KpKP13 Protein target profile

Riboflavin biosynthesis bifunctional protein ribD

Accession: KP13_02046

Gene: ribD AHE46049.1 3D evidence: AlphaFold DB model + ColabFold model UniProt A0A0H3GSM9

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Length 367

Pocket druggability (P2Rank · AlphaFold DB model) 0.917

Direct ligand evidence 0 57 total records

Functional annotation 0 EC 7 GO

Target summary

Promising target candidate with multiple supporting evidence streams.

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

Main supporting evidence

No similar human protein detected The current BLAST sequence screen did not find a significant human match, lowering apparent off-target risk. Core gene across strains Marked as conserved by both pan-genome tools: Roary and CoreCruncher. Second pocket predictor agrees P2Rank predicted binding-site probability 0.92. Structure available AlphaFold DB model + ColabFold model Review the complete evidence below

Risks to review

Evidence gaps

No metabolic context No SBML/network-derived reaction evidence is loaded for this protein.

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: No hit
Gut microbiome similarity: 3.6% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 86.921 Higher values support similarity to known essential genes.
DEG E-value: 0.0 Smaller values mean stronger essential-gene similarity.

Structure confidence

ColabFold pLDDT: 96.74 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) 0.917

Structure A0A0H3GSM9

Pocket Pocket 1

Druggability (FPocket) 0.39

Structure A0A0H3GSM9

Pocket Pocket 22

ColabFold model

P2Rank 0.92 · Pocket 1

FPocket 0.822 · Pocket 26

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 172 / 4744 genomes with a hit

Prevalence 3.6%

Sequence

Primary amino-acid sequence viewer.

MQDEMYMARALKLAARGRFTTHPNPNVGCVIVKDGEIVGEGFHYRAGEPHAEVHALRMAGEKARGATAYVTLEPCSHHGRTPPCCDALIAAGVSRVVAAMQDPNPQVAGRGLYRLQQAGIEVSHGLMMNEAEALNKGFLKRMRTGFPWVQLKLGASLDGRTAMASGESQWITSPQARRDVQRLRAQSHAILTSSATVLADDPALTVRWQELSADTQALYPEENLRQPLRVVIDSQNRVTPEHRIVQQAGETLFARLRADERQWPESARTLLVPEHNGHLDLVLLMMLLGKQQINSVWVEAGATLAGALLQAGLVDELIVYIAPKLLGNAARGLCALPGLEELSQAPHFKFNEIRQVGPDVCLHLTTA

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

7 GO

Subcellular localization

Localization: Cytoplasmic

Gene Ontology (GO)

GO:0008270 Binding to a zinc ion (Zn).
GO:0008835 Catalysis of the reaction: 2,5-diamino-6-hydroxy-4-(5-phosphoribosylamino)-pyrimidine + H2O + H+ = 5-amino-6-(5-phosphoribosylamino)uracil + NH4.
GO:0016787 Catalysis of the hydrolysis of various bonds, e.g. C-O, C-N, C-C, phosphoric anhydride bonds, etc.
GO:0009231 The chemical reactions and pathways resulting in the formation of riboflavin (vitamin B2), the precursor for the coenzymes flavin mononucleotide (FMN) and flavin adenine dinucleotide (FAD).
GO:0008703 Catalysis of the reaction: 5-amino-6-(5-phosphoribitylamino)uracil + NADP+ = 5-amino-6-(5-phosphoribosylamino)uracil + H+ + NADPH.
GO:0003824 Catalysis of a biochemical reaction at physiological temperatures. In biologically catalyzed reactions, the reactants are known as substrates, and the catalysts are naturally occurring macromolecular substances known as enzymes. Enzymes possess specific binding sites for substrates, and are usually composed wholly or largely of protein, but RNA that has catalytic activity (ribozyme) is often also regarded as enzymatic.
GO:0050661 Binding to nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions; binding may be to either the oxidized form, NADP+, or the reduced form, NADPH.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

25 records

Show feature table

Start	End	DB	Term	Name
144	362	SUPERFAMILY	SSF53597	Dihydrofolate reductase-like
144	362	InterPro	IPR024072	Dihydrofolate reductase-like domain superfamily
1	140	Gene3D	G3DSA:3.40.140.10	Cytidine Deaminase, domain 2
146	365	NCBIfam	TIGR00227	riboflavin-specific deaminase C-terminal domain
146	365	InterPro	IPR011549	Riboflavin-specific deaminase, C-terminal
50	88	ProSitePatterns	PS00903	Cytidine and deoxycytidylate deaminases zinc-binding region signature.
50	88	InterPro	IPR016192	APOBEC/CMP deaminase, zinc-binding
141	363	PANTHER	PTHR38011	DIHYDROFOLATE REDUCTASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_8G06820)
141	367	Gene3D	G3DSA:3.40.430.10	Dihydrofolate Reductase, subunit A
141	367	InterPro	IPR024072	Dihydrofolate reductase-like domain superfamily
141	366	FunFam	G3DSA:3.40.430.10:FF:000006	Riboflavin biosynthesis protein RibD
1	367	PIRSF	PIRSF006769	RibD
1	367	InterPro	IPR004794	Riboflavin biosynthesis protein RibD
147	362	Pfam	PF01872	RibD C-terminal domain
147	362	InterPro	IPR002734	Bacterial bifunctional deaminase-reductase, C-terminal
1	140	FunFam	G3DSA:3.40.140.10:FF:000025	Riboflavin biosynthesis protein RibD
7	362	NCBIfam	TIGR00326	bifunctional diaminohydroxyphosphoribosylaminopyrimidine deaminase/5-amino-6-(5-phosphoribosylamino)uracil reductase RibD
7	362	InterPro	IPR004794	Riboflavin biosynthesis protein RibD
2	99	Pfam	PF00383	Cytidine and deoxycytidylate deaminase zinc-binding region
2	99	InterPro	IPR002125	Cytidine and deoxycytidylate deaminase domain
3	145	SUPERFAMILY	SSF53927	Cytidine deaminase-like
3	145	InterPro	IPR016193	Cytidine deaminase-like
1	123	ProSiteProfiles	PS51747	Cytidine and deoxycytidylate deaminases domain profile.
1	123	InterPro	IPR002125	Cytidine and deoxycytidylate deaminase domain
7	119	CDD	cd01284	Riboflavin_deaminase-reductase

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

0.917

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Surrounding area

Pocket 2 P2Rank #2

0.879

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Surrounding area

Pocket 3 P2Rank #3

0.672

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Surrounding area

Pocket 4 P2Rank #4

0.172

Likely same site as FPocket 22 0.7 Å 12 shared residues 100% of smaller site

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Surrounding area

Pocket 5 P2Rank #5

0.062

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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 #22

0.39

Likely same site as P2Rank 4 0.7 Å 12 shared residues 100% of smaller site

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Surrounding area

Residue sets

UniProt: Active site:52-52 Proton donor

UniProt: Binding site:154-154

UniProt: Binding site:168-168

UniProt: Binding site:170-170

UniProt: Binding site:184-184

UniProt: Binding site:196-196

UniProt: Binding site:200-200

UniProt: Binding site:204-204

UniProt: Binding site:207-207

UniProt: Binding site:234-234

UniProt: Binding site:299-299

UniProt: Binding site:301-307

UniProt: Binding site:50-50

UniProt: Binding site:75-75

UniProt: Binding site:84-84

Binding pockets · P2Rank

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

Pocket 1 P2Rank #1

0.92

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Surrounding area

Pocket 2 P2Rank #2

0.84

Likely same site as FPocket 20 2.3 Å 15 shared residues 94% of smaller site

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Surrounding area

Pocket 3 P2Rank #3

0.683

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Surrounding area

Pocket 4 P2Rank #4

0.16

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Surrounding area

Pocket 5 P2Rank #5

0.055

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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 #26

0.822 Unusual size

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Surrounding area

Pocket 2 FPocket #20

0.368

Likely same site as P2Rank 2 2.3 Å 15 shared residues 94% of smaller site

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Surrounding area

Pocket 3 FPocket #19

0.228

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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_A0A0H3GSM9	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold KP13_02046	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.

57 records

Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 same-protein records

Transferred evidence 7 records from similar proteins

Structural ligands 7 0 loaded crystals

Measured bioactivity 0 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

5GP PDB via homolog 363.2 Da · LogP -2.57 · TPSA 206.0 Open detail RCSB PDB

AI9 PDB via homolog Detail RCSB PDB

AIF PDB via homolog Detail RCSB PDB

AOF PDB via homolog Detail RCSB PDB

CAC 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
5GP RCSB PDB	3ZPG	D0CB74	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…`
AI9 RCSB PDB	4G3M	P17618	354.2 Da LogP -3.46 TPSA 231.5	1 viol.	✓ Clean	`C([C@H]([C@H]([C@H](/C=N/C1=C(C(=O)NC(=O)N1)N)O…`
AIF RCSB PDB	3EX8	P17618	354.2 Da LogP -3.46 TPSA 231.5	1 viol.	✓ Clean	`C([C@H]([C@H]([C@@H](\C=N\C1=C(C(=O)NC(=O)N1)N)…`
AOF RCSB PDB	4G3M	P17618	354.2 Da LogP -3.39 TPSA 220.2	1 viol.	✓ Clean	`C([C@@H]1[C@H]([C@H]([C@@H](O1)NC2=C(C(=O)NC(=O…`
CAC RCSB PDB	3ZPG	D0CB74	137.0 Da LogP -0.52 TPSA 40.1	✓ Ro5	✓ Clean	`C[As](=O)(C)[O-]`
MA5 RCSB PDB	2AZN	Q58085	452.5 Da LogP -2.40 TPSA 178.5	2 viol.	✓ Clean	`C1CCC(CC1)CCO[C@H]2[C@@H]([C@H]([C@@H]([C@H](O2…`
OXL RCSB PDB	3ZPG	D0CB74	88.0 Da LogP -3.51 TPSA 80.3	✓ Ro5	✓ Clean	`C(=O)(C(=O)[O-])[O-]`

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
ZINC1532555 ZINC	1.000	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)[…`
ZINC58649445 ZINC	1.000	452.5 Da LogP -2.40 TPSA 178.5	2 viol.	✓ Clean	`OC[C@H]1O[C@H](O[C@@H]2[C@@H](CO)O[C@@H](OCCC3C…`
ZINC14881288 ZINC	0.818	494.6 Da LogP -1.23 TPSA 178.5	2 viol.	✓ Clean	`OC[C@H]1O[C@H](O[C@@H]2[C@@H](CO)O[C@@H](OCCCCC…`
ZINC25725098 ZINC	0.786	438.5 Da LogP -2.79 TPSA 178.5	2 viol.	✓ Clean	`OC[C@H]1O[C@H](O[C@@H]2[C@@H](CO)O[C@@H](OCC3CC…`
ZINC1532637 ZINC	0.722	283.2 Da LogP -2.69 TPSA 159.5	✓ Ro5	✓ Clean	`Nc1nc2c(ncn2[C@H]2O[C@@H](CO)[C@H](O)[C@@H]2O)c…`
ZINC1550030 ZINC	0.722	283.2 Da LogP -2.69 TPSA 159.5	✓ Ro5	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@H](CO)[C@@H](O)[C@H]2O)c…`
ZINC1570863 ZINC	0.722	283.2 Da LogP -2.69 TPSA 159.5	✓ Ro5	✓ Clean	`Nc1nc2c(ncn2[C@H]2O[C@H](CO)[C@@H](O)[C@H]2O)c(…`
ZINC1698205 ZINC	0.722	283.2 Da LogP -2.69 TPSA 159.5	✓ Ro5	✓ Clean	`Nc1nc2c(ncn2[C@H]2O[C@H](CO)[C@@H](O)[C@@H]2O)c…`
ZINC2020098 ZINC	0.722	283.2 Da LogP -2.69 TPSA 159.5	✓ Ro5	✓ Clean	`Nc1nc2c(ncn2[C@H]2O[C@@H](CO)[C@H](O)[C@H]2O)c(…`
ZINC38580950 ZINC	0.722	282.3 Da LogP -2.72 TPSA 165.3	✓ Ro5	✓ Clean	`NC[C@H]1O[C@@H](n2cnc3c(=O)[nH]c(N)nc32)[C@H](O…`
ZINC3869967 ZINC	0.722	283.2 Da LogP -2.69 TPSA 159.5	✓ Ro5	✓ Clean	`Nc1nc2c(ncn2[C@H]2O[C@@H](CO)[C@@H](O)[C@H]2O)c…`
ZINC3869968 ZINC	0.722	283.2 Da LogP -2.69 TPSA 159.5	✓ Ro5	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@@H](CO)[C@@H](O)[C@H]2O)…`
ZINC3869969 ZINC	0.722	283.2 Da LogP -2.69 TPSA 159.5	✓ Ro5	✓ Clean	`Nc1nc2c(ncn2[C@H]2O[C@@H](CO)[C@@H](O)[C@@H]2O)…`
ZINC3869970 ZINC	0.722	283.2 Da LogP -2.69 TPSA 159.5	✓ Ro5	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@@H](CO)[C@@H](O)[C@@H]2O…`
ZINC4990799 ZINC	0.722	282.3 Da LogP -2.72 TPSA 165.3	✓ Ro5	✓ Clean	`NC[C@@H]1O[C@H](n2cnc3c(=O)[nH]c(N)nc32)[C@H](O…`
ZINC4990800 ZINC	0.722	282.3 Da LogP -2.72 TPSA 165.3	✓ Ro5	✓ Clean	`NC[C@@H]1O[C@@H](n2cnc3c(=O)[nH]c(N)nc32)[C@H](…`
ZINC4990801 ZINC	0.722	282.3 Da LogP -2.72 TPSA 165.3	✓ Ro5	✓ Clean	`NC[C@@H]1O[C@H](n2cnc3c(=O)[nH]c(N)nc32)[C@@H](…`
ZINC4990802 ZINC	0.722	282.3 Da LogP -2.72 TPSA 165.3	✓ Ro5	✓ Clean	`NC[C@@H]1O[C@@H](n2cnc3c(=O)[nH]c(N)nc32)[C@@H]…`
ZINC5605239 ZINC	0.722	283.2 Da LogP -2.69 TPSA 159.5	✓ Ro5	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@@H](CO)[C@H](O)[C@H]2O)c…`
ZINC6119283 ZINC	0.722	283.2 Da LogP -2.69 TPSA 159.5	✓ Ro5	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@H](CO)[C@H](O)[C@H]2O)c(…`
ZINC6585367 ZINC	0.722	283.2 Da LogP -2.69 TPSA 159.5	✓ Ro5	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@H](CO)[C@@H](O)[C@@H]2O)…`
ZINC8613125 ZINC	0.722	283.2 Da LogP -2.69 TPSA 159.5	✓ Ro5	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@H](CO)[C@H](O)[C@@H]2O)c…`
ZINC97973759 ZINC	0.722	282.3 Da LogP -2.72 TPSA 165.3	✓ Ro5	✓ Clean	`NC[C@H]1O[C@@H](n2cnc3c(=O)[nH]c(N)nc32)[C@H](O…`
ZINC97973760 ZINC	0.722	282.3 Da LogP -2.72 TPSA 165.3	✓ Ro5	✓ Clean	`NC[C@H]1O[C@@H](n2cnc3c(=O)[nH]c(N)nc32)[C@@H](…`
ZINC12501360 ZINC	0.689	363.2 Da LogP -2.57 TPSA 206.0	1 viol.	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@H](CO)[C@@H](O)[C@@H]2OP…`
ZINC100727895 ZINC	0.678	347.2 Da LogP -2.50 TPSA 196.8	1 viol.	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@H](CO)[C@@H](O)[C@H]2P(=…`
ZINC17610743 ZINC	0.678	347.2 Da LogP -2.50 TPSA 196.8	1 viol.	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@H](CO)[C@@H](O)[C@@H]2P(…`
ZINC38580951 ZINC	0.678	308.3 Da LogP -1.37 TPSA 188.0	✓ Ro5	Alert	`[N-]=[N+]=NC[C@H]1O[C@@H](n2cnc3c(=O)[nH]c(N)nc…`
ZINC5030599 ZINC	0.678	308.3 Da LogP -1.37 TPSA 188.0	✓ Ro5	Alert	`[N-]=[N+]=NC[C@@H]1O[C@H](n2cnc3c(=O)[nH]c(N)nc…`
ZINC5030600 ZINC	0.678	308.3 Da LogP -1.37 TPSA 188.0	✓ Ro5	Alert	`[N-]=[N+]=NC[C@@H]1O[C@@H](n2cnc3c(=O)[nH]c(N)n…`
ZINC5030605 ZINC	0.678	308.3 Da LogP -1.37 TPSA 188.0	✓ Ro5	Alert	`[N-]=[N+]=NC[C@@H]1O[C@H](n2cnc3c(=O)[nH]c(N)nc…`
ZINC5030606 ZINC	0.678	308.3 Da LogP -1.37 TPSA 188.0	✓ Ro5	Alert	`[N-]=[N+]=NC[C@@H]1O[C@@H](n2cnc3c(=O)[nH]c(N)n…`
ZINC38308095 ZINC	0.651	384.4 Da LogP -3.96 TPSA 178.5	2 viol.	✓ Clean	`CCCO[C@@H]1O[C@H](CO)[C@@H](O[C@@H]2O[C@H](CO)[…`
ZINC17420659 ZINC	0.650	297.3 Da LogP -2.03 TPSA 148.5	✓ Ro5	✓ Clean	`CO[C@H]1[C@@H](CO)O[C@@H](n2cnc3c(=O)[nH]c(N)nc…`
ZINC2522481 ZINC	0.650	297.3 Da LogP -2.03 TPSA 148.5	✓ Ro5	✓ Clean	`CO[C@H]1[C@H](CO)O[C@H](n2cnc3c(=O)[nH]c(N)nc32…`
ZINC4963099 ZINC	0.650	297.3 Da LogP -2.03 TPSA 148.5	✓ Ro5	✓ Clean	`CO[C@@H]1[C@H](CO)O[C@H](n2cnc3c(=O)[nH]c(N)nc3…`
ZINC4963101 ZINC	0.650	297.3 Da LogP -2.03 TPSA 148.5	✓ Ro5	✓ Clean	`CO[C@H]1[C@H](CO)O[C@H](n2cnc3c(=O)[nH]c(N)nc32…`
ZINC4963103 ZINC	0.650	297.3 Da LogP -2.03 TPSA 148.5	✓ Ro5	✓ Clean	`CO[C@@H]1[C@@H](CO)O[C@H](n2cnc3c(=O)[nH]c(N)nc…`
ZINC4963104 ZINC	0.650	297.3 Da LogP -2.03 TPSA 148.5	✓ Ro5	✓ Clean	`CO[C@H]1[C@@H](CO)O[C@H](n2cnc3c(=O)[nH]c(N)nc3…`
ZINC5998227 ZINC	0.650	297.3 Da LogP -2.03 TPSA 148.5	✓ Ro5	✓ Clean	`CO[C@@H]1[C@@H](CO)O[C@@H](n2cnc3c(=O)[nH]c(N)n…`
ZINC82188588 ZINC	0.650	297.3 Da LogP -2.03 TPSA 148.5	✓ Ro5	✓ Clean	`CO[C@H]1[C@H](O)[C@H](n2cnc3c(=O)[nH]c(N)nc32)O…`
ZINC82188589 ZINC	0.650	297.3 Da LogP -2.03 TPSA 148.5	✓ Ro5	✓ Clean	`CO[C@@H]1[C@H](O)[C@H](n2cnc3c(=O)[nH]c(N)nc32)…`
ZINC83290877 ZINC	0.650	297.3 Da LogP -2.03 TPSA 148.5	✓ Ro5	✓ Clean	`CO[C@@H]1[C@H](CO)O[C@H](n2cnc3c(=O)[nH]c(N)nc3…`
ZINC4743778 ZINC	0.636	437.4 Da LogP -0.97 TPSA 182.6	1 viol.	✓ Clean	`Cc1ccc(S(=O)(=O)OC[C@H]2O[C@@H](n3cnc4c(=O)[nH]…`
ZINC4743780 ZINC	0.636	437.4 Da LogP -0.97 TPSA 182.6	1 viol.	✓ Clean	`Cc1ccc(S(=O)(=O)OC[C@@H]2O[C@@H](n3cnc4c(=O)[nH…`
ZINC4743782 ZINC	0.636	437.4 Da LogP -0.97 TPSA 182.6	1 viol.	✓ Clean	`Cc1ccc(S(=O)(=O)OC[C@H]2O[C@@H](n3cnc4c(=O)[nH]…`
ZINC4743783 ZINC	0.636	437.4 Da LogP -0.97 TPSA 182.6	1 viol.	✓ Clean	`Cc1ccc(S(=O)(=O)OC[C@@H]2O[C@@H](n3cnc4c(=O)[nH…`
ZINC6585366 ZINC	0.627	285.2 Da LogP -1.71 TPSA 139.3	✓ Ro5	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@H](CO)[C@@H](F)[C@@H]2O)…`
ZINC78175055 ZINC	0.627	282.3 Da LogP -2.72 TPSA 165.3	✓ Ro5	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@H](CO)[C@@H](O)[C@H]2N)c…`
ZINC78175062 ZINC	0.627	282.3 Da LogP -2.72 TPSA 165.3	✓ Ro5	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@H](CO)[C@H](O)[C@@H]2N)c…`

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 A0A0H3GSM9