Protein profile

KP13_00754

50S ribosomal protein L22

Genome: KpKP13

Gene: rplV AHE42370.1 Structure source: AlphaFold + ColabFold UniProt A0A0H3GZA8

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Amino acids 110

Annotations 6

Features 17

PDB binders 18

Druggability 0.411

Overview

Basic information about this protein and its source genome.

Accession: KP13_00754
Assembly: Klebsiella pneumoniae subsp. pneumoniae Kp13, complete sequence
Gene: rplV AHE42370.1
Status: annotated
Amino acids: 110
Structure source: AlphaFold + ColabFold

GO:0003735 The action of a molecule that contributes to the structural integrity of the ribosome. GO:0015934 The larger of the two subunits of a ribosome. Two sites on the ribosomal large subunit are involved in translation, namely the aminoacyl site (A site) and peptidyl site (P site). 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:0019843 Binding to a ribosomal RNA.

Target profile

Computed evidence for target prioritization.

Human off-target: No hit
Human identity (%): 0.0
Gut microbiome off-target: hit
Essential (DEG): Y
DEG identity (%): 97.273
DEG E-value: 5.34e-74
Localization: Cytoplasmic
ColabFold pLDDT: 95.55

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 0.411

Structure A0A0H3GZA8

Pocket Pocket 1

P2Rank

Structure A0A0H3GZA8

Pocket No pockets

ColabFold model

FPocket 0.616 · Pocket 3

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 2212 / 4744 genomes with a hit

Normalized 0.466

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

6 GO

Gene Ontology (GO)

GO:0003735 The action of a molecule that contributes to the structural integrity of the ribosome.
GO:0015934 The larger of the two subunits of a ribosome. Two sites on the ribosomal large subunit are involved in translation, namely the aminoacyl site (A site) and peptidyl site (P site).
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:0019843 Binding to a ribosomal RNA.

Sequence Features

Domain/signature hits from InterPro and related databases.

17 records

Show feature table

Start	End	DB	Term	Name
1	110	FunFam	G3DSA:3.90.470.10:FF:000001	50S ribosomal protein L22
5	107	CDD	cd00336	Ribosomal_L22
5	107	InterPro	IPR001063	Ribosomal protein L22/L17
2	109	PANTHER	PTHR13501	CHLOROPLAST 50S RIBOSOMAL PROTEIN L22-RELATED
2	109	InterPro	IPR005727	Ribosomal protein L22, bacterial/chloroplast-type
5	108	Pfam	PF00237	Ribosomal protein L22p/L17e
5	108	InterPro	IPR001063	Ribosomal protein L22/L17
83	107	ProSitePatterns	PS00464	Ribosomal protein L22 signature.
83	107	InterPro	IPR018260	Ribosomal protein L22/L17, conserved site
1	110	Gene3D	G3DSA:3.90.470.10	Ribosomal protein L22/L17
1	110	InterPro	IPR036394	Ribosomal protein L22/L17 superfamily
5	107	NCBIfam	TIGR01044	50S ribosomal protein L22
5	107	InterPro	IPR005727	Ribosomal protein L22, bacterial/chloroplast-type
1	110	Hamap	MF_01331_B	50S ribosomal protein L22 [rplV].
1	110	InterPro	IPR005727	Ribosomal protein L22, bacterial/chloroplast-type
1	109	SUPERFAMILY	SSF54843	Ribosomal protein L22
1	109	InterPro	IPR036394	Ribosomal protein L22/L17 superfamily

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_A0A0H3GZA8	AlphaFold	—	—	full sequence	—	Viewing
ColabFold KP13_00754	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
1				0.411

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
3				0.616

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.

68 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
1F3	4IOA	Q9RXJ7	843.0 Da LogP 5.33 TPSA 191.5	3 viol.	✓ Clean	`CC[C@@H]1[C@@]2([C@@H]([C@H](C(=O)[C@@H](C[C@@]…`
1F4	4IOC	Q9RXJ7	817.0 Da LogP 5.28 TPSA 175.3	3 viol.	✓ Clean	`CC[C@@H]1[C@@]2([C@@H]([C@@H](C(=O)[C@@H](C[C@@…`
1MG	6XZ7	P61175	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)…`
4AC	6XA1	P18621	365.2 Da LogP -2.07 TPSA 180.4	✓ Ro5	✓ Clean	`CC(=O)NC1=NC(=O)N(C=C1)[C@H]2[C@@H]([C@@H]([C@H…`
5GP	6GAW	A0A4X1TXR4	363.2 Da LogP -2.57 TPSA 206.0	1 viol.	✓ Clean	`c1nc2c(n1[C@H]3[C@@H]([C@@H]([C@H](O3)COP(=O)(O…`
5MU	5JTE	P61175	338.2 Da LogP -2.43 TPSA 171.3	✓ Ro5	✓ Clean	`CC1=CN(C(=O)NC1=O)[C@H]2[C@@H]([C@@H]([C@H](O2)…`
ERY	3J7Z	P61175	733.9 Da LogP 1.79 TPSA 193.9	2 viol.	✓ Clean	`CC[C@@H]1[C@@]([C@@H]([C@H](C(=O)[C@@H](C[C@@](…`
GNP	6YDP	A0A4X1TXR4	522.2 Da LogP -2.76 TPSA 301.9	3 viol.	✓ Clean	`c1nc2c(n1[C@H]3[C@@H]([C@@H]([C@H](O3)CO[P@](=O…`
GSP	6GAW	A0A4X1TXR4	539.2 Da LogP -2.22 TPSA 282.0	3 viol.	✓ Clean	`c1nc2c(n1[C@H]3[C@@H]([C@@H]([C@H](O3)CO[P@](=O…`
LMA	3PIO	Q9RXJ7	831.1 Da LogP 4.78 TPSA 191.8	2 viol.	✓ Clean	`C[C@@H]1C[C@@H]([C@H]([C@@H](O1)O[C@H]2[C@H](C[…`
M2G	6XA1	P18621	391.3 Da LogP -2.09 TPSA 183.3	✓ Ro5	✓ Clean	`CN(C)C1=Nc2c(ncn2[C@H]3[C@@H]([C@@H]([C@H](O3)C…`
MA6	6XA1	P18621	375.3 Da LogP -1.38 TPSA 163.3	✓ Ro5	✓ Clean	`CN(C)c1c2c(ncn1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H]…`
MVM	6OLF	P18621	433.9 Da LogP 3.26 TPSA 88.8	✓ Ro5	✓ Clean	`c1cc2c(nc1)n(nn2)c3ccc(cc3)C(=O)N(c4c(cccn4)Cl)…`
OHX	4V88	P05740	286.4 Da LogP -3.55 TPSA 156.1	1 viol.	✓ Clean	`N[Os](N)(N)(N)(N)N`
OMC	6XA1	P18621	337.2 Da LogP -1.79 TPSA 166.4	✓ Ro5	✓ Clean	`CO[C@@H]1[C@@H]([C@H](O[C@H]1N2C=CC(=NC2=O)N)CO…`
PAR	5NDV	P05740	615.6 Da LogP -8.86 TPSA 347.3	3 viol.	✓ Clean	`C1[C@H]([C@@H]([C@H]([C@@H]([C@H]1N)O[C@@H]2[C@…`
PSU	6XZ7	P61175	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…`
SPM	6GAW	A0A4X1TXR4	202.3 Da LogP -0.36 TPSA 76.1	✓ Ro5	✓ Clean	`C(CCNCCCN)CNCCCN`

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
ZINC13515793	1.000	338.2 Da LogP -2.43 TPSA 171.3	✓ Ro5	✓ Clean	`Cc1cn([C@@H]2O[C@H](COP(=O)(O)O)[C@@H](O)[C@H]2…`
ZINC1532734	1.000	202.3 Da LogP -0.36 TPSA 76.1	✓ Ro5	✓ Clean	`NCCCNCCCCNCCCN`
ZINC218456124	1.000	433.9 Da LogP 3.26 TPSA 88.8	✓ Ro5	✓ Clean	`O=C(c1ccc(-n2nnc3cccnc32)cc1)N(c1ncccc1Cl)[C@@H…`
ZINC239222141	1.000	733.9 Da LogP 1.79 TPSA 193.9	2 viol.	✓ Clean	`CC[C@@H]1OC(=O)[C@H](C)[C@H](O[C@@H]2C[C@](C)(O…`
ZINC239222142	1.000	733.9 Da LogP 1.79 TPSA 193.9	2 viol.	✓ Clean	`CC[C@@H]1OC(=O)[C@H](C)[C@H](O[C@@H]2C[C@](C)(O…`
ZINC239415425	1.000	733.9 Da LogP 1.79 TPSA 193.9	2 viol.	✓ Clean	`CC[C@@H]1OC(=O)[C@H](C)[C@H](O[C@@H]2C[C@](C)(O…`
ZINC239415426	1.000	733.9 Da LogP 1.79 TPSA 193.9	2 viol.	✓ Clean	`CC[C@@H]1OC(=O)[C@H](C)[C@H](O[C@@H]2C[C@](C)(O…`
ZINC100052153	0.905	454.5 Da LogP -6.65 TPSA 262.4	2 viol.	✓ Clean	`NC[C@H]1O[C@H](O[C@@H]2[C@@H](N)C[C@@H](N)[C@H]…`
ZINC100223147	0.905	454.5 Da LogP -6.65 TPSA 262.4	2 viol.	✓ Clean	`NC[C@@H]1O[C@@H](O[C@@H]2[C@@H](O[C@@H]3O[C@H](…`
ZINC103649633	0.905	454.5 Da LogP -6.65 TPSA 262.4	2 viol.	✓ Clean	`NC[C@H]1O[C@H](O[C@@H]2[C@@H](N)C[C@@H](N)[C@H]…`
ZINC242575106	0.905	454.5 Da LogP -6.65 TPSA 262.4	2 viol.	✓ Clean	`NC[C@@H]1O[C@H](O[C@H]2[C@@H](O[C@@H]3O[C@H](CO…`
ZINC242575107	0.905	454.5 Da LogP -6.65 TPSA 262.4	2 viol.	✓ Clean	`NC[C@@H]1O[C@H](O[C@H]2[C@@H](O[C@@H]3O[C@H](CO…`
ZINC242575108	0.905	454.5 Da LogP -6.65 TPSA 262.4	2 viol.	✓ Clean	`NC[C@@H]1O[C@H](O[C@H]2[C@@H](O[C@@H]3O[C@H](CO…`
ZINC242575109	0.905	454.5 Da LogP -6.65 TPSA 262.4	2 viol.	✓ Clean	`NC[C@@H]1O[C@H](O[C@H]2[C@@H](O[C@@H]3O[C@H](CO…`
ZINC43664294	0.905	454.5 Da LogP -6.65 TPSA 262.4	2 viol.	✓ Clean	`NC[C@@H]1O[C@H](O[C@H]2[C@@H](O[C@H]3O[C@@H](CO…`
ZINC43664297	0.905	454.5 Da LogP -6.65 TPSA 262.4	2 viol.	✓ Clean	`NC[C@@H]1O[C@H](O[C@H]2[C@@H](O[C@H]3O[C@@H](CO…`
ZINC43664300	0.905	454.5 Da LogP -6.65 TPSA 262.4	2 viol.	✓ Clean	`NC[C@@H]1O[C@H](O[C@H]2[C@@H](O[C@H]3O[C@@H](CO…`
ZINC43664303	0.905	454.5 Da LogP -6.65 TPSA 262.4	2 viol.	✓ Clean	`NC[C@@H]1O[C@H](O[C@H]2[C@@H](O[C@H]3O[C@@H](CO…`
ZINC53255716	0.905	454.5 Da LogP -6.65 TPSA 262.4	2 viol.	✓ Clean	`NC[C@H]1O[C@H](O[C@@H]2[C@@H](N)C[C@@H](N)[C@H]…`
ZINC56874669	0.905	454.5 Da LogP -6.65 TPSA 262.4	2 viol.	✓ Clean	`NC[C@H]1O[C@H](O[C@@H]2[C@@H](N)C[C@@H](N)[C@H]…`
ZINC27564039	0.867	202.3 Da LogP -0.36 TPSA 76.1	✓ Ro5	✓ Clean	`NCCCCNCCCNCCCN`
ZINC13377742	0.857	230.4 Da LogP 0.42 TPSA 76.1	✓ Ro5	✓ Clean	`NCCCCNCCCCNCCCCN`
ZINC13518650	0.837	418.2 Da LogP -2.31 TPSA 217.8	1 viol.	✓ Clean	`Cc1cn([C@@H]2O[C@H](CO[P@@](=O)(O)OP(=O)(O)O)[C…`
ZINC239415175	0.831	790.0 Da LogP 2.75 TPSA 200.0	2 viol.	✓ Clean	`CCC(=O)O[C@@H]1[C@H](O[C@@H]2[C@H](C)[C@H](O[C@…`
ZINC239415176	0.831	790.0 Da LogP 2.75 TPSA 200.0	2 viol.	✓ Clean	`CCC(=O)O[C@@H]1[C@H](O[C@@H]2[C@H](C)[C@H](O[C@…`
ZINC239415177	0.831	790.0 Da LogP 2.75 TPSA 200.0	2 viol.	✓ Clean	`CCC(=O)O[C@@H]1[C@H](O[C@@H]2[C@H](C)[C@H](O[C@…`
ZINC239415178	0.831	790.0 Da LogP 2.75 TPSA 200.0	2 viol.	✓ Clean	`CCC(=O)O[C@@H]1[C@H](O[C@@H]2[C@H](C)[C@H](O[C@…`
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@@](=…`
ZINC60184027	0.810	455.5 Da LogP -6.62 TPSA 256.6	2 viol.	✓ Clean	`N[C@H]1C[C@@H](N)[C@H](O)[C@@H](O[C@@H]2O[C@H](…`
ZINC239347287	0.807	749.0 Da LogP 1.90 TPSA 180.1	2 viol.	✓ Clean	`CC[C@@H]1OC(=O)[C@H](C)[C@H](O[C@@H]2C[C@](C)(O…`
ZINC239347288	0.807	749.0 Da LogP 1.90 TPSA 180.1	2 viol.	✓ Clean	`CC[C@@H]1OC(=O)[C@H](C)[C@H](O[C@@H]2C[C@](C)(O…`
ZINC239347289	0.807	749.0 Da LogP 1.90 TPSA 180.1	2 viol.	✓ Clean	`CC[C@@H]1OC(=O)[C@H](C)[C@H](O[C@@H]2C[C@](C)(O…`
ZINC239347290	0.807	749.0 Da LogP 1.90 TPSA 180.1	2 viol.	✓ Clean	`CC[C@@H]1OC(=O)[C@H](C)[C@H](O[C@@H]2C[C@](C)(O…`
ZINC13519607	0.804	498.2 Da LogP -2.19 TPSA 264.4	2 viol.	✓ Clean	`Cc1cn([C@@H]2O[C@H](CO[P@](=O)(O)O[P@](=O)(O)OP…`
ZINC31298140	0.804	498.2 Da LogP -2.19 TPSA 264.4	2 viol.	✓ Clean	`Cc1cn([C@@H]2O[C@H](CO[P@@](=O)(O)O[P@@](=O)(O)…`
ZINC81168754	0.804	498.2 Da LogP -2.19 TPSA 264.4	2 viol.	✓ Clean	`Cc1cn([C@@H]2O[C@H](CO[P@@](=O)(O)O[P@@](=O)(O)…`
ZINC81168756	0.804	498.2 Da LogP -2.19 TPSA 264.4	2 viol.	✓ Clean	`Cc1cn([C@@H]2O[C@H](CO[P@@](=O)(O)O[P@@](=O)(O)…`
ZINC1598087	0.800	215.4 Da LogP 1.61 TPSA 64.1	✓ Ro5	✓ Clean	`NCCCCCCNCCCCCCN`
ZINC239165236	0.784	862.1 Da LogP 2.68 TPSA 226.3	2 viol.	✓ Clean	`CCOC(=O)CCC(=O)O[C@@H]1[C@H](O[C@@H]2[C@H](C)[C…`
ZINC239165237	0.784	862.1 Da LogP 2.68 TPSA 226.3	2 viol.	✓ Clean	`CCOC(=O)CCC(=O)O[C@@H]1[C@H](O[C@@H]2[C@H](C)[C…`
ZINC239165238	0.784	862.1 Da LogP 2.68 TPSA 226.3	2 viol.	✓ Clean	`CCOC(=O)CCC(=O)O[C@@H]1[C@H](O[C@@H]2[C@H](C)[C…`
ZINC239165239	0.784	862.1 Da LogP 2.68 TPSA 226.3	2 viol.	✓ Clean	`CCOC(=O)CCC(=O)O[C@@H]1[C@H](O[C@@H]2[C@H](C)[C…`
ZINC13518175	0.755	450.1 Da LogP -2.13 TPSA 171.3	✓ Ro5	✓ Clean	`O=c1[nH]c(=O)n([C@@H]2O[C@H](COP(=O)(O)O)[C@@H]…`
ZINC256001609	0.739	483.5 Da LogP -7.33 TPSA 288.4	2 viol.	✓ Clean	`NC[C@@H]1O[C@H](O[C@@H]2[C@H](N)C[C@H](N)[C@H](…`
ZINC256001611	0.739	483.5 Da LogP -7.33 TPSA 288.4	2 viol.	✓ Clean	`NC[C@@H]1O[C@H](O[C@@H]2[C@H](N)C[C@H](N)[C@H](…`
ZINC256001612	0.739	483.5 Da LogP -7.33 TPSA 288.4	2 viol.	✓ Clean	`NC[C@@H]1O[C@H](O[C@@H]2[C@H](N)C[C@H](N)[C@H](…`
ZINC53132258	0.739	483.5 Da LogP -7.33 TPSA 288.4	2 viol.	✓ Clean	`NC[C@H]1O[C@H](O[C@@H]2[C@@H](N)C[C@@H](N)[C@H]…`
ZINC77301567	0.739	483.5 Da LogP -7.33 TPSA 288.4	2 viol.	✓ Clean	`NC[C@H]1O[C@H](O[C@H]2[C@H](N)C[C@H](N)[C@@H](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.