KpKP13 Protein target profile

Adenylosuccinate lyase

Accession: KP13_04866

Gene: AHE45226.1 purB 3D evidence: AlphaFold DB model + ColabFold model UniProt A0A0H3GVM8

Export view

Length 456

Pocket druggability (P2Rank · AlphaFold DB model) 0.116

Direct ligand evidence 0 57 total records

Functional annotation 1 EC 8 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. Structure available AlphaFold DB model + ColabFold model Ligand evidence via structure/bioactivity 7 structural and 0 bioactivity records.

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 (%): 23.247 Lower values reduce human off-target concern.
Human E-value: 5.01e-07
Gut microbiome similarity: 12.6% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 94.079 Higher values support similarity to known essential genes.
DEG E-value: 0.0 Smaller values mean stronger essential-gene similarity.

Structure confidence

ColabFold pLDDT: 97.82 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) 0.116

Structure A0A0H3GVM8

Pocket Pocket 1

Druggability (FPocket) 0.248

Structure A0A0H3GVM8

Pocket Pocket 3

ColabFold model

P2Rank 0.071 · Pocket 1

FPocket 0.145 · Pocket 7

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 598 / 4744 genomes with a hit

Prevalence 12.6%

Sequence

Primary amino-acid sequence viewer.

MELSSLTAVSPVDGRYGDKVSALRGIFSEFGLLKFRVQVEVRWLQKLAAHAAIKEVPAFAADANGFLDKIVADFSVEDAERIKTIERTTNHDVKAVEYFLKEKVADVAELHAVSEFIHFACTSEDINNLSHALMLKTARDEVVLPYWRKLIDAVKDLATQYRDVPLLSRTHGQPATPSTMGKEMANVAYRMERQYRQLNQVEILGKINGAVGNYNAHIAAYPEVDWHQFSEEFVTSLGIQWNPYTTQIEPHDYIAELFDCIARFNTILIDFDRDVWGYIALNHFKQKTIAGEIGSSTMPHKVNPIDFENSEGNLGLANAVMQHLASKLPVSRWQRDLTDSTVLRNLGVGIGYALIAYQSTLKGISKLELNQDRLLDELDHNWEVLAEPIQTVMRRYGIEKPYEKLKELTRGKRVDAEGMKQFIDSLALPEEEKVRLKAMTPANYIGRATTMVDELK

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 8 GO

Subcellular localization

Localization: Cytoplasmic

Enzyme Commission (EC)

4.3.2.2

Gene Ontology (GO)

GO:0009152 The chemical reactions and pathways resulting in the formation of a purine ribonucleotide, a compound consisting of ribonucleoside (a purine base linked to a ribose sugar) esterified with a phosphate group at either the 3' or 5'-hydroxyl group of the sugar.
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:0004018 Catalysis of the reaction: N6-(1,2-dicarboxyethyl)AMP = fumarate + AMP.
GO:0006188 The chemical reactions and pathways resulting in the formation of IMP, inosine monophosphate.
GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
GO:0070626 Catalysis of the reaction: (S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido)succinate = fumarate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide.
GO:0044208 The chemical reactions and pathways resulting in the formation of adenosine monophosphate (AMP) from inosine 5'-monophosphate (IMP).
GO:0006189 The chemical reactions and pathways resulting in the formation of IMP, inosine monophosphate, by the stepwise assembly of a purine ring on ribose 5-phosphate.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

28 records

Show feature table

Start	End	DB	Term	Name
12	455	NCBIfam	TIGR00928	adenylosuccinate lyase
12	455	InterPro	IPR004769	Adenylosuccinate lyase
23	446	CDD	cd01598	PurB
294	303	ProSitePatterns	PS00163	Fumarate lyases signature.
294	303	InterPro	IPR020557	Fumarate lyase, conserved site
14	312	Pfam	PF00206	Lyase
14	312	InterPro	IPR022761	Fumarate lyase, N-terminal
382	445	Gene3D	G3DSA:1.10.40.30	-
118	384	FunFam	G3DSA:1.20.200.10:FF:000004	Adenylosuccinate lyase
118	449	Gene3D	G3DSA:1.20.200.10	Fumarase/aspartase (Central domain)
382	445	FunFam	G3DSA:1.10.40.30:FF:000004	Adenylosuccinate lyase
10	454	SUPERFAMILY	SSF48557	L-aspartase-like
10	454	InterPro	IPR008948	L-Aspartase-like
163	181	PRINTS	PR00149	Fumarate lyase superfamily signature
163	181	InterPro	IPR000362	Fumarate lyase family
294	310	PRINTS	PR00149	Fumarate lyase superfamily signature
294	310	InterPro	IPR000362	Fumarate lyase family
117	135	PRINTS	PR00149	Fumarate lyase superfamily signature
117	135	InterPro	IPR000362	Fumarate lyase family
251	278	PRINTS	PR00149	Fumarate lyase superfamily signature
251	278	InterPro	IPR000362	Fumarate lyase family
1	117	Gene3D	G3DSA:1.10.275.10	-
1	117	InterPro	IPR024083	Fumarase/histidase, N-terminal
331	445	Pfam	PF08328	Adenylosuccinate lyase C-terminal
331	445	InterPro	IPR013539	Adenylosuccinate lyase PurB, C-terminal
1	117	FunFam	G3DSA:1.10.275.10:FF:000003	Adenylosuccinate lyase
2	454	PANTHER	PTHR43411	ADENYLOSUCCINATE LYASE
2	454	InterPro	IPR047136	Adenylosuccinate lyase PurB, bacteria

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.

Download VMD script Full viewer

Loading 3D structure...

Drag to rotate — click the view, then scroll to zoom.

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

0.116

Show in viewer

Surrounding area

Pocket 2 P2Rank #2

0.04

Show in viewer

Surrounding area

Pocket 3 P2Rank #3

0.035

Show in viewer

Surrounding area

Pocket 4 P2Rank #4

0.019

Show in viewer

Surrounding area

Pocket 5 P2Rank #5

0.015

Show in viewer

Surrounding area

Binding pockets · FPocket

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

Pocket 1 FPocket #3

0.248

Show in viewer

Surrounding area

Binding pockets · P2Rank

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

Pocket 1 P2Rank #1

0.071

Show in viewer

Surrounding area

Pocket 2 P2Rank #2

0.068

Show in viewer

Surrounding area

Pocket 3 P2Rank #3

0.056

Show in viewer

Surrounding area

Pocket 4 P2Rank #4

0.048

Show in viewer

Surrounding area

Pocket 5 P2Rank #5

0.007

Show in viewer

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_A0A0H3GVM8	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold KP13_04866	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

2SA PDB via homolog 463.3 Da · LogP -2.11 · TPSA 246.7 Open detail RCSB PDB

DTT PDB via homolog Detail RCSB PDB

FUM PDB via homolog Detail RCSB PDB

MLI PDB via homolog Detail RCSB PDB

N2P 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
2SA RCSB PDB	2PTR	P0AB89	463.3 Da LogP -2.11 TPSA 246.7	2 viol.	✓ Clean	`c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)…`
DTT RCSB PDB	1RE5	Q88N37	154.3 Da LogP -0.43 TPSA 40.5	✓ Ro5	✓ Clean	`C([C@@H]([C@H](CS)O)O)S`
FUM RCSB PDB	2PTQ	P0AB89	116.1 Da LogP -0.29 TPSA 74.6	✓ Ro5	✓ Clean	`C(=C/C(=O)O)\C(=O)O`
MLI RCSB PDB	2PFM	A0A6L8PR48	102.0 Da LogP -3.12 TPSA 80.3	✓ Ro5	✓ Clean	`C(C(=O)[O-])C(=O)[O-]`
N2P RCSB PDB	4NSL	Q8ZPZ6	102.2 Da LogP 0.07 TPSA 52.0	✓ Ro5	✓ Clean	`C(CCN)CCN`
OXL RCSB PDB	2X75	Q7A0G9	88.0 Da LogP -3.51 TPSA 80.3	✓ Ro5	✓ Clean	`C(=O)(C(=O)[O-])[O-]`
SIN RCSB PDB	4EEI	Q5NIQ1	118.1 Da LogP -0.06 TPSA 74.6	✓ Ro5	✓ Clean	`C(CC(=O)O)C(=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
ZINC12501520 ZINC	1.000	458.5 Da LogP -0.88 TPSA 123.5	1 viol.	✓ Clean	`OCCOCCOCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC1685531 ZINC	1.000	200.4 Da LogP 2.80 TPSA 52.0	✓ Ro5	✓ Clean	`NCCCCCCCCCCCCN`
ZINC34273707 ZINC	1.000	256.5 Da LogP 4.37 TPSA 52.0	✓ Ro5	✓ Clean	`NCCCCCCCCCCCCCCCCN`
ZINC3874716 ZINC	1.000	414.5 Da LogP -0.90 TPSA 114.3	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC4096207 ZINC	1.000	463.3 Da LogP -2.11 TPSA 246.7	2 viol.	✓ Clean	`O=C(O)C[C@H](Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O…`
ZINC4283769 ZINC	1.000	238.3 Da LogP -0.96 TPSA 77.4	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCO`
ZINC4521548 ZINC	1.000	282.3 Da LogP -0.95 TPSA 86.6	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCOCCO`
ZINC5178646 ZINC	1.000	228.4 Da LogP 3.59 TPSA 52.0	✓ Ro5	✓ Clean	`NCCCCCCCCCCCCCCN`
ZINC5178829 ZINC	1.000	326.4 Da LogP -0.93 TPSA 95.8	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCOCCOCCO`
ZINC5178830 ZINC	1.000	370.4 Da LogP -0.91 TPSA 105.1	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC12494556 ZINC	0.767	383.3 Da LogP -2.22 TPSA 200.1	2 viol.	✓ Clean	`O=C(O)C[C@H](Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO)[C@…`
ZINC14414258 ZINC	0.767	383.3 Da LogP -2.22 TPSA 200.1	2 viol.	✓ Clean	`O=C(O)C[C@H](Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO)[C@…`
ZINC218557566 ZINC	0.767	383.3 Da LogP -2.22 TPSA 200.1	2 viol.	✓ Clean	`O=C(O)C[C@H](Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO)[C@…`
ZINC218557648 ZINC	0.767	383.3 Da LogP -2.22 TPSA 200.1	2 viol.	✓ Clean	`O=C(O)C[C@H](Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO)[C@…`
ZINC13516496 ZINC	0.721	361.3 Da LogP -1.40 TPSA 172.1	✓ Ro5	✓ Clean	`CNc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@@H]…`
ZINC115086873 ZINC	0.688	209.2 Da LogP -1.08 TPSA 83.2	✓ Ro5	✓ Clean	`NOCCOCCOCCOCCO`
ZINC137432264 ZINC	0.688	457.6 Da LogP -0.91 TPSA 129.3	1 viol.	✓ Clean	`NCCOCCOCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC146143823 ZINC	0.688	237.3 Da LogP -1.00 TPSA 83.2	✓ Ro5	✓ Clean	`NCCOCCOCCOCCOCCO`
ZINC1542984442 ZINC	0.688	413.5 Da LogP -0.93 TPSA 120.1	✓ Ro5	✓ Clean	`NCCOCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC1565503710 ZINC	0.688	254.3 Da LogP -0.03 TPSA 57.2	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCS`
ZINC1580161 ZINC	0.688	208.3 Da LogP -0.33 TPSA 57.2	✓ Ro5	✓ Clean	`COCCOCCOCCOCCO`
ZINC16052118 ZINC	0.688	340.4 Da LogP -0.28 TPSA 84.8	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCO`
ZINC16052257 ZINC	0.688	384.5 Da LogP -0.26 TPSA 94.1	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC1857792028 ZINC	0.688	430.6 Da LogP 0.04 TPSA 94.1	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCOCCOCCOCCOCCS`
ZINC1857792057 ZINC	0.688	474.6 Da LogP 0.06 TPSA 103.3	1 viol.	✓ Clean	`OCCOCCOCCOCCOCCOCCOCCOCCOCCOCCS`
ZINC230494776 ZINC	0.688	325.4 Da LogP -0.96 TPSA 101.6	✓ Ro5	✓ Clean	`NCCOCCOCCOCCOCCOCCOCCO`
ZINC34317654 ZINC	0.688	472.6 Da LogP -0.23 TPSA 112.5	1 viol.	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC38917157 ZINC	0.688	210.3 Da LogP -0.04 TPSA 47.9	✓ Ro5	✓ Clean	`OCCOCCOCCOCCS`
ZINC44076059 ZINC	0.688	428.5 Da LogP -0.24 TPSA 103.3	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC5210101 ZINC	0.688	252.3 Da LogP -0.31 TPSA 66.4	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCO`
ZINC5650743 ZINC	0.688	222.3 Da LogP 0.07 TPSA 57.2	✓ Ro5	✓ Clean	`CCOCCOCCOCCOCCO`
ZINC5997860 ZINC	0.688	296.4 Da LogP -0.29 TPSA 75.6	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCO`
ZINC6403917 ZINC	0.688	354.4 Da LogP 0.11 TPSA 84.8	✓ Ro5	✓ Clean	`CCOCCOCCOCCOCCOCCOCCOCCO`
ZINC77271182 ZINC	0.688	281.3 Da LogP -0.98 TPSA 92.4	✓ Ro5	✓ Clean	`NCCOCCOCCOCCOCCOCCO`
ZINC83253921 ZINC	0.688	369.5 Da LogP -0.95 TPSA 110.9	✓ Ro5	✓ Clean	`NCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC90741446 ZINC	0.688	386.5 Da LogP 0.02 TPSA 84.8	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCOCCOCCOCCS`
ZINC90741447 ZINC	0.688	298.4 Da LogP -0.01 TPSA 66.4	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCOCCS`
ZINC1852448 ZINC	0.672	437.3 Da LogP 0.17 TPSA 172.1	✓ Ro5	✓ Clean	`O=P(O)(O)OC[C@@H]1O[C@H](n2cnc3c(NCc4ccccc4)ncn…`
ZINC2097407 ZINC	0.672	437.3 Da LogP 0.17 TPSA 172.1	✓ Ro5	✓ Clean	`O=P(O)(O)OC[C@H]1O[C@@H](n2cnc3c(NCc4ccccc4)ncn…`
ZINC3212712 ZINC	0.672	437.3 Da LogP 0.17 TPSA 172.1	✓ Ro5	✓ Clean	`O=P(O)(O)OC[C@@H]1O[C@@H](n2cnc3c(NCc4ccccc4)nc…`
ZINC5412148 ZINC	0.672	437.3 Da LogP 0.17 TPSA 172.1	✓ Ro5	✓ Clean	`O=P(O)(O)OC[C@@H]1O[C@H](n2cnc3c(NCc4ccccc4)ncn…`
ZINC5412151 ZINC	0.672	437.3 Da LogP 0.17 TPSA 172.1	✓ Ro5	✓ Clean	`O=P(O)(O)OC[C@@H]1O[C@@H](n2cnc3c(NCc4ccccc4)nc…`
ZINC5412155 ZINC	0.672	437.3 Da LogP 0.17 TPSA 172.1	✓ Ro5	✓ Clean	`O=P(O)(O)OC[C@@H]1O[C@H](n2cnc3c(NCc4ccccc4)ncn…`
ZINC5412158 ZINC	0.672	437.3 Da LogP 0.17 TPSA 172.1	✓ Ro5	✓ Clean	`O=P(O)(O)OC[C@@H]1O[C@@H](n2cnc3c(NCc4ccccc4)nc…`
ZINC5439578 ZINC	0.657	415.3 Da LogP -0.07 TPSA 172.1	✓ Ro5	✓ Clean	`CC(C)=CCNc1ncnc2c1ncn2[C@H]1O[C@@H](COP(=O)(O)O…`
ZINC5439579 ZINC	0.657	415.3 Da LogP -0.07 TPSA 172.1	✓ Ro5	✓ Clean	`CC(C)=CCNc1ncnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)…`
ZINC5439581 ZINC	0.657	415.3 Da LogP -0.07 TPSA 172.1	✓ Ro5	✓ Clean	`CC(C)=CCNc1ncnc2c1ncn2[C@H]1O[C@@H](COP(=O)(O)O…`
ZINC5439583 ZINC	0.657	415.3 Da LogP -0.07 TPSA 172.1	✓ Ro5	✓ Clean	`CC(C)=CCNc1ncnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)…`
ZINC13531934 ZINC	0.656	348.2 Da LogP -1.74 TPSA 180.3	✓ Ro5	✓ Clean	`O=P(O)(O)OC[C@H]1O[C@@H](n2cnc3c(O)ncnc32)[C@@H…`
ZINC16990100 ZINC	0.656	364.3 Da LogP -1.16 TPSA 160.1	✓ Ro5	✓ Clean	`O=P(O)(O)OC[C@@H]1O[C@H](n2cnc3c(S)ncnc32)[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 A0A0H3GVM8