KpATCC43816 Protein target profile

ribosomal protein L2

Accession: VK055_3758

Gene: AIK82313.1 rplB 3D evidence: AlphaFold DB model + ColabFold model Metabolism Not in network UniProt A0A0H3GWL9

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Length 255

Pocket druggability (P2Rank · AlphaFold DB model) 0.234

Direct ligand evidence 0 56 total records

Functional annotation 0 EC 9 GO

Target summary

Target candidate with partial support; inspect missing evidence before prioritizing.

Automated synthesis of the evidence currently loaded. Review the underlying records before prioritizing this protein.

Main supporting evidence

Core gene across strains Marked as conserved by both pan-genome tools: Roary and CoreCruncher. Moderate predicted binding pocket FPocket selected-pocket score 0.58. This supports review but is not experimental validation. Structure available AlphaFold DB model + ColabFold model Ligand evidence via structure/bioactivity 6 structural and 0 bioactivity records.

Risks to review

Evidence coverage

Core evidence streams are available for this target.

Terms and data sources used on this page

PDB: experimentally determined structures from the Protein Data Bank. These are the strongest structural evidence, but may cover only part of the protein.

AlphaFold DB model: a precomputed predicted structure downloaded from AlphaFold Database/UniProt, not an experiment performed here.

ColabFold model: a predicted structure generated for this workspace; interpret it with coverage and confidence.

pLDDT: confidence score for predicted structures. High values support local geometry; low values mean the region should not drive pocket interpretation.

FPocket / P2Rank: software tools that predict possible ligand-binding pockets on a 3D structure. They are useful screening signals, not experimental validation.

Druggability: a pocket-based estimate of whether a small molecule could bind productively. It does not mean a drug already exists.

PDB ligand: a compound observed in an experimental structure. Direct same-protein records are stronger than homolog-transferred records.

ChEMBL: a public database of measured compound bioactivity. Direct entries are stronger than entries transferred from similar proteins.

ZINC: a purchasable-compound database. Here it marks proposed candidates from chemical similarity, not measured binders.

LigQ / LigQ_2: an internal Target pipeline step that gathers PDB, ChEMBL, and ZINC ligand evidence for each protein.

Off-target: sequence similarity to proteins we prefer not to hit, such as human proteins or beneficial gut microbiome proteins.

DEG: Database of Essential Genes. A match suggests the protein resembles genes known to be essential in other organisms.

Roary / CoreCruncher: pan-genome tools used to decide whether a gene is core across analyzed strains or accessory/strain-specific.

EC / GO: functional annotations: EC describes enzyme reactions; GO describes biological process, molecular function, or cellular component.

KEGG pathway: a curated metabolic route label used here to group reactions imported from the metabolic model.

Chokepoint: a metabolic reaction that is the only producer or consumer of a metabolite in the imported model.

Prioritization evidence

Selectivity, essentiality, structural confidence, conservation, and predicted binding-site evidence.

Off-target risk

Human off-target: Hit
Human identity (%): 42.222 Lower values reduce human off-target concern.
Human E-value: 9.19e-23
Gut microbiome similarity: 80.0% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 98.431 Higher values support similarity to known essential genes.
DEG E-value: 0.0 Smaller values mean stronger essential-gene similarity.

Structure confidence

ColabFold pLDDT: 95.64 0-100 confidence; >70 supports local structural interpretation.

Binding-site evidence

AlphaFold DB / UniProt model

P2Rank's binding-site probability is the primary druggability signal shown across the app; FPocket's druggability score is shown alongside it for comparison. Both estimate small-molecule pocket quality after applying the curated structure priority — neither is experimental binding evidence. The 3D viewer may show a different loaded structure, so visible pockets can differ.

Druggability (P2Rank) 0.234

Structure A0A0H3GWL9

Pocket Pocket 1

Druggability (FPocket) 0.582

Structure A0A0H3GWL9

Pocket Pocket 8

ColabFold model

P2Rank 0.077 · Pocket 1

FPocket 0.094 · Pocket 3

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 3795 / 4744 genomes with a hit

Prevalence 80.0%

Metabolic context

Reactions catalyzed, pathway membership, and centrality in the genome-scale metabolic network.

This protein is not associated with the imported metabolic network for this genome.

Browse the genome's metabolic network

Imported from KpATCC43816.sbml · 2026-07-09

Sequence

Primary amino-acid sequence viewer.

MVNPELHKGKPFAPLLEKNSKSGGRNNNGRITTRHIGGGHKQAYRIVDFKRNKDGIPAVVERLEYDPNRSANIALVLYKDGERRYILAPKGLKAGDQIQSGVDAAIKAGNTLPMRNIPVGSTVHNVEMKPGKGGQLARSAGTYVQIVARDGAYVTLRLRSGEMRKVEADCRATLGEVGNAEHMLRVLGKAGAARWRGVRPTVRGTAMNPVDHPHGGGEGRNFGKHPVSPWGLQTKGKKTRSNKRTDKFIVRRRSK

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

9 GO

Subcellular localization

Localization: Cytoplasmic

Gene Ontology (GO)

GO:0003735 The action of a molecule that contributes to the structural integrity of the ribosome.
GO:0016740 Catalysis of the transfer of a group, e.g. a methyl group, glycosyl group, acyl group, phosphorus-containing, or other groups, from one compound (generally regarded as the donor) to another compound (generally regarded as the acceptor). Transferase is the systematic name for any enzyme of EC class 2.
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:0003723 Binding to an RNA molecule or a portion thereof.
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:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
GO:0019843 Binding to a ribosomal RNA.
GO:0002181 The chemical reactions and pathways resulting in the formation of a protein in the cytoplasm. This is a ribosome-mediated process in which the information in messenger RNA (mRNA) is used to specify the sequence of amino acids in the protein.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

33 records

Show feature table

Start	End	DB	Term	Name
4	254	NCBIfam	TIGR01171	50S ribosomal protein L2
4	254	InterPro	IPR005880	Ribosomal protein L2, bacterial/organellar-type
200	211	ProSitePatterns	PS00467	Ribosomal protein L2 signature.
200	211	InterPro	IPR022671	Ribosomal protein L2, conserved site
203	246	MobiDBLite	mobidb-lite	consensus disorder prediction
24	99	Pfam	PF00181	Ribosomal Proteins L2, RNA binding domain
24	99	InterPro	IPR022666	Ribosomal Proteins L2, RNA binding domain
24	100	SMART	SM01383	Ribosomal_L2_2
24	100	InterPro	IPR002171	Ribosomal protein L2
109	251	SUPERFAMILY	SSF50104	Translation proteins SH3-like domain
109	251	InterPro	IPR008991	Translation protein SH3-like domain superfamily
20	254	PANTHER	PTHR13691	RIBOSOMAL PROTEIN L2
20	254	InterPro	IPR002171	Ribosomal protein L2
1	96	Gene3D	G3DSA:2.40.50.140	-
1	96	InterPro	IPR012340	Nucleic acid-binding, OB-fold
107	231	Pfam	PF03947	Ribosomal Proteins L2, C-terminal domain
107	231	InterPro	IPR022669	Ribosomal protein L2, C-terminal
1	255	PIRSF	PIRSF002158	RPL2p_RPL2a_RPL8e_RPL2o
1	255	InterPro	IPR002171	Ribosomal protein L2
1	254	Hamap	MF_01320_B	50S ribosomal protein L2 [rplB].
1	254	InterPro	IPR005880	Ribosomal protein L2, bacterial/organellar-type
2	107	SUPERFAMILY	SSF50249	Nucleic acid-binding proteins
2	107	InterPro	IPR012340	Nucleic acid-binding, OB-fold
1	37	MobiDBLite	mobidb-lite	consensus disorder prediction
97	177	Gene3D	G3DSA:2.30.30.30	-
97	177	InterPro	IPR014722	Ribosomal protein L2, domain 2
178	255	Gene3D	G3DSA:4.10.950.10	Ribosomal protein L2, domain 3
178	255	InterPro	IPR014726	Ribosomal protein L2, domain 3
1	96	FunFam	G3DSA:2.40.50.140:FF:000003	50S ribosomal protein L2
106	233	SMART	SM01382	Ribosomal_L2_C_2
106	233	InterPro	IPR022669	Ribosomal protein L2, C-terminal
100	177	FunFam	G3DSA:2.30.30.30:FF:000001	50S ribosomal protein L2
178	255	FunFam	G3DSA:4.10.950.10:FF:000001	50S ribosomal protein L2

3D structure

Selected loaded structure. Experimental PDB entries may cover only a portion of the sequence; AlphaFold DB and ColabFold models typically cover the full protein but remain computational predictions.

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Pocket score High Medium Low

How colors and pocket overlays are used

Uniform protein color marks the displayed model as a single molecular object.

Experimental PDB structures may be colored by chain to distinguish subunits or copies present in the file.

Pocket colors and alpha spheres are evidence overlays for predicted binding cavities; they are not alternative protein chains.

'Alpha spheres' is FPocket's own cavity-shape geometry, imported when available and aligned with the loaded structure.

'Pocket atoms'/'Predicted site atoms' show the pocket's residue atoms instead: P2Rank reports residues rather than alpha spheres, and FPocket falls back to this when alpha-sphere geometry is unavailable or doesn't align.

'No pocket geometry' means neither alpha spheres nor residue-position data could be found for that pocket; the layer just highlights the same residues as 'Nearby residues'.

Pocket details Inspect a specific pocket, or open the full viewer

Binding pockets · P2Rank

Druggability (P2Rank): high ≥ 0.5 · medium 0.2–0.49 · low < 0.2

Pocket 1 P2Rank #1

0.234

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Surrounding area

Pocket 2 P2Rank #2

0.175

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Surrounding area

Pocket 3 P2Rank #3

0.093

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Surrounding area

Binding pockets · FPocket

Druggability (FPocket): high ≥ 0.7 · medium 0.4–0.69 · low < 0.4

Pocket 1 FPocket #8

0.582

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Surrounding area

Pocket 2 FPocket #1

0.347

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Surrounding area

Pocket 3 FPocket #17

0.255

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Surrounding area

Pocket 4 FPocket #4

0.237

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Surrounding area

Binding pockets · P2Rank

Druggability (P2Rank): high ≥ 0.5 · medium 0.2–0.49 · low < 0.2

Pocket 1 P2Rank #1

0.077

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Surrounding area

Pocket 2 P2Rank #2

0.077

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Surrounding area

Pocket 3 P2Rank #3

0.03

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Surrounding area

Pocket 4 P2Rank #4

0.012

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Surrounding area

All structural evidence 0 experimental · 2 predicted

Structural evidence

0 + 2

Experimental PDB entries plus predicted AlphaFold DB or ColabFold models. Click Switch to display a different loaded structure in the viewer.

Entry	Method	Resolution	Chain	Coverage	Links	Status
AlphaFold DB AF_A0A0H3GWL9	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold VK055_3758	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.

56 records

Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 same-protein records

Transferred evidence 6 records from similar proteins

Structural ligands 6 0 loaded crystals

Measured bioactivity 0 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

1MG PDB via homolog 377.3 Da · LogP -2.56 · TPSA 195.2 Open detail RCSB PDB

8UZ PDB via homolog Detail RCSB PDB

LLL PDB via homolog Detail RCSB PDB

OHX PDB via homolog Detail RCSB PDB

PAR PDB via homolog Detail RCSB PDB

Highest-confidence structural evidence: ligands co-crystallized with this exact protein. If the source PDB is loaded in Target, 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 RCSB PDB	6PJ6	P60422	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)…`
8UZ RCSB PDB	5NDW	P0CX45	483.5 Da LogP -7.33 TPSA 288.4	2 viol.	✓ Clean	`C1[C@H]([C@@H]([C@H]([C@@H]([C@H]1N)O[C@@H]2[C@…`
LLL RCSB PDB	5OBM	P0CX45	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…`
OHX RCSB PDB	4V88	P0CX45	286.4 Da LogP -3.55 TPSA 156.1	1 viol.	✓ Clean	`N[Os](N)(N)(N)(N)N`
PAR RCSB PDB	5NDV	P0CX45	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 RCSB PDB	6PJ6	P60422	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
ZINC253708542 ZINC	1.000	449.5 Da LogP -3.98 TPSA 213.7	2 viol.	✓ Clean	`CN[C@@H]1[C@H](O)[C@H](O[C@@H]2[C@H](N)C[C@H](N…`
ZINC253708545 ZINC	1.000	449.5 Da LogP -3.98 TPSA 213.7	2 viol.	✓ Clean	`CN[C@@H]1[C@H](O)[C@H](O[C@H]2[C@@H](O)[C@@H](O…`
ZINC253708547 ZINC	1.000	449.5 Da LogP -3.98 TPSA 213.7	2 viol.	✓ Clean	`CN[C@@H]1[C@H](O)[C@H](O[C@H]2[C@@H](O)[C@@H](O…`
ZINC253708549 ZINC	1.000	449.5 Da LogP -3.98 TPSA 213.7	2 viol.	✓ Clean	`CN[C@@H]1[C@H](O)[C@H](O[C@@H]2[C@H](N)C[C@H](N…`
ZINC8216590 ZINC	1.000	449.5 Da LogP -3.98 TPSA 213.7	2 viol.	✓ Clean	`CN[C@@H]1[C@@H](O)[C@@H](O[C@@H]2[C@@H](O)[C@H]…`
ZINC100052153 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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]…`
ZINC256001609 ZINC	0.860	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](…`
ZINC256001610 ZINC	0.860	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 ZINC	0.860	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 ZINC	0.860	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 ZINC	0.860	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 ZINC	0.860	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…`
ZINC2048392517 ZINC	0.833	463.6 Da LogP -3.72 TPSA 199.7	2 viol.	✓ Clean	`CNC[C@@H]1CC[C@@H](N)[C@@H](O[C@H]2[C@@H](N)C[C…`
ZINC2383303497 ZINC	0.833	463.6 Da LogP -3.72 TPSA 199.7	2 viol.	✓ Clean	`CNC[C@H]1CC[C@H](N)[C@H](O[C@H]2[C@H](N)C[C@H](…`
ZINC257407586 ZINC	0.833	463.6 Da LogP -3.72 TPSA 199.7	2 viol.	✓ Clean	`CNC[C@@H]1CC[C@H](N)[C@H](O[C@@H]2[C@H](N)C[C@H…`
ZINC257407587 ZINC	0.833	463.6 Da LogP -3.72 TPSA 199.7	2 viol.	✓ Clean	`CNC[C@@H]1CC[C@H](N)[C@H](O[C@H]2[C@H](O)[C@@H]…`
ZINC257407588 ZINC	0.833	463.6 Da LogP -3.72 TPSA 199.7	2 viol.	✓ Clean	`CNC[C@@H]1CC[C@H](N)[C@H](O[C@@H]2[C@H](N)C[C@H…`
ZINC257407589 ZINC	0.833	463.6 Da LogP -3.72 TPSA 199.7	2 viol.	✓ Clean	`CNC[C@@H]1CC[C@H](N)[C@H](O[C@H]2[C@H](O)[C@@H]…`
ZINC44018317 ZINC	0.833	463.6 Da LogP -3.72 TPSA 199.7	2 viol.	✓ Clean	`CNC[C@H]1CC[C@@H](N)[C@@H](O[C@H]2[C@@H](N)C[C@…`
ZINC44018319 ZINC	0.833	463.6 Da LogP -3.72 TPSA 199.7	2 viol.	✓ Clean	`CNC[C@H]1CC[C@@H](N)[C@@H](O[C@H]2[C@@H](N)C[C@…`
ZINC44018321 ZINC	0.833	463.6 Da LogP -3.72 TPSA 199.7	2 viol.	✓ Clean	`CNC[C@H]1CC[C@@H](N)[C@@H](O[C@H]2[C@@H](N)C[C@…`
ZINC44018323 ZINC	0.833	463.6 Da LogP -3.72 TPSA 199.7	2 viol.	✓ Clean	`CNC[C@H]1CC[C@@H](N)[C@@H](O[C@H]2[C@@H](N)C[C@…`
ZINC60183269 ZINC	0.833	463.6 Da LogP -3.72 TPSA 199.7	2 viol.	✓ Clean	`CNC[C@@H]1CC[C@@H](N)[C@@H](O[C@H]2[C@@H](N)C[C…`
ZINC8214612 ZINC	0.833	463.6 Da LogP -3.72 TPSA 199.7	2 viol.	✓ Clean	`CNC[C@@H]1CC[C@@H](N)[C@@H](O[C@@H]2[C@@H](N)C[…`
ZINC100015274 ZINC	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 ZINC	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 ZINC	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[…`
ZINC65748564 ZINC	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 ZINC	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 ZINC	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 ZINC	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](…`
ZINC17654095 ZINC	0.756	484.5 Da LogP -7.29 TPSA 282.6	2 viol.	✓ Clean	`NC[C@@H]1O[C@@H](O[C@@H]2[C@@H](N)C[C@@H](N)[C@…`
ZINC1857793042 ZINC	0.756	484.5 Da LogP -7.29 TPSA 282.6	2 viol.	✓ Clean	`NC[C@H]1O[C@H](O[C@@H]2[C@@H](N)C[C@@H](N)[C@H]…`
ZINC239203292 ZINC	0.756	484.5 Da LogP -7.29 TPSA 282.6	2 viol.	✓ Clean	`NC[C@@H]1O[C@H](O[C@H]2[C@@H](O)[C@@H](O[C@@H]3…`
ZINC245224174 ZINC	0.756	484.5 Da LogP -7.29 TPSA 282.6	2 viol.	✓ Clean	`NC[C@@H]1O[C@@H](O[C@@H]2[C@H](N)C[C@H](N)[C@@H…`
ZINC245224175 ZINC	0.756	484.5 Da LogP -7.29 TPSA 282.6	2 viol.	✓ Clean	`NC[C@@H]1O[C@@H](O[C@@H]2[C@H](N)C[C@H](N)[C@@H…`
ZINC43470138 ZINC	0.756	484.5 Da LogP -7.29 TPSA 282.6	2 viol.	✓ Clean	`NC[C@H]1O[C@@H](O[C@@H]2[C@@H](N)C[C@@H](N)[C@H…`
ZINC8214590 ZINC	0.756	484.5 Da LogP -7.29 TPSA 282.6	2 viol.	✓ Clean	`NC[C@H]1O[C@H](O[C@@H]2[C@@H](N)C[C@@H](N)[C@H]…`

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.

Cross-references

External database identifiers for this protein, its structures, ligands, and metabolic reactions.

Sequence

UniProt A0A0H3GWL9