Target Pathogen

Overview

Basic information about this protein and its source genome.

Accession: KP13_00761
Assembly: Klebsiella pneumoniae subsp. pneumoniae Kp13, complete sequence
Gene: AHE42376.1 rplE
Status: annotated
Amino acids: 179
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.

Target profile

Computed evidence for target prioritization.

Human off-target: hit
Human identity (%): 32.576
Human E-value: 6.51e-12
Gut microbiome off-target: hit
Essential (DEG): Y
DEG identity (%): 100.0
DEG E-value: 2.7500000000000003e-132
Localization: Cytoplasmic
ColabFold pLDDT: 90.2

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 0.318

Structure A0A0H3H3W1

Pocket Pocket 4

P2Rank 0.006

Structure A0A0H3H3W1

Pocket Pocket 1

ColabFold model

FPocket 0.127 · Pocket 2

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 3717 / 4744 genomes with a hit

Normalized 0.784

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

3 GO

Gene Ontology (GO)

3

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.

Sequence Features

Domain/signature hits from InterPro and related databases.

17 records

Show feature table

Start	End	DB	Term	Name
24	80	Pfam	PF00281	Ribosomal protein L5
24	80	InterPro	IPR031310	Ribosomal protein L5, N-terminal
1	179	Gene3D	G3DSA:3.30.1440.10	-
1	179	InterPro	IPR022803	Ribosomal protein L5 domain superfamily
57	73	ProSitePatterns	PS00358	Ribosomal protein L5 signature.
57	73	InterPro	IPR020929	Ribosomal protein L5, conserved site
4	179	SUPERFAMILY	SSF55282	RL5-like
4	179	InterPro	IPR022803	Ribosomal protein L5 domain superfamily
1	179	PIRSF	PIRSF002161	RPL5p_RPL5a_RPL11e_RPL5o
1	179	InterPro	IPR002132	Ribosomal protein L5
84	177	Pfam	PF00673	ribosomal L5P family C-terminus
84	177	InterPro	IPR031309	Ribosomal protein L5, C-terminal
13	179	PANTHER	PTHR11994	60S RIBOSOMAL PROTEIN L11-RELATED
13	179	InterPro	IPR002132	Ribosomal protein L5
1	179	FunFam	G3DSA:3.30.1440.10:FF:000001	50S ribosomal protein L5
1	179	Hamap	MF_01333_B	50S ribosomal protein L5 [rplE].
1	179	InterPro	IPR020930	Ribosomal protein L5, bacterial-type

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_A0A0H3H3W1	AlphaFold	—	—	full sequence	—	Viewing
ColabFold KP13_00761	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
4				0.318

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	5MEI	Q3E757	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_00761