KpATCC43816 Protein target profile

excinuclease ABC subunit B

Accession: VK055_1726

Gene: AIK80346.1 uvrB 3D evidence: AlphaFold DB model + ColabFold model Metabolism Not in network UniProt A0A0H3GKA2

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Length 673

Pocket druggability (P2Rank · AlphaFold DB model) 0.91

Direct ligand evidence 0 56 total records

Functional annotation 0 EC 11 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. Second pocket predictor agrees P2Rank predicted binding-site probability 0.91. 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 (%): 33.036 Lower values reduce human off-target concern.
Human E-value: 6.73e-06
Gut microbiome similarity: 86.6% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 79.315 Higher values support similarity to known essential genes.
DEG E-value: 0.0 Smaller values mean stronger essential-gene similarity.

Structure confidence

ColabFold pLDDT: 87.86 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) 0.91

Structure A0A0H3GKA2

Pocket Pocket 1

Druggability (FPocket) 0.333

Structure A0A0H3GKA2

Pocket Pocket 43

ColabFold model

P2Rank 0.894 · Pocket 1

FPocket 0.895 · Pocket 37

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 4106 / 4744 genomes with a hit

Prevalence 86.6%

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.

MSKSFVLHSAFRPSGDQPEAIRRLEEGLEDGLAHQTLLGVTGSGKTFTIANVIADLQRPTMVLAPNKTLAAQLYGEMKEFFPENAVEYFVSYYDYYQPEAYVPSSDTFIEKDASVNEHIEQMRLSATKALLERRDVVVVASVSAIYGLGDPDLYLKMMLHLTVGMLIDQRAILRRLAELQYTRNDQAFQRGTFRVRGEVIDVFPAESDDIALRIELFDEEVERLSLFDPLTGHVEGTVPRYTIYPKTHYVTPRERIVQAMEEIKLELAERRKVLLANNKLLEEQRLTQRTQFDLEMMNELGYCSGIENYSRFLSGRGPGEPPPTLFDYLPADGLLVIDESHVTVPQIGGMYRGDRARKETLVEYGFRLPSALDNRPMKFEEFEALAPQTIYVSATPGAYELDKSGGEVVDQVVRPTGLLDPIIEVRPVATQVDDLLSEIRLRTAINERVLVTTLTKRMAEDLTEYLEEHGERVRYLHSDIDTVERMEIIRDLRLGEFDVLVGINLLREGLDMPEVSLVAILDADKEGFLRSERSLIQTIGRAARNVNGKAILYGDKITPSMAKAIGETERRREKQQRYNEEHGIVPQGLNKKVVDILQLGQGLAKTKAKGRGKAKAVEPAGLSAVDMTPKALQQKIHELEGQMMQHAQNLEFEEAAQIRDQLHQLRELFIAAS

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

11 GO

Subcellular localization

Localization: Cytoplasmic

Gene Ontology (GO)

GO:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
GO:0009380 Any of the protein complexes formed by the UvrABC excinuclease system, which carries out nucleotide excision repair. Three different complexes are formed by the 3 proteins as they proceed through the excision repair process. First a complex consisting of two A subunits and two B subunits bind DNA and unwind it around the damaged site. Then, the A subunits disassociate leaving behind a stable complex between B subunits and DNA. Now, subunit C binds to this B+DNA complex and causes subunit B to nick the DNA on one side of the complex while subunit C nicks the DNA on the other side of the complex. DNA polymerase I and DNA ligase can then repair the resulting gap.
GO:0003677 Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).
GO:0005515 Binding to a protein.
GO:0016787 Catalysis of the hydrolysis of various bonds, e.g. C-O, C-N, C-C, phosphoric anhydride bonds, etc.
GO:0016887 Catalysis of the reaction: ATP + H2O = ADP + H+ phosphate. ATP hydrolysis is used in some reactions as an energy source, for example to catalyze a reaction or drive transport against a concentration gradient.
GO:0006289 A DNA repair process in which a small region of the strand surrounding the damage is removed from the DNA helix as an oligonucleotide. The small gap left in the DNA helix is filled in by the sequential action of DNA polymerase and DNA ligase. Nucleotide excision repair recognizes a wide range of substrates, including damage caused by UV irradiation (pyrimidine dimers and 6-4 photoproducts) and chemicals (intrastrand cross-links and bulky adducts).
GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
GO:0009381 Catalysis of the hydrolysis of ester linkages within deoxyribonucleic acid at sites flanking regions of damaged DNA to which the Uvr ABC excinuclease complexes bind.
GO:0004386 Catalysis of the reaction: ATP + H2O = ADP + phosphate, to drive the unwinding of a DNA or RNA helix.
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.

46 records

Show feature table

Start	End	DB	Term	Name
625	669	SUPERFAMILY	SSF46600	C-terminal UvrC-binding domain of UvrB
625	669	InterPro	IPR036876	UVR domain superfamily
264	284	Coils	Coil	Coil
552	593	Pfam	PF12344	Ultra-violet resistance protein B
552	593	InterPro	IPR024759	UvrB, YAD/RRR-motif-containing domain
420	590	CDD	cd18790	SF2_C_UvrB
5	414	CDD	cd17916	DEXHc_UvrB
1	230	FunFam	G3DSA:3.40.50.300:FF:000401	UvrABC system protein B
441	544	Pfam	PF00271	Helicase conserved C-terminal domain
441	544	InterPro	IPR001650	Helicase, C-terminal
613	673	Gene3D	G3DSA:4.10.860.10	UVR domain
3	669	PANTHER	PTHR24029	UVRABC SYSTEM PROTEIN B
3	669	InterPro	IPR004807	UvrABC system, subunit B
636	656	Coils	Coil	Coil
9	425	SMART	SM00487	ultradead3
9	425	InterPro	IPR014001	Helicase superfamily 1/2, ATP-binding domain
633	668	ProSiteProfiles	PS50151	UVR domain profile.
633	668	InterPro	IPR001943	UVR domain
431	597	ProSiteProfiles	PS51194	Superfamilies 1 and 2 helicase C-terminal domain profile.
431	597	InterPro	IPR001650	Helicase, C-terminal
26	183	ProSiteProfiles	PS51192	Superfamilies 1 and 2 helicase ATP-binding type-1 domain profile.
26	183	InterPro	IPR014001	Helicase superfamily 1/2, ATP-binding domain
4	243	Gene3D	G3DSA:3.40.50.300	-
4	243	InterPro	IPR027417	P-loop containing nucleoside triphosphate hydrolase
269	414	Gene3D	G3DSA:3.40.50.300	-
269	414	InterPro	IPR027417	P-loop containing nucleoside triphosphate hydrolase
460	546	SMART	SM00490	helicmild6
460	546	InterPro	IPR001650	Helicase, C-terminal
5	415	SUPERFAMILY	SSF52540	P-loop containing nucleoside triphosphate hydrolases
5	415	InterPro	IPR027417	P-loop containing nucleoside triphosphate hydrolase
37	584	SUPERFAMILY	SSF52540	P-loop containing nucleoside triphosphate hydrolases
37	584	InterPro	IPR027417	P-loop containing nucleoside triphosphate hydrolase
634	667	Pfam	PF02151	UvrB/uvrC motif
634	667	InterPro	IPR001943	UVR domain
3	668	Hamap	MF_00204	UvrABC system protein B [uvrB].
3	668	InterPro	IPR004807	UvrABC system, subunit B
159	249	Pfam	PF17757	UvrB interaction domain
159	249	InterPro	IPR041471	UvrB, interaction domain
5	666	NCBIfam	TIGR00631	excinuclease ABC subunit UvrB
5	666	InterPro	IPR004807	UvrABC system, subunit B
16	92	Pfam	PF04851	Type III restriction enzyme, res subunit
16	92	InterPro	IPR006935	Helicase/UvrB, N-terminal
231	414	FunFam	G3DSA:3.40.50.300:FF:000477	UvrABC system protein B
415	590	FunFam	G3DSA:3.40.50.300:FF:000257	UvrABC system protein B
415	590	Gene3D	G3DSA:3.40.50.300	-
415	590	InterPro	IPR027417	P-loop containing nucleoside triphosphate hydrolase

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

0.91

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Surrounding area

Pocket 2 P2Rank #2

0.846

Likely same site as FPocket 43 4.7 Å 28 shared residues 88% of smaller site

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Surrounding area

Pocket 3 P2Rank #3

0.261

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Surrounding area

Pocket 4 P2Rank #4

0.086

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Surrounding area

Pocket 5 P2Rank #5

0.025

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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 #43

0.333 Unusual size

Likely same site as P2Rank 2 4.7 Å 28 shared residues 88% of smaller site

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Surrounding area

Residue sets

UniProt: Binding site:39-46

Binding pockets · P2Rank

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

Pocket 1 P2Rank #1

0.894

Likely same site as FPocket 30 1.4 Å 22 shared residues 100% of smaller site

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Surrounding area

Pocket 2 P2Rank #2

0.84

Likely same site as FPocket 37 5.2 Å 30 shared residues 97% of smaller site

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Surrounding area

Pocket 3 P2Rank #3

0.179

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Surrounding area

Pocket 4 P2Rank #4

0.054

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Surrounding area

Pocket 5 P2Rank #5

0.051

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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 #37

0.895 Unusual size

Likely same site as P2Rank 2 5.2 Å 30 shared residues 97% of smaller site

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Surrounding area

Pocket 2 FPocket #10

0.701

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Surrounding area

Pocket 3 FPocket #30

0.628 Unusual size

Likely same site as P2Rank 1 1.4 Å 22 shared residues 100% of smaller site

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Surrounding area

Pocket 4 FPocket #40

0.538 Unusual size

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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_A0A0H3GKA2	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold VK055_1726	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

ANP PDB via homolog 506.2 Da · LogP -2.06 · TPSA 281.9 Open detail RCSB PDB

BEF PDB via homolog Detail RCSB PDB

FLQ PDB via homolog Detail RCSB PDB

FLU PDB via homolog Detail RCSB PDB

IHP 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
ANP RCSB PDB	6L5N	Q9NR30	506.2 Da LogP -2.06 TPSA 281.9	3 viol.	✓ Clean	`c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)…`
BEF RCSB PDB	3PEW	P20449	66.0 Da LogP 0.88 TPSA 0.0	✓ Ro5	✓ Clean	`[Be-](F)(F)F`
FLQ RCSB PDB	2FDC	P56981	516.6 Da LogP 4.09 TPSA 134.2	1 viol.	✓ Clean	`CC(=O)NCCCCCCNC(=O)c1ccc2c(c1)C3(c4ccc(cc4Oc5c3…`
FLU RCSB PDB	2NMV	P37954	332.3 Da LogP 3.97 TPSA 87.7	✓ Ro5	✓ Clean	`c1ccc(c(c1)C2=C3C=CC(=O)C=C3Oc4c2ccc(c4)O)C(=O)O`
IHP RCSB PDB	3RRN	P20449	660.0 Da LogP -3.13 TPSA 400.6	3 viol.	✓ Clean	`C1(C(C(C(C(C1OP(=O)(O)O)OP(=O)(O)O)OP(=O)(O)O)O…`
M2A RCSB PDB	5ELX	P20449	560.4 Da LogP 0.16 TPSA 250.7	3 viol.	✓ Clean	`CNc1ccccc1C(=O)O[C@@H]2[C@@H]([C@@H](O[C@H]2n3c…`

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
ZINC3872582 ZINC	1.000	332.3 Da LogP 3.97 TPSA 87.7	✓ Ro5	✓ Clean	`O=C(O)c1ccccc1-c1c2ccc(=O)cc-2oc2cc(O)ccc12`
ZINC205587376 ZINC	0.821	474.5 Da LogP 3.91 TPSA 131.1	✓ Ro5	✓ Clean	`NCCCCCCNC(=O)c1ccc2c(c1)C1(OC2=O)c2ccc(O)cc2Oc2…`
ZINC12360002 ZINC	0.810	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)OP(=O…`
ZINC12360703 ZINC	0.810	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)OP(=O…`
ZINC12503599 ZINC	0.810	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)OP(=O…`
ZINC16546165 ZINC	0.810	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@H](CO[P@](=O)(O)OP(=O)(…`
ZINC31977053 ZINC	0.810	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO[P@](=O)(O)OP(=O)…`
ZINC4806433 ZINC	0.810	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)OP(=O…`
ZINC53683898 ZINC	0.810	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@@](=O)(O)OP(=…`
ZINC8586019 ZINC	0.810	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO[P@](=O)(O)OP(=O)…`
ZINC8586020 ZINC	0.810	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@@](=O)(O)OP(=…`
ZINC8586021 ZINC	0.810	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO[P@@](=O)(O)OP(=O…`
ZINC8586022 ZINC	0.810	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@@](=O)(O)OP(=…`
ZINC101257688 ZINC	0.807	489.5 Da LogP 4.04 TPSA 142.4	✓ Ro5	✓ Clean	`O=C(O)CCCCCNC(=O)c1ccc2c(c1)C1(OC2=O)c2ccc(O)cc…`
ZINC5030658 ZINC	0.771	376.3 Da LogP 3.67 TPSA 125.0	✓ Ro5	✓ Clean	`O=C(O)c1ccc(-c2c3ccc(=O)cc-3oc3cc(O)ccc23)c(C(=…`
ZINC4344388 ZINC	0.760	346.3 Da LogP 4.06 TPSA 76.7	✓ Ro5	✓ Clean	`COC(=O)c1ccccc1-c1c2ccc(=O)cc-2oc2cc(O)ccc12`
ZINC4582277 ZINC	0.756	304.3 Da LogP 3.98 TPSA 70.7	✓ Ro5	✓ Clean	`O=c1ccc2c(-c3ccccc3O)c3ccc(O)cc3oc-2c1`
ZINC5248684 ZINC	0.755	376.3 Da LogP 3.67 TPSA 125.0	✓ Ro5	✓ Clean	`O=C(O)c1ccc(C(=O)O)c(-c2c3ccc(=O)cc-3oc3cc(O)cc…`
ZINC13518964 ZINC	0.741	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C@H](…`
ZINC1532515 ZINC	0.741	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](COP(=O)(O)O)[C@H](O…`
ZINC1571045 ZINC	0.741	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C@@H]…`
ZINC1842158 ZINC	0.741	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](COP(=O)(O)O)[C@H](O…`
ZINC2046931 ZINC	0.741	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C@H](…`
ZINC2126310 ZINC	0.741	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@@H](…`
ZINC3201891 ZINC	0.741	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C@@H]…`
ZINC3201893 ZINC	0.741	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](COP(=O)(O)O)[C@@H](…`
ZINC3830180 ZINC	0.741	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](COP(=O)(O)O)[C@@H](…`
ZINC3860156 ZINC	0.741	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@@H](…`
ZINC3977897 ZINC	0.741	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@H](COP(=O)(O)O)[C@@H](O…`
ZINC4806442 ZINC	0.741	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@H](O…`
ZINC8613167 ZINC	0.741	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@H](O…`
ZINC4096224 ZINC	0.729	346.2 Da LogP -1.90 TPSA 191.9	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@](N)(=O)O)[C@@…`
ZINC12503850 ZINC	0.726	427.3 Da LogP -2.04 TPSA 229.4	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@](=O)(O)OS(=O)…`
ZINC141161066 ZINC	0.726	427.3 Da LogP -2.04 TPSA 229.4	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@](=O)(O)OS(=O)…`
ZINC141163786 ZINC	0.726	427.3 Da LogP -2.04 TPSA 229.4	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@](=O)(O)OS(=O)…`
ZINC4228246 ZINC	0.726	427.3 Da LogP -2.04 TPSA 229.4	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)OS(=O…`
ZINC13556870 ZINC	0.722	420.1 Da LogP -3.48 TPSA 261.0	1 viol.	✓ Clean	`O=P(O)(O)O[C@H]1[C@@H](O)[C@@H](O)[C@H](O)[C@@H…`
ZINC71789368 ZINC	0.722	420.1 Da LogP -3.48 TPSA 261.0	1 viol.	✓ Clean	`O=P(O)(O)O[C@H]1[C@H](OP(=O)(O)O)[C@@H](O)[C@H]…`
ZINC71792243 ZINC	0.722	420.1 Da LogP -3.48 TPSA 261.0	1 viol.	✓ Clean	`O=P(O)(O)O[C@H]1[C@H](O)[C@@H](O)[C@@H](O)[C@@H…`
ZINC205997784 ZINC	0.721	458.4 Da LogP 4.10 TPSA 153.9	✓ Ro5	Alert	`[N-]=[N+]=NCCCNC(=O)c1ccc2c(c1)C1(OC2=O)c2ccc(O…`
ZINC25762071 ZINC	0.720	362.3 Da LogP 3.13 TPSA 139.8	✓ Ro5	✓ Clean	`Nc1cc(C(=O)O)c(-c2c3ccc(=O)cc-3oc3cc(O)ccc23)cc…`
ZINC4344383 ZINC	0.717	288.3 Da LogP 4.27 TPSA 50.4	✓ Ro5	✓ Clean	`O=c1ccc2c(-c3ccccc3)c3ccc(O)cc3oc-2c1`
ZINC105372833 ZINC	0.712	345.3 Da LogP -1.93 TPSA 197.6	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(N)(N)=O)[C@H](O…`
ZINC105372837 ZINC	0.712	345.3 Da LogP -1.93 TPSA 197.6	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(N)(N)=O)[C@H](O…`
ZINC17107643 ZINC	0.712	345.3 Da LogP -1.93 TPSA 197.6	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(N)(N)=O)[C@@H](…`
ZINC204538551 ZINC	0.712	345.3 Da LogP -1.93 TPSA 197.6	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(N)(N)=O)[C@@H](…`
ZINC953075800 ZINC	0.712	474.5 Da LogP 3.91 TPSA 131.1	✓ Ro5	✓ Clean	`NCCCCCCNC(=O)c1ccc2c(c1)C(=O)OC21c2ccc(O)cc2Oc2…`
ZINC230495868 ZINC	0.707	413.4 Da LogP 3.03 TPSA 105.1	✓ Ro5	✓ Clean	`C#CCNC(=O)c1ccc2c(c1)C1(OC2=O)c2ccc(O)cc2Oc2cc(…`
ZINC100015959 ZINC	0.706	420.1 Da LogP -3.48 TPSA 261.0	1 viol.	✓ Clean	`O=P(O)(O)O[C@H]1[C@H](O)[C@@H](OP(=O)(O)O)[C@H]…`
ZINC1501016356 ZINC	0.706	420.1 Da LogP -3.48 TPSA 261.0	1 viol.	✓ Clean	`O=P(O)(O)OC1C(O)[C@H](OP(=O)(O)O)C(O)[C@H](OP(=…`

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 A0A0H3GKA2