Protein profile

KP13_00756

50S ribosomal protein L16

Genome: KpKP13

Gene: rplP AHE42372.1 Structure source: AlphaFold + ColabFold UniProt A0A0H3H3W4

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Amino acids 136

Annotations 4

Features 27

PDB binders 8

Druggability 0.503

Overview

Basic information about this protein and its source genome.

Accession: KP13_00756
Assembly: Klebsiella pneumoniae subsp. pneumoniae Kp13, complete sequence
Gene: rplP AHE42372.1
Status: annotated
Amino acids: 136
Structure source: AlphaFold + ColabFold

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. GO:0019843 Binding to a ribosomal RNA.

Target profile

Computed evidence for target prioritization.

Human off-target: hit
Human identity (%): 31.356
Human E-value: 9.48e-09
Gut microbiome off-target: hit
Essential (DEG): Y
DEG identity (%): 99.265
DEG E-value: 6.23e-96
Localization: Cytoplasmic
ColabFold pLDDT: 94.54

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 0.503

Structure A0A0H3H3W4

Pocket Pocket 5

P2Rank

Structure A0A0H3H3W4

Pocket No pockets

ColabFold model

FPocket 0.39 · Pocket 2

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 3732 / 4744 genomes with a hit

Normalized 0.787

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

4 GO

Gene Ontology (GO)

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.
GO:0019843 Binding to a ribosomal RNA.

Sequence Features

Domain/signature hits from InterPro and related databases.

27 records

Show feature table

Start	End	DB	Term	Name
81	92	ProSitePatterns	PS00701	Ribosomal protein L16 signature 2.
81	92	InterPro	IPR020798	Ribosomal protein L16, conserved site
1	136	Gene3D	G3DSA:3.90.1170.10	Ribosomal protein L10e/L16
1	136	InterPro	IPR036920	Ribosomal protein L10e/L16 superfamily
2	126	NCBIfam	TIGR01164	50S ribosomal protein L16
2	126	InterPro	IPR000114	Ribosomal protein L16
58	69	ProSitePatterns	PS00586	Ribosomal protein L16 signature 1.
58	69	InterPro	IPR020798	Ribosomal protein L16, conserved site
87	116	PRINTS	PR00060	Ribosomal protein L16 signature
87	116	InterPro	IPR000114	Ribosomal protein L16
57	86	PRINTS	PR00060	Ribosomal protein L16 signature
57	86	InterPro	IPR000114	Ribosomal protein L16
41	52	PRINTS	PR00060	Ribosomal protein L16 signature
41	52	InterPro	IPR000114	Ribosomal protein L16
23	35	PRINTS	PR00060	Ribosomal protein L16 signature
23	35	InterPro	IPR000114	Ribosomal protein L16
4	133	PANTHER	PTHR12220	50S/60S RIBOSOMAL PROTEIN L16
4	133	InterPro	IPR000114	Ribosomal protein L16
3	133	SUPERFAMILY	SSF54686	Ribosomal protein L16p/L10e
3	133	InterPro	IPR036920	Ribosomal protein L10e/L16 superfamily
1	136	FunFam	G3DSA:3.90.1170.10:FF:000001	50S ribosomal protein L16
1	133	Hamap	MF_01342	50S ribosomal protein L16 [rplP].
1	133	InterPro	IPR000114	Ribosomal protein L16
4	131	Pfam	PF00252	Ribosomal protein L16p/L10e
4	131	InterPro	IPR016180	Ribosomal protein L10e/L16
23	131	CDD	cd01433	Ribosomal_L16_L10e
23	131	InterPro	IPR016180	Ribosomal protein L10e/L16

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_A0A0H3H3W4	AlphaFold	—	—	full sequence	—	Viewing
ColabFold KP13_00756	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				0.08
1				0.002
6				0.001
7				0.0

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
2				0.39

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

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
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…`

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).

Ligand	Tanimoto	MW · LogP · TPSA	Lipinski	PAINS	SMILES
ZINC65748564	0.813	484.1 Da LogP -2.43 TPSA 275.2	2 viol.	✓ Clean	`O=c1[nH]cc([C@H]2O[C@@H](CO[P@@](=O)(O)O[P@@](=…`
ZINC65748567	0.813	484.1 Da LogP -2.43 TPSA 275.2	2 viol.	✓ Clean	`O=c1[nH]cc([C@H]2O[C@@H](CO[P@@](=O)(O)O[P@@](=…`
ZINC77312680	0.813	484.1 Da LogP -2.43 TPSA 275.2	2 viol.	✓ Clean	`O=c1[nH]cc([C@@H]2O[C@H](CO[P@@](=O)(O)O[P@@](=…`
ZINC11616626	0.782	365.2 Da LogP -1.72 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1nc(F)nc2c1ncn2[C@H]1O[C@H](COP(=O)(O)O)[C@@H…`
ZINC1555157	0.782	365.2 Da LogP -1.72 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1nc(F)nc2c1ncn2[C@H]1O[C@@H](COP(=O)(O)O)[C@H…`
ZINC33902473	0.782	365.2 Da LogP -1.72 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1nc(F)nc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@@…`
ZINC3830848	0.782	365.2 Da LogP -1.72 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1nc(F)nc2c1ncn2[C@H]1O[C@@H](COP(=O)(O)O)[C@@…`
ZINC3830849	0.782	365.2 Da LogP -1.72 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1nc(F)nc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C@…`
ZINC3830850	0.782	365.2 Da LogP -1.72 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1nc(F)nc2c1ncn2[C@H]1O[C@@H](COP(=O)(O)O)[C@@…`
ZINC3830851	0.782	365.2 Da LogP -1.72 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1nc(F)nc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C@…`
ZINC3927870	0.782	365.2 Da LogP -1.72 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1nc(F)nc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@@…`
ZINC64479802	0.782	365.2 Da LogP -1.72 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1nc(F)nc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@H…`
ZINC80452830	0.782	365.2 Da LogP -1.72 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1nc(F)nc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@H…`
ZINC109564049	0.772	393.3 Da LogP -1.14 TPSA 186.1	1 viol.	✓ Clean	`CSc1nc(N)c2ncn([C@@H]3O[C@H](COP(=O)(O)O)[C@H](…`
ZINC13473522	0.772	393.3 Da LogP -1.14 TPSA 186.1	1 viol.	✓ Clean	`CSc1nc(N)c2ncn([C@@H]3O[C@H](COP(=O)(O)O)[C@@H]…`
ZINC14589030	0.772	393.3 Da LogP -1.14 TPSA 186.1	1 viol.	✓ Clean	`CSc1nc(N)c2ncn([C@@H]3O[C@H](COP(=O)(O)O)[C@@H]…`
ZINC33979258	0.772	364.2 Da LogP -2.45 TPSA 200.2	1 viol.	✓ Clean	`O=c1[nH]c(O)nc2c1ncn2[C@H]1O[C@@H](COP(=O)(O)O)…`
ZINC33979259	0.772	364.2 Da LogP -2.45 TPSA 200.2	1 viol.	✓ Clean	`O=c1[nH]c(O)nc2c1ncn2[C@H]1O[C@@H](COP(=O)(O)O)…`
ZINC72113294	0.772	393.3 Da LogP -1.14 TPSA 186.1	1 viol.	✓ Clean	`CSc1nc(N)c2ncn([C@@H]3O[C@H](COP(=O)(O)O)[C@H](…`
ZINC78920152	0.772	364.2 Da LogP -2.45 TPSA 200.2	1 viol.	✓ Clean	`O=c1[nH]c(O)nc2c1ncn2[C@H]1O[C@@H](COP(=O)(O)O)…`
ZINC12501413	0.759	363.2 Da LogP -2.57 TPSA 206.0	1 viol.	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@H](COP(=O)(O)O)[C@@H](O)…`
ZINC12958448	0.759	363.2 Da LogP -2.57 TPSA 206.0	1 viol.	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@H](COP(=O)(O)O)[C@H](O)[…`
ZINC1532555	0.759	363.2 Da LogP -2.57 TPSA 206.0	1 viol.	✓ Clean	`Nc1nc2c(ncn2[C@H]2O[C@@H](COP(=O)(O)O)[C@H](O)[…`
ZINC16546189	0.759	363.2 Da LogP -2.57 TPSA 206.0	1 viol.	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@H](COP(=O)(O)O)[C@H](O)[…`
ZINC2159505	0.759	363.2 Da LogP -2.57 TPSA 206.0	1 viol.	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@H](COP(=O)(O)O)[C@@H](O)…`
ZINC3073318	0.759	363.2 Da LogP -2.57 TPSA 206.0	1 viol.	✓ Clean	`Nc1nc2c(ncn2[C@H]2O[C@@H](COP(=O)(O)O)[C@@H](O)…`
ZINC3869963	0.759	363.2 Da LogP -2.57 TPSA 206.0	1 viol.	✓ Clean	`Nc1nc2c(ncn2[C@H]2O[C@@H](COP(=O)(O)O)[C@@H](O)…`
ZINC3869965	0.759	363.2 Da LogP -2.57 TPSA 206.0	1 viol.	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@@H](COP(=O)(O)O)[C@@H](O…`
ZINC9334496	0.759	363.2 Da LogP -2.57 TPSA 206.0	1 viol.	✓ Clean	`Nc1nc2c(ncn2[C@H]2O[C@@H](COP(=O)(O)O)[C@H](O)[…`
ZINC12496640	0.732	297.3 Da LogP -2.23 TPSA 145.5	✓ Ro5	✓ Clean	`CNc1nc2c(ncn2[C@@H]2O[C@H](CO)[C@@H](O)[C@H]2O)…`
ZINC15265567	0.732	297.3 Da LogP -2.23 TPSA 145.5	✓ Ro5	✓ Clean	`CNc1nc2c(ncn2[C@@H]2O[C@H](CO)[C@@H](O)[C@@H]2O…`
ZINC28525041	0.732	297.3 Da LogP -2.23 TPSA 145.5	✓ Ro5	✓ Clean	`CNc1nc2c(ncn2[C@@H]2O[C@H](CO)[C@H](O)[C@@H]2O)…`
ZINC13518964	0.727	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C@H](…`
ZINC1532515	0.727	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](COP(=O)(O)O)[C@H](O…`
ZINC1571045	0.727	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C@@H]…`
ZINC1842158	0.727	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](COP(=O)(O)O)[C@H](O…`
ZINC2046931	0.727	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C@H](…`
ZINC2126310	0.727	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@@H](…`
ZINC3201891	0.727	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C@@H]…`
ZINC3201893	0.727	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](COP(=O)(O)O)[C@@H](…`
ZINC3830180	0.727	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](COP(=O)(O)O)[C@@H](…`
ZINC3860156	0.727	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@@H](…`
ZINC3977897	0.727	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@H](COP(=O)(O)O)[C@@H](O…`
ZINC4806442	0.727	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@H](O…`
ZINC8613167	0.727	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@H](O…`
ZINC13507671	0.722	297.3 Da LogP -2.68 TPSA 148.7	✓ Ro5	✓ Clean	`Cn1c(N)nc2c(ncn2[C@@H]2O[C@H](CO)[C@@H](O)[C@@H…`
ZINC5344125	0.722	297.3 Da LogP -2.68 TPSA 148.7	✓ Ro5	✓ Clean	`Cn1c(N)nc2c(ncn2[C@@H]2O[C@H](CO)[C@@H](O)[C@H]…`
ZINC78216565	0.722	297.3 Da LogP -2.68 TPSA 148.7	✓ Ro5	✓ Clean	`Cn1c(N)nc2c(ncn2[C@@H]2O[C@H](CO)[C@H](O)[C@H]2…`
ZINC78216566	0.722	297.3 Da LogP -2.68 TPSA 148.7	✓ Ro5	✓ Clean	`Cn1c(N)nc2c(ncn2[C@@H]2O[C@H](CO)[C@H](O)[C@@H]…`
ZINC4824264	0.698	281.3 Da LogP -1.67 TPSA 139.5	✓ Ro5	✓ Clean	`Cc1nc(N)c2ncn([C@H]3O[C@@H](CO)[C@@H](O)[C@H]3O…`

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.