KpKP13 Protein target profile

DNA polymerase IV

Accession: KP13_32224

Gene: dinB AHE46193.1 3D evidence: AlphaFold DB model + ColabFold model UniProt A0A0H3GN39

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Length 370

Pocket druggability (P2Rank · AlphaFold DB model) 0.557

Direct ligand evidence 0 85 total records

Functional annotation 1 EC 8 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

Independent pocket support: P2Rank + FPocket Both predictors report a high-scoring binding site (P2Rank 0.56, FPocket 0.79). Use the 3D pocket comparison to verify whether they identify the same site. Core gene across strains Marked as conserved by both pan-genome tools: Roary and CoreCruncher. Strong predicted binding pocket FPocket selected-pocket score 0.79. This is a computational pocket signal, not binding validation. Second pocket predictor agrees P2Rank predicted binding-site probability 0.56. 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: Hit
Human identity (%): 55.814 Lower values reduce human off-target concern.
Human E-value: 1.34e-10
Gut microbiome similarity: 3.2% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): N
DEG identity (%): 0.0 Higher values support similarity to known essential genes.

Structure confidence

ColabFold pLDDT: 92.65 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) 0.557

Structure A0A0H3GN39

Pocket Pocket 1

Druggability (FPocket) 0.791

Structure A0A0H3GN39

Pocket Pocket 2

ColabFold model

P2Rank 0.581 · Pocket 1

FPocket 0.776 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 153 / 4744 genomes with a hit

Prevalence 3.2%

Sequence

Primary amino-acid sequence viewer.

MKFASVFAMLYGYTVLSLTMRKIIHVDMDCFFAAVEMRDNPALRDIPLAIGGSRVQRGVISTANYPARKFGVRSAMPTATALKLCPHLTLLPGRFDAYKEASNHIREIFSRYTSRIEPLSLDEAYLDVSDSEHCHGSATLIAQEIRQTIERELRLTASAGVAPVKFLAKIASDMNKPNGQFVIAPHQVAEFVRALPLAKIPGVGKVSAAKLENMGLRTCGDVQNSDLAMLLKRFGKFGRILWERSHGIDEREIHNDRQRKSVGVERTLAEDIHEWPECEAIIENLYPELERRLAKVKPDLLIARQGIKLKFNDFQLTTQEHVWPRLNKEDLIATAHKAWDERRGGRGVRLVGLHVTLLDPQLERQLLLGI

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 8 GO

Subcellular localization

Localization: Cytoplasmic

Enzyme Commission (EC)

2.7.7.7

Gene Ontology (GO)

GO:0003887 Catalysis of the reaction: deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1); DNA-template-directed extension of the 3'-end of a DNA strand by one nucleotide at a time.
GO:0003684 Binding to damaged DNA.
GO:0006281 The process of restoring DNA after damage. Genomes are subject to damage by chemical and physical agents in the environment (e.g. UV and ionizing radiations, chemical mutagens, fungal and bacterial toxins, etc.) and by free radicals or alkylating agents endogenously generated in metabolism. DNA is also damaged because of errors during its replication. A variety of different DNA repair pathways have been reported that include direct reversal, base excision repair, nucleotide excision repair, photoreactivation, bypass, double-strand break repair pathway, and mismatch repair pathway.
GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
GO:0000287 Binding to a magnesium (Mg) ion.
GO:0006261 A DNA replication process that uses parental DNA as a template for the DNA-dependent DNA polymerases that synthesize the new strands.
GO:0042276 The conversion of DNA-damage induced single-stranded gaps into large molecular weight DNA after replication by using a specialized DNA polymerase or replication complex to insert a defined nucleotide across the lesion. This process does not remove the replication-blocking lesions and causes an increase in the endogenous mutation level. For example, in E. coli, a low fidelity DNA polymerase, pol V, copies lesions that block replication fork progress. This produces mutations specifically targeted to DNA template damage sites, but it can also produce mutations at undamaged sites.
GO:0009432 An error-prone process for repairing damaged microbial DNA.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

32 records

Show feature table

Start	End	DB	Term	Name
40	92	FunFam	G3DSA:3.40.1170.60:FF:000001	DNA polymerase IV
23	204	ProSiteProfiles	PS50173	UmuC domain profile.
23	204	InterPro	IPR001126	UmuC domain
26	173	Pfam	PF00817	impB/mucB/samB family
26	173	InterPro	IPR001126	UmuC domain
11	17	Phobius	SIGNAL_PEPTIDE_C_REGION	C-terminal region of a signal peptide.
259	366	Pfam	PF11799	impB/mucB/samB family C-terminal domain
259	366	InterPro	IPR017961	DNA polymerase, Y-family, little finger domain
1	2	Phobius	SIGNAL_PEPTIDE_N_REGION	N-terminal region of a signal peptide.
3	10	Phobius	SIGNAL_PEPTIDE_H_REGION	Hydrophobic region of a signal peptide.
18	370	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
40	92	Gene3D	G3DSA:3.40.1170.60	-
20	360	PANTHER	PTHR11076	DNA REPAIR POLYMERASE UMUC / TRANSFERASE FAMILY MEMBER
87	184	FunFam	G3DSA:3.30.70.270:FF:000002	DNA polymerase IV
188	216	Pfam	PF11798	IMS family HHH motif
188	216	InterPro	IPR024728	DNA polymerase type-Y, HhH motif
20	368	Hamap	MF_01113	DNA polymerase IV [dinB].
20	368	InterPro	IPR022880	DNA polymerase IV
260	370	Gene3D	G3DSA:3.30.1490.100	-
260	370	InterPro	IPR036775	DNA polymerase, Y-family, little finger domain superfamily
24	358	CDD	cd03586	PolY_Pol_IV_kappa
24	358	InterPro	IPR022880	DNA polymerase IV
260	370	FunFam	G3DSA:3.30.1490.100:FF:000002	DNA polymerase IV
23	184	Gene3D	G3DSA:3.30.70.270	-
23	184	InterPro	IPR043128	Reverse transcriptase/Diguanylate cyclase domain
1	17	Phobius	SIGNAL_PEPTIDE	Signal peptide region
186	247	FunFam	G3DSA:1.10.150.20:FF:000019	DNA polymerase IV
260	368	SUPERFAMILY	SSF100879	Lesion bypass DNA polymerase (Y-family), little finger domain
260	368	InterPro	IPR036775	DNA polymerase, Y-family, little finger domain superfamily
19	253	SUPERFAMILY	SSF56672	DNA/RNA polymerases
19	253	InterPro	IPR043502	DNA/RNA polymerase superfamily
185	246	Gene3D	G3DSA:1.10.150.20	-

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

0.557

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Surrounding area

Pocket 2 P2Rank #2

0.133

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Surrounding area

Pocket 3 P2Rank #3

0.029

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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 #2

0.791

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Surrounding area

Residue sets

UniProt: Active site:104-104

UniProt: Binding site:103-103

UniProt: Binding site:8-8

UniProt: Site:13-13 Substrate discrimination

Binding pockets · P2Rank

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

Pocket 1 P2Rank #1

0.581

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Surrounding area

Pocket 2 P2Rank #2

0.101

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Surrounding area

Pocket 3 P2Rank #3

0.047

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Surrounding area

Pocket 4 P2Rank #4

0.006

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Surrounding area

Pocket 5 P2Rank #5

0.006

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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_A0A0H3GN39	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold KP13_32224	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.

85 records

Chemistry signal

Structural and bioactivity evidence are both available for this target.

Direct evidence 0 same-protein records

Transferred evidence 35 records from similar proteins

Structural ligands 32 0 loaded crystals

Measured bioactivity 3 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

0G4 PDB via homolog 486.2 Da · LogP -0.53 · TPSA 232.8 Open detail RCSB PDB

0G8 PDB via homolog Detail RCSB PDB

0KX PDB via homolog Detail RCSB PDB

0OH PDB via homolog Detail RCSB PDB

0OJ 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
0G4 RCSB PDB	4QW9	Q97W02	486.2 Da LogP -0.53 TPSA 232.8	2 viol.	✓ Clean	`C1[C@H](O[C@H](S1)COP(=O)(O)OP(=O)(NP(=O)(O)O)O…`
0G8 RCSB PDB	4QWA	Q97W02	389.2 Da LogP -0.36 TPSA 183.4	✓ Ro5	✓ Clean	`C1[C@H](O[C@H](S1)COP(=O)(O)OP(=O)(O)O)N2C=CC(=…`
0KX RCSB PDB	4IRC	Q47155	466.2 Da LogP -1.61 TPSA 253.0	2 viol.	✓ Clean	`C1[C@@H]([C@H](O[C@H]1N2C=CC(=NC2=O)N)COP(=O)(N…`
0OH RCSB PDB	4EBC	Q9UNA4	501.2 Da LogP 0.06 TPSA 249.7	3 viol.	✓ Clean	`c1nc(c2c(n1)n(cn2)[C@H]3C[C@@H]([C@]4([C@@H]3C4…`
0OJ RCSB PDB	4EBD	Q9UNA4	501.2 Da LogP -0.15 TPSA 249.7	3 viol.	✓ Clean	`c1nc(c2c(n1)n(cn2)[C@]34C[C@H]3[C@@H]([C@H](C4)…`
1FZ RCSB PDB	4IR1	Q47155	481.2 Da LogP -1.59 TPSA 246.9	1 viol.	✓ Clean	`CC1=CN(C(=O)NC1=O)[C@H]2C[C@@H]([C@H](O2)COP(=O…`
2LF RCSB PDB	4TQS	Q97W02	345.2 Da LogP -1.49 TPSA 185.8	✓ Ro5	✓ Clean	`C1[C@@H]([C@H]2[C@H](c3nc4c(n3[C@@H]1O2)N=C(NC4…`
2TM RCSB PDB	6JUQ	Q47155	481.2 Da LogP -2.10 TPSA 261.2	2 viol.	✓ Clean	`C1=CN(C(=O)N=C1N)[C@H]2[C@@H]([C@@H]([C@H](O2)C…`
3TT RCSB PDB	4QWD	Q97W02	468.2 Da LogP -0.67 TPSA 232.8	2 viol.	✓ Clean	`C1[C@H](O[C@H](S1)COP(=O)(O)OP(=O)(NP(=O)(O)O)O…`
8GT RCSB PDB	5C5J	Q47155	539.2 Da LogP -3.04 TPSA 319.1	3 viol.	✓ Clean	`C([C@@H]1[C@H]([C@H]([C@@H](O1)N2C3=C(C(=O)NC(=…`
A38 RCSB PDB	6VG6	Q97W02	347.2 Da LogP -1.54 TPSA 185.8	✓ Ro5	✓ Clean	`c1nc(c2c(n1)N(C(=O)N2)[C@H]3C[C@@H]([C@H](O3)CO…`
ADI RCSB PDB	3GV5	Q9UNA4	395.2 Da LogP 0.31 TPSA 192.1	✓ Ro5	✓ Clean	`c1nc(c2c(n1)n(cn2)[C@H]3CC[C@H](O3)CO[P@@](=O)(…`
AF RCSB PDB	3KHH	Q97W02	181.2 Da LogP 2.84 TPSA 26.0	✓ Ro5	✓ Clean	`c1ccc-2c(c1)Cc3c2ccc(c3)N`
BAP RCSB PDB	2IBK	Q97W02	304.3 Da LogP 2.90 TPSA 60.7	✓ Ro5	✓ Clean	`c1cc2ccc3cc4c(c5c3c2c(c1)cc5)C[C@H]([C@H]([C@@H…`
DCP RCSB PDB	3GQC	Q9UBZ9	467.2 Da LogP -1.18 TPSA 250.2	2 viol.	✓ Clean	`C1[C@@H]([C@H](O[C@H]1N2C=CC(=NC2=O)N)CO[P@@](=…`
DCT RCSB PDB	1S97	Q97W02	451.2 Da LogP -0.15 TPSA 230.0	1 viol.	✓ Clean	`C1C[C@@H](O[C@@H]1CO[P@](=O)(O)O[P@](=O)(O)OP(=…`
DDS RCSB PDB	2IMW	Q97W02	475.2 Da LogP 0.43 TPSA 238.7	1 viol.	✓ Clean	`c1nc(c2c(n1)n(cn2)[C@H]3CC[C@H](O3)CO[P@@](=O)(…`
DDY RCSB PDB	1S9F	Q97W02	371.2 Da LogP -0.27 TPSA 183.4	✓ Ro5	✓ Clean	`C1C[C@@H](O[C@@H]1CO[P@@](=O)(O)OP(=O)(O)O)N2C=…`
DG3 RCSB PDB	1JXL	Q97W02	491.2 Da LogP -0.28 TPSA 258.6	2 viol.	✓ Clean	`c1nc2c(n1[C@H]3CC[C@H](O3)CO[P@@](=O)(O)O[P@](=…`
DGT RCSB PDB	2AGP	Q97W02	507.2 Da LogP -1.31 TPSA 278.9	3 viol.	✓ Clean	`c1nc2c(n1[C@H]3C[C@@H]([C@H](O3)CO[P@@](=O)(O)O…`
DOC RCSB PDB	4TQS	Q97W02	291.2 Da LogP -0.39 TPSA 136.9	✓ Ro5	✓ Clean	`C1C[C@@H](O[C@@H]1COP(=O)(O)O)N2C=CC(=NC2=O)N`
DPO RCSB PDB	5YUZ	Q47155	173.9 Da LogP -3.34 TPSA 135.6	✓ Ro5	✓ Clean	`[O-]P(=O)([O-])OP(=O)([O-])[O-]`
DT RCSB PDB	6VG6	Q97W02	322.2 Da LogP -1.40 TPSA 151.1	✓ Ro5	✓ Clean	`CC1=CN(C(=O)NC1=O)[C@H]2C[C@@H]([C@H](O2)COP(=O…`
DTP RCSB PDB	1S0M	Q97W02	491.2 Da LogP -0.60 TPSA 258.9	2 viol.	✓ Clean	`c1nc(c2c(n1)n(cn2)[C@H]3C[C@@H]([C@H](O3)CO[P@]…`
DZ4 RCSB PDB	6VKP	Q97W02	490.2 Da LogP -1.03 TPSA 261.7	2 viol.	✓ Clean	`c1nc(c2c(n1)n(cn2)[C@H]3C[C@@H]([C@H](O3)CO[P@@…`
FTD RCSB PDB	4QWE	Q97W02	409.2 Da LogP -0.25 TPSA 180.9	✓ Ro5	✓ Clean	`C1[C@H](O[C@H](S1)COP(=O)(O)OP(=O)(O)O)N2CC(=C(…`
LTP RCSB PDB	4QWC	Q97W02	387.2 Da LogP -1.30 TPSA 203.7	✓ Ro5	✓ Clean	`C1[C@H]([C@@H](O[C@@H]1N2C=CC(=NC2=O)N)COP(=O)(…`
POP RCSB PDB	2AGO	Q97W02	176.0 Da LogP -2.08 TPSA 129.9	✓ Ro5	✓ Clean	`O[P@@](=O)([O-])O[P@@](=O)(O)[O-]`
TTP RCSB PDB	1S0O	Q97W02	482.2 Da LogP -1.16 TPSA 244.1	2 viol.	✓ Clean	`CC1=CN(C(=O)NC1=O)[C@H]2C[C@@H]([C@H](O2)CO[P@]…`
TTW RCSB PDB	5YYD	Q47155	481.2 Da LogP -1.59 TPSA 246.9	1 viol.	✓ Clean	`CC1=CN(C(=O)NC1=O)[C@H]2C[C@@H]([C@H](O2)COP(=O…`
XG4 RCSB PDB	6VG6	Q97W02	506.2 Da LogP -1.73 TPSA 281.7	3 viol.	✓ Clean	`c1nc2c(n1[C@H]3C[C@@H]([C@H](O3)CO[P@@](=O)(N[P…`
YYY RCSB PDB	4QWB	Q97W02	387.2 Da LogP -1.30 TPSA 203.7	✓ Ro5	✓ Clean	`C1[C@@H]([C@H](O[C@H]1N2C=CC(=NC2=O)N)CO[P@@](=…`

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
CHEMBL1529592 ChEMBL	Q9UNA4	—	304.3 Da LogP 3.57 TPSA 43.4	✓ Ro5	✓ Clean	`C=CCOC(=O)C(=O)/C=C/c1ccc2c(c1)Cc1ccccc1-2`
CHEMBL1715183 ChEMBL	Q9UNA4	—	803.9 Da LogP 4.01 TPSA 236.7	3 viol.	✓ Clean	`CCCCCCCCCCCCCCCCCCNc1ccn(C2OC(COP(=O)(O)OCC3OC(…`
CHEMBL417727 ChEMBL	Q9UNA4	—	223.2 Da LogP 2.31 TPSA 60.2	✓ Ro5	Alert	`Nc1ccc2c(c1)C(=O)C(=O)c1ccccc1-2`

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
ZINC12503365 ZINC	1.000	467.2 Da LogP -1.18 TPSA 250.2	2 viol.	✓ Clean	`Nc1ccn([C@H]2C[C@@H](O)[C@@H](CO[P@](=O)(O)O[P@…`
ZINC13434879 ZINC	1.000	491.2 Da LogP -0.60 TPSA 258.9	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1C[C@H](O)[C@H](CO[P@@](=O)…`
ZINC13434881 ZINC	1.000	491.2 Da LogP -0.60 TPSA 258.9	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1C[C@H](O)[C@H](CO[P@@](=O)(…`
ZINC13434883 ZINC	1.000	491.2 Da LogP -0.60 TPSA 258.9	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1C[C@@H](O)[C@H](CO[P@@](=O…`
ZINC13434884 ZINC	1.000	491.2 Da LogP -0.60 TPSA 258.9	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1C[C@@H](O)[C@H](CO[P@@](=O)…`
ZINC13435050 ZINC	1.000	467.2 Da LogP -1.18 TPSA 250.2	2 viol.	✓ Clean	`Nc1ccn([C@@H]2C[C@H](O)[C@H](CO[P@@](=O)(O)O[P@…`
ZINC13507072 ZINC	1.000	482.2 Da LogP -1.16 TPSA 244.1	2 viol.	✓ Clean	`Cc1cn([C@@H]2C[C@@H](O)[C@H](CO[P@@](=O)(O)O[P@…`
ZINC1713558 ZINC	1.000	223.2 Da LogP 2.31 TPSA 60.2	✓ Ro5	Alert	`Nc1ccc2c(c1)C(=O)C(=O)c1ccccc1-2`
ZINC33979251 ZINC	1.000	482.2 Da LogP -1.16 TPSA 244.1	2 viol.	✓ Clean	`Cc1cn([C@@H]2C[C@H](O)[C@H](CO[P@@](=O)(O)O[P@@…`
ZINC8215662 ZINC	1.000	491.2 Da LogP -0.60 TPSA 258.9	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1C[C@H](O)[C@@H](CO[P@@](=O)…`
ZINC8215945 ZINC	1.000	467.2 Da LogP -1.18 TPSA 250.2	2 viol.	✓ Clean	`Nc1ccn([C@H]2C[C@H](O)[C@@H](CO[P@@](=O)(O)O[P@…`
ZINC8664605 ZINC	1.000	491.2 Da LogP -0.60 TPSA 258.9	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1C[C@H](O)[C@@H](CO[P@@](=O…`
ZINC12503703 ZINC	0.982	427.2 Da LogP -1.42 TPSA 232.3	2 viol.	✓ Clean	`Nc1nc2c(ncn2[C@@H]2C[C@H](O)[C@@H](CO[P@@](=O)(…`
ZINC8215878 ZINC	0.982	427.2 Da LogP -1.42 TPSA 232.3	2 viol.	✓ Clean	`Nc1nc2c(ncn2[C@H]2C[C@H](O)[C@@H](CO[P@@](=O)(O…`
ZINC12495199 ZINC	0.981	411.2 Da LogP -0.72 TPSA 212.4	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1C[C@H](O)[C@@H](CO[P@@](=O…`
ZINC12501706 ZINC	0.981	475.2 Da LogP 0.43 TPSA 238.7	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1CC[C@@H](CO[P@](=O)(O)O[P@@…`
ZINC12501708 ZINC	0.981	475.2 Da LogP 0.43 TPSA 238.7	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1CC[C@H](CO[P@@](=O)(O)O[P@…`
ZINC13434873 ZINC	0.981	411.2 Da LogP -0.72 TPSA 212.4	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1C[C@H](O)[C@H](CO[P@@](=O)…`
ZINC13434875 ZINC	0.981	411.2 Da LogP -0.72 TPSA 212.4	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1C[C@H](O)[C@H](CO[P@@](=O)(…`
ZINC13434876 ZINC	0.981	411.2 Da LogP -0.72 TPSA 212.4	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1C[C@@H](O)[C@H](CO[P@](=O)…`
ZINC13434878 ZINC	0.981	411.2 Da LogP -0.72 TPSA 212.4	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1C[C@@H](O)[C@H](CO[P@@](=O)…`
ZINC8215728 ZINC	0.981	411.2 Da LogP -0.72 TPSA 212.4	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1C[C@H](O)[C@@H](CO[P@@](=O)…`
ZINC12503053 ZINC	0.959	402.2 Da LogP -1.28 TPSA 197.6	✓ Ro5	✓ Clean	`Cc1cn([C@@H]2C[C@H](O)[C@@H](CO[P@@](=O)(O)OP(=…`
ZINC13435042 ZINC	0.959	387.2 Da LogP -1.30 TPSA 203.7	✓ Ro5	✓ Clean	`Nc1ccn([C@@H]2C[C@H](O)[C@H](CO[P@](=O)(O)OP(=O…`
ZINC14960508 ZINC	0.959	387.2 Da LogP -1.30 TPSA 203.7	✓ Ro5	✓ Clean	`Nc1ccn([C@@H]2C[C@H](O)[C@@H](CO[P@](=O)(O)OP(=…`
ZINC33979243 ZINC	0.959	402.2 Da LogP -1.28 TPSA 197.6	✓ Ro5	✓ Clean	`Cc1cn([C@@H]2C[C@H](O)[C@H](CO[P@@](=O)(O)OP(=O…`
ZINC33979244 ZINC	0.959	402.2 Da LogP -1.28 TPSA 197.6	✓ Ro5	✓ Clean	`Cc1cn([C@H]2C[C@H](O)[C@H](CO[P@@](=O)(O)OP(=O)…`
ZINC33979245 ZINC	0.959	402.2 Da LogP -1.28 TPSA 197.6	✓ Ro5	✓ Clean	`Cc1cn([C@@H]2C[C@@H](O)[C@H](CO[P@@](=O)(O)OP(=…`
ZINC33979246 ZINC	0.959	402.2 Da LogP -1.28 TPSA 197.6	✓ Ro5	✓ Clean	`Cc1cn([C@H]2C[C@@H](O)[C@H](CO[P@@](=O)(O)OP(=O…`
ZINC8215882 ZINC	0.959	402.2 Da LogP -1.28 TPSA 197.6	✓ Ro5	✓ Clean	`Cc1cn([C@H]2C[C@H](O)[C@@H](CO[P@@](=O)(O)OP(=O…`
ZINC3874029 ZINC	0.870	223.2 Da LogP 2.04 TPSA 60.2	✓ Ro5	Alert	`Nc1ccc2c(c1)C(=O)c1ccccc1C2=O`
ZINC12296728 ZINC	0.845	347.2 Da LogP -1.54 TPSA 185.8	✓ Ro5	✓ Clean	`Nc1nc2c(ncn2[C@H]2C[C@@H](O)[C@@H](COP(=O)(O)O)…`
ZINC13527599 ZINC	0.845	347.2 Da LogP -1.54 TPSA 185.8	✓ Ro5	✓ Clean	`Nc1nc2c(ncn2[C@@H]2C[C@@H](O)[C@@H](COP(=O)(O)O…`
ZINC13527603 ZINC	0.845	347.2 Da LogP -1.54 TPSA 185.8	✓ Ro5	✓ Clean	`Nc1nc2c(ncn2[C@@H]2C[C@H](O)[C@@H](COP(=O)(O)O)…`
ZINC1532627 ZINC	0.845	347.2 Da LogP -1.54 TPSA 185.8	✓ Ro5	✓ Clean	`Nc1nc2c(ncn2[C@@H]2C[C@@H](O)[C@H](COP(=O)(O)O)…`
ZINC1730395 ZINC	0.845	347.2 Da LogP -1.54 TPSA 185.8	✓ Ro5	✓ Clean	`Nc1nc2c(ncn2[C@H]2C[C@H](O)[C@@H](COP(=O)(O)O)O…`
ZINC3869846 ZINC	0.845	347.2 Da LogP -1.54 TPSA 185.8	✓ Ro5	✓ Clean	`Nc1nc2c(ncn2[C@@H]2C[C@H](O)[C@H](COP(=O)(O)O)O…`
ZINC3869847 ZINC	0.845	347.2 Da LogP -1.54 TPSA 185.8	✓ Ro5	✓ Clean	`Nc1nc2c(ncn2[C@H]2C[C@H](O)[C@H](COP(=O)(O)O)O2…`
ZINC3869848 ZINC	0.845	347.2 Da LogP -1.54 TPSA 185.8	✓ Ro5	✓ Clean	`Nc1nc2c(ncn2[C@H]2C[C@@H](O)[C@H](COP(=O)(O)O)O…`
ZINC196576711 ZINC	0.842	490.2 Da LogP -0.63 TPSA 264.7	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1C[C@H](N)[C@H](CO[P@@](=O)…`
ZINC111459735 ZINC	0.836	481.2 Da LogP -1.20 TPSA 249.9	2 viol.	✓ Clean	`Cc1cn([C@@H]2C[C@H](N)[C@H](CO[P@@](=O)(O)O[P@@…`
ZINC138164075 ZINC	0.836	498.2 Da LogP 0.21 TPSA 227.1	2 viol.	✓ Clean	`Cc1cn([C@@H]2C[C@H](O)[C@H](CO[P@@](=O)(O)O[P@@…`
ZINC90741958 ZINC	0.836	347.2 Da LogP 1.01 TPSA 134.6	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1CC[C@H](CO[P@@](=O)(O)OP)O1`
ZINC90741960 ZINC	0.836	347.2 Da LogP 1.01 TPSA 134.6	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1CC[C@@H](CO[P@@](=O)(O)OP)…`
ZINC12958401 ZINC	0.833	331.2 Da LogP -0.83 TPSA 165.8	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1C[C@@H](O)[C@@H](COP(=O)(O)…`
ZINC13538980 ZINC	0.833	331.2 Da LogP -0.83 TPSA 165.8	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1C[C@@H](O)[C@@H](COP(=O)(O…`
ZINC1532626 ZINC	0.833	331.2 Da LogP -0.83 TPSA 165.8	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1C[C@@H](O)[C@H](COP(=O)(O)…`
ZINC3869813 ZINC	0.833	331.2 Da LogP -0.83 TPSA 165.8	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1C[C@H](O)[C@H](COP(=O)(O)O…`
ZINC3869814 ZINC	0.833	331.2 Da LogP -0.83 TPSA 165.8	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1C[C@H](O)[C@H](COP(=O)(O)O)…`
ZINC3869815 ZINC	0.833	331.2 Da LogP -0.83 TPSA 165.8	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1C[C@@H](O)[C@H](COP(=O)(O)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.

Cross-references

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

Sequence

UniProt A0A0H3GN39

Chemistry

ChEMBL CHEMBL1529592 ChEMBL CHEMBL1715183 ChEMBL CHEMBL417727