os](N)(N)(N)(N)N`

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).

No ChEMBL hits found through similar proteins.

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

No virtual-screening candidates for this protein.

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.

KP13_04674