Protein profile

KP13_31772

30S ribosomal protein S12

Genome: KpKP13

Gene: AHE42357.1 Structure source: AlphaFold + ColabFold UniProt A0A0H3GU37

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Amino acids 124

Annotations 6

Features 31

PDB binders 13

Druggability 0.171

Overview

Basic information about this protein and its source genome.

Accession: KP13_31772
Assembly: Klebsiella pneumoniae subsp. pneumoniae Kp13, complete sequence
Gene: AHE42357.1
Status: annotated
Amino acids: 124
Structure source: AlphaFold + ColabFold

GO:0015935 The smaller of the two subunits of a ribosome. 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. GO:0000049 Binding to a transfer RNA.

Target profile

Computed evidence for target prioritization.

Human off-target: hit
Human identity (%): 48.182
Human E-value: 1.22e-28
Gut microbiome off-target: hit
Essential (DEG): Y
DEG identity (%): 99.194
DEG E-value: 2.53e-88
Localization: Cytoplasmic
ColabFold pLDDT: 94.57

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 0.171

Structure A0A0H3GU37

Pocket Pocket 3

P2Rank 0.023

Structure A0A0H3GU37

Pocket Pocket 1

ColabFold model

FPocket 0.164 · Pocket 7

P2Rank 0.074 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 3951 / 4744 genomes with a hit

Normalized 0.833

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

6 GO

Gene Ontology (GO)

GO:0015935 The smaller of the two subunits of a ribosome.
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.
GO:0000049 Binding to a transfer RNA.

Sequence Features

Domain/signature hits from InterPro and related databases.

31 records

Show feature table

Start	End	DB	Term	Name
1	124	FunFam	G3DSA:2.40.50.140:FF:000001	30S ribosomal protein S12
12	123	Pfam	PF00164	Ribosomal protein S12/S23
12	123	InterPro	IPR006032	Ribosomal protein S12/S23
3	110	CDD	cd03368	Ribosomal_S12
3	110	InterPro	IPR005679	Ribosomal protein S12, bacterial-type
1	124	Gene3D	G3DSA:2.40.50.140	-
1	124	InterPro	IPR012340	Nucleic acid-binding, OB-fold
18	123	PANTHER	PTHR11652	30S RIBOSOMAL PROTEIN S12 FAMILY MEMBER
18	123	InterPro	IPR006032	Ribosomal protein S12/S23
1	124	PIRSF	PIRSF002133	RPS12p_RPS12a_RPS23e_RPS12o
1	124	InterPro	IPR006032	Ribosomal protein S12/S23
3	123	SUPERFAMILY	SSF50249	Nucleic acid-binding proteins
3	123	InterPro	IPR012340	Nucleic acid-binding, OB-fold
110	122	PRINTS	PR01034	Ribosomal protein S12 signature
110	122	InterPro	IPR006032	Ribosomal protein S12/S23
94	110	PRINTS	PR01034	Ribosomal protein S12 signature
94	110	InterPro	IPR006032	Ribosomal protein S12/S23
58	77	PRINTS	PR01034	Ribosomal protein S12 signature
58	77	InterPro	IPR006032	Ribosomal protein S12/S23
27	42	PRINTS	PR01034	Ribosomal protein S12 signature
27	42	InterPro	IPR006032	Ribosomal protein S12/S23
77	94	PRINTS	PR01034	Ribosomal protein S12 signature
77	94	InterPro	IPR006032	Ribosomal protein S12/S23
42	57	PRINTS	PR01034	Ribosomal protein S12 signature
42	57	InterPro	IPR006032	Ribosomal protein S12/S23
1	123	Hamap	MF_00403_B	30S ribosomal protein S12 [rpsL].
1	123	InterPro	IPR005679	Ribosomal protein S12, bacterial-type
43	50	ProSitePatterns	PS00055	Ribosomal protein S12 signature.
43	50	InterPro	IPR006032	Ribosomal protein S12/S23
1	124	NCBIfam	TIGR00981	30S ribosomal protein S12
1	124	InterPro	IPR005679	Ribosomal protein S12, 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.

No pockets are loaded yet for the displayed AlphaFold model AF_A0A0H3GU37 structure. Run experimental pocket backfill to show FPocket/P2Rank overlays on this structure.

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_A0A0H3GU37	AlphaFold	—	—	full sequence	—	Viewing
ColabFold KP13_31772	ColabFold	—	—	full sequence	—	Loaded

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.

65 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
3TS	4B3T	Q5SHN3	740.2 Da LogP -5.98 TPSA 336.3	3 viol.	✓ Clean	`c1cc(ccc1CO[C@@H]2[C@H](O[C@@H]([C@@H]([C@H]2O)…`
AM2	4AQY	Q5SHN3	539.6 Da LogP -6.95 TPSA 283.6	3 viol.	✓ Clean	`CN[C@H]1[C@H]([C@@H]2[C@H](C[C@H]([C@H](O2)O[C@…`
FES	6RW4	O15235	175.8 Da LogP 1.29 TPSA 0.0	✓ Ro5	✓ Clean	`S1[Fe]S[Fe]1`
GCP	4V8Y	P0CX29	521.2 Da LogP -2.22 TPSA 289.9	3 viol.	✓ Clean	`c1nc2c(n1[C@H]3[C@@H]([C@@H]([C@H](O3)CO[P@](=O…`
GNP	6RW5	O15235	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…`
LLL	5OBM	P0CX29	449.5 Da LogP -3.98 TPSA 213.7	2 viol.	✓ Clean	`C[C@@]1(CO[C@@H]([C@@H]([C@H]1NC)O)O[C@H]2[C@@H…`
M5Z	4B3R	Q5SHN3	731.8 Da LogP -5.84 TPSA 325.3	3 viol.	✓ Clean	`c1ccc(cc1)CC[C@@H]2OC[C@@H]3[C@@H](O2)[C@@H]([C…`
OHX	4V8E	Q5SHN3	286.4 Da LogP -3.55 TPSA 156.1	1 viol.	✓ Clean	`N[Os](N)(N)(N)(N)N`
ON0	4B3M	Q5SHN3	703.7 Da LogP -6.10 TPSA 325.3	3 viol.	✓ Clean	`c1ccc(cc1)[C@@H]2OC[C@@H]3[C@@H](O2)[C@@H]([C@H…`
PAR	4LF7	F6DEQ7	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@…`
RPO	4B3S	Q5SHN3	705.8 Da LogP -6.64 TPSA 336.3	3 viol.	✓ Clean	`c1ccc(cc1)CO[C@@H]2[C@H](O[C@@H]([C@@H]([C@H]2O…`
SCM	1FJG	Q5SHN3	332.4 Da LogP -2.93 TPSA 129.5	✓ Ro5	✓ Clean	`C[C@@H]1CC(=O)[C@]2([C@@H](O1)O[C@@H]3[C@H]([C@…`
SRY	6RW4	O15235	581.6 Da LogP -7.74 TPSA 331.4	3 viol.	✓ Clean	`[H]/N=C(/N)\N[C@@H]1[C@H]([C@@H]([C@H]([C@@H]([…`

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).

Ligand	UniProt (homolog)	pchembl	MW · LogP · TPSA	Lipinski	PAINS	SMILES
DWT	P62266	9.21	503.5 Da LogP 5.75 TPSA 97.6	2 viol.	✓ Clean	`Cc1ccc(cc1Nc2c3cn(nc3nc(n2)c4cccnc4)C)C(=O)Nc5c…`
DXH	P62266	8.06	503.5 Da LogP 5.75 TPSA 97.6	2 viol.	✓ Clean	`Cc1ccc(cc1Nc2c3cnn(c3nc(n2)c4cccnc4)C)C(=O)Nc5c…`

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
ZINC239248067	1.000	539.6 Da LogP -6.95 TPSA 283.6	3 viol.	✓ Clean	`CN[C@@H]1[C@H](O[C@@H]2O[C@H](CO)[C@H](N)[C@H](…`
ZINC239248068	1.000	539.6 Da LogP -6.95 TPSA 283.6	3 viol.	✓ Clean	`CN[C@@H]1[C@H](O[C@@H]2O[C@H](CO)[C@H](N)[C@H](…`
ZINC239248069	1.000	539.6 Da LogP -6.95 TPSA 283.6	3 viol.	✓ Clean	`CN[C@@H]1[C@H](O[C@@H]2O[C@H](CO)[C@H](N)[C@H](…`
ZINC239248070	1.000	539.6 Da LogP -6.95 TPSA 283.6	3 viol.	✓ Clean	`CN[C@@H]1[C@H](O[C@@H]2O[C@H](CO)[C@H](N)[C@H](…`
ZINC245256945	1.000	332.4 Da LogP -2.93 TPSA 129.5	✓ Ro5	✓ Clean	`CN[C@H]1[C@@H](O)[C@@H](NC)[C@@H](O)[C@H]2O[C@H…`
ZINC245256946	1.000	332.4 Da LogP -2.93 TPSA 129.5	✓ Ro5	✓ Clean	`CN[C@@H]1[C@@H]2O[C@]3(O)C(=O)C[C@H](C)O[C@@H]3…`
ZINC245256947	1.000	332.4 Da LogP -2.93 TPSA 129.5	✓ Ro5	✓ Clean	`CN[C@@H]1[C@@H]2O[C@]3(O)C(=O)C[C@H](C)O[C@@H]3…`
ZINC245256948	1.000	332.4 Da LogP -2.93 TPSA 129.5	✓ Ro5	✓ Clean	`CN[C@H]1[C@@H](O)[C@@H](NC)[C@H](O)[C@H]2O[C@H]…`
ZINC5273778	1.000	332.4 Da LogP -2.93 TPSA 129.5	✓ Ro5	✓ Clean	`CN[C@@H]1[C@@H](O)[C@@H]2O[C@H]3O[C@@H](C)CC(=O…`
ZINC53006806	1.000	332.4 Da LogP -2.93 TPSA 129.5	✓ Ro5	✓ Clean	`CN[C@H]1[C@@H](O)[C@@H](NC)[C@H](O)[C@H]2O[C@@H…`
ZINC57406608	1.000	332.4 Da LogP -2.93 TPSA 129.5	✓ Ro5	✓ Clean	`CN[C@H]1[C@@H](O)[C@@H](NC)[C@@H](O)[C@H]2O[C@@…`
ZINC57406609	1.000	332.4 Da LogP -2.93 TPSA 129.5	✓ Ro5	✓ Clean	`CN[C@H]1[C@@H](O)[C@@H](NC)[C@@H](O)[C@H]2O[C@@…`
ZINC57406610	1.000	332.4 Da LogP -2.93 TPSA 129.5	✓ Ro5	✓ Clean	`CN[C@H]1[C@@H](O)[C@@H](NC)[C@@H](O)[C@H]2O[C@@…`
ZINC57406611	1.000	332.4 Da LogP -2.93 TPSA 129.5	✓ Ro5	✓ Clean	`CN[C@H]1[C@@H](O)[C@@H](NC)[C@@H](O)[C@H]2O[C@@…`
ZINC71789713	1.000	332.4 Da LogP -2.93 TPSA 129.5	✓ Ro5	✓ Clean	`CN[C@@H]1[C@H](O)[C@H]2O[C@@H]3O[C@@H](C)CC(=O)…`
ZINC71789714	1.000	332.4 Da LogP -2.93 TPSA 129.5	✓ Ro5	✓ Clean	`CN[C@@H]1[C@H](O)[C@H]2O[C@H]3O[C@@H](C)CC(=O)[…`
ZINC71789715	1.000	332.4 Da LogP -2.93 TPSA 129.5	✓ Ro5	✓ Clean	`CN[C@@H]1[C@H](O)[C@H]2O[C@@H]3O[C@@H](C)CC(=O)…`
ZINC71789716	1.000	332.4 Da LogP -2.93 TPSA 129.5	✓ Ro5	✓ Clean	`CN[C@@H]1[C@H](O)[C@H]2O[C@H]3O[C@@H](C)CC(=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]…`
ZINC104869865	0.850	443.2 Da LogP -2.45 TPSA 252.6	2 viol.	✓ Clean	`Nc1nc2c(ncn2[C@H]2O[C@H](CO[P@@](=O)(O)OP(=O)(O…`
ZINC12504289	0.850	443.2 Da LogP -2.45 TPSA 252.6	2 viol.	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@H](CO[P@@](=O)(O)OP(=O)(…`
ZINC34541308	0.850	443.2 Da LogP -2.45 TPSA 252.6	2 viol.	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@H](CO[P@@](=O)(O)OP(=O)(…`
ZINC35000839	0.850	443.2 Da LogP -2.45 TPSA 252.6	2 viol.	✓ Clean	`Nc1nc2c(ncn2[C@H]2O[C@@H](CO[P@@](=O)(O)OP(=O)(…`
ZINC45284491	0.850	443.2 Da LogP -2.45 TPSA 252.6	2 viol.	✓ Clean	`Nc1nc2c(ncn2[C@H]2O[C@@H](CO[P@@](=O)(O)OP(=O)(…`
ZINC80639694	0.850	443.2 Da LogP -2.45 TPSA 252.6	2 viol.	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@H](CO[P@@](=O)(O)OP(=O)(…`
ZINC8215481	0.850	443.2 Da LogP -2.45 TPSA 252.6	2 viol.	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@H](CO[P@@](=O)(O)OP(=O)(…`
ZINC100015274	0.828	477.6 Da LogP -3.33 TPSA 199.7	2 viol.	✓ Clean	`CCN[C@@H]1C[C@H](N)[C@@H](O[C@H]2O[C@H](CN)CC[C…`
ZINC100735707	0.828	477.6 Da LogP -3.33 TPSA 199.7	2 viol.	✓ Clean	`CCN[C@@H]1C[C@H](N)[C@@H](O[C@H]2O[C@H](CN)CC[C…`
ZINC103650285	0.828	477.6 Da LogP -3.33 TPSA 199.7	2 viol.	✓ Clean	`CCN[C@@H]1C[C@H](N)[C@@H](O[C@@H]2O[C@H](CN)CC[…`
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](…`
ZINC12501413	0.783	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	0.783	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	0.783	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	0.783	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	0.783	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	0.783	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	0.783	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	0.783	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…`

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.