Protein target profile

VK055_2887

adenylosuccinate synthase

Genome: KpATCC43816 Gene: purA AIK81476.1 3D evidence: AlphaFold DB model + ColabFold model Metabolism 1 reaction UniProt A0A0H3GLD4

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Length 432

Pocket druggability 0.975

Metabolic reactions 1

Chokepoint Yes

Direct ligand evidence 0 65 total records

Functional annotation 1 EC 8 GO

Target summary

Strong target candidate with converging metabolic, structural and chemical evidence.

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

Main supporting evidence

Metabolic bottleneck Catalyzes a reaction that is the only producer or consumer of a metabolite in the imported metabolic model. Central metabolic position More central than 99.9% of genes in this genome. No isoenzyme backup detected Imported GPR rules do not show an alternative enzyme for the catalyzed reaction set. Core gene across strains Marked as conserved by both pan-genome tools: Roary and CoreCruncher. Review the complete evidence below

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 (%): 43.478 Lower values reduce human off-target concern.
Human E-value: 6.13e-09
Gut microbiome similarity: 6.9% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 77.546 Higher values support similarity to known essential genes.
DEG E-value: 0.0 Smaller values mean stronger essential-gene similarity.

Localization

Localization: Cytoplasmic

Structure confidence

ColabFold pLDDT: 96.73 0-100 confidence; >70 supports local structural interpretation.

Binding-site evidence

AlphaFold DB / UniProt model

The selected pocket score is the FPocket value used for ranking after applying the curated structure priority. It estimates small-molecule pocket quality; it is not experimental binding evidence. The 3D viewer may show a different loaded structure, so visible pockets can differ.

FPocket 0.975

Structure A0A0H3GLD4

Pocket Pocket 4

P2Rank 0.947

Structure A0A0H3GLD4

Pocket Pocket 1

ColabFold model

FPocket 0.996 · Pocket 1

P2Rank 0.931 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 325 / 4744 genomes with a hit

Prevalence 6.9%

Cross-references

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

Sequence

UniProt A0A0H3GLD4

Pathways

KEGG R01135 BioCyc ADENYLOSUCCINATE-SYNTHASE-RXN

Metabolic context

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

Explore metabolic network

Attractive metabolic target: catalyzes a producing chokepoint reaction in Alanine, aspartate and glutamate metabolism, no isoenzyme backup detected, more central than 99.9% of genes in this genome.

Relative network centrality 99.9% more central than 99.9% of genes in this genome

Chokepoint Chokepoint gene

Imported from KpATCC43816.sbml · 2026-07-09

Sequence

Primary amino-acid sequence viewer.

MGNNVVVLGTQWGDEGKGKIVDLLTERAKYVVRYQGGHNAGHTLVINGEKTVLHLIPSGILRENVTSIIGNGVVLSPAALMKEMKGLEDRGIPVRERLLLSEACPLILDYHVALDVAREKARGAKAIGTTGRGIGPAYEDKVARRGLRVGDLFDKATFADKLKEVMEYHNFQLVNFYKAEAVDYQKVLDDVMAIADILTSMVVDVSDLLDQARQRGDFVMFEGAQGTLLDIDHGTYPYVTSSNTTAGGVATGSGLGPRYVDYVLGIIKAYSTRVGAGPFPTELFDETGEFLCKQGNEFGATTGRRRRTGWLDAVAVRRAVQINSLSGFCLTKLDVLDGLKEVKICVGYRMPDGREVTTTPLAADNWEGIEPIYETMPGWSETTFGVKERSGLPQAALNYIQRIEELTGVPVDIISTGPDRTETMILRDPFDA

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 8 GO

Enzyme Commission (EC)

6.3.4.4

Gene Ontology (GO)

GO:0005525 Binding to GTP, guanosine triphosphate.
GO:0000166 Binding to a nucleotide, any compound consisting of a nucleoside that is esterified with (ortho)phosphate or an oligophosphate at any hydroxyl group on the ribose or deoxyribose.
GO:0006164 The chemical reactions and pathways resulting in the formation of a purine nucleotide, a compound consisting of nucleoside (a purine base linked to a deoxyribose or ribose sugar) esterified with a phosphate group at either the 3' or 5'-hydroxyl group of the sugar.
GO:0004019 Catalysis of the reaction: L-aspartate + GTP + IMP = N(6)-(1,2-dicarboxyethyl)-AMP + GDP + 3 H+ + phosphate.
GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
GO:0000287 Binding to a magnesium (Mg) ion.
GO:0044208 The chemical reactions and pathways resulting in the formation of adenosine monophosphate (AMP) from inosine 5'-monophosphate (IMP).
GO:0046040 The chemical reactions and pathways involving IMP, inosine monophosphate.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

26 records

Show feature table

Start	End	DB	Term	Name
4	425	SMART	SM00788	adenylsucc_synt
4	425	InterPro	IPR001114	Adenylosuccinate synthetase
6	430	NCBIfam	TIGR00184	adenylosuccinate synthase
6	430	InterPro	IPR001114	Adenylosuccinate synthetase
6	424	Pfam	PF00709	Adenylosuccinate synthetase
6	424	InterPro	IPR001114	Adenylosuccinate synthetase
102	201	Gene3D	G3DSA:1.10.300.10	Adenylosuccinate Synthetase, subunit A, domain 2
102	201	InterPro	IPR042110	Adenylosuccinate synthetase, domain 2
102	201	FunFam	G3DSA:1.10.300.10:FF:000001	Adenylosuccinate synthetase
6	259	Gene3D	G3DSA:3.40.440.10	Adenylosuccinate Synthetase, subunit A, domain 1
6	259	InterPro	IPR042109	Adenylosuccinate synthetase, domain 1
267	432	Gene3D	G3DSA:3.90.170.10	Adenylosuccinate Synthetase, subunit A, domain 3
267	432	InterPro	IPR042111	Adenylosuccinate synthetase, domain 3
3	431	SUPERFAMILY	SSF52540	P-loop containing nucleoside triphosphate hydrolases
3	431	InterPro	IPR027417	P-loop containing nucleoside triphosphate hydrolase
4	424	PANTHER	PTHR11846	ADENYLOSUCCINATE SYNTHETASE
4	424	InterPro	IPR001114	Adenylosuccinate synthetase
1	432	Hamap	MF_00011	Adenylosuccinate synthetase [purA].
1	432	InterPro	IPR001114	Adenylosuccinate synthetase
11	18	ProSitePatterns	PS01266	Adenylosuccinate synthetase GTP-binding site.
11	18	InterPro	IPR018220	Adenylosuccinate synthase, GTP-binding site
3	425	CDD	cd03108	AdSS
3	425	InterPro	IPR001114	Adenylosuccinate synthetase
133	144	ProSitePatterns	PS00513	Adenylosuccinate synthetase active site.
133	144	InterPro	IPR033128	Adenylosuccinate synthase, active site
267	429	FunFam	G3DSA:3.90.170.10:FF:000001	Adenylosuccinate synthetase

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 · FPocket

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

Site 1 FPocket #4

0.975

Likely same site as P2Rank 1 1.6 Å 45 shared residues 90% of smaller site

Unusual size

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Surrounding area

Binding pockets · P2Rank

Probability: high ≥ 0.5 · medium 0.2–0.49 · low < 0.2

Site 1 P2Rank #1

0.947

Likely same site as FPocket 4 1.6 Å 45 shared residues 90% of smaller site

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Surrounding area

Site 2 P2Rank #2

0.056

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Surrounding area

Site 3 P2Rank #3

0.049

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Surrounding area

Site 4 P2Rank #4

0.033

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Surrounding area

Residue sets

UniProt: Active site:14-14 Proton acceptor

UniProt: Active site:141-141

UniProt: Active site:42-42 Proton donor

UniProt: Binding site:13-19

UniProt: Binding site:130-130 in other chain

UniProt: Binding site:14-14

UniProt: Binding site:14-17 in other chain

UniProt: Binding site:144-144

UniProt: Binding site:225-225 in other chain

UniProt: Binding site:240-240 in other chain

UniProt: Binding site:300-306

UniProt: Binding site:304-304 in other chain

UniProt: Binding site:306-306

UniProt: Binding site:332-334

UniProt: Binding site:39-42 in other chain

UniProt: Binding site:41-41

UniProt: Binding site:41-43

UniProt: Binding site:415-417

Binding pockets · P2Rank

Probability: high ≥ 0.5 · medium 0.2–0.49 · low < 0.2

Site 1 P2Rank #1

0.931

Likely same site as FPocket 1 2.5 Å 48 shared residues 91% of smaller site

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Surrounding area

Site 2 P2Rank #2

0.094

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Surrounding area

Site 3 P2Rank #3

0.039

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Surrounding area

Site 4 P2Rank #4

0.021

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Surrounding area

Site 5 P2Rank #5

0.015

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Surrounding area

Residue sets

UniProt: Active site:14-14 Proton acceptor

UniProt: Active site:141-141

UniProt: Active site:42-42 Proton donor

UniProt: Binding site:13-19

UniProt: Binding site:130-130 in other chain

UniProt: Binding site:14-14

UniProt: Binding site:14-17 in other chain

UniProt: Binding site:144-144

UniProt: Binding site:225-225 in other chain

UniProt: Binding site:240-240 in other chain

UniProt: Binding site:300-306

UniProt: Binding site:304-304 in other chain

UniProt: Binding site:306-306

UniProt: Binding site:332-334

UniProt: Binding site:39-42 in other chain

UniProt: Binding site:41-41

UniProt: Binding site:41-43

UniProt: Binding site:415-417

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_A0A0H3GLD4	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold VK055_2887	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.

65 records

Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 same-protein records

Transferred evidence 15 records from similar proteins

Structural ligands 15 0 loaded crystals

Measured bioactivity 0 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

DOI PDB via homolog 412.2 Da · LogP -0.94 · TPSA 206.6 Open detail RCSB PDB

DPO PDB via homolog Detail RCSB PDB

GCP PDB via homolog Detail RCSB PDB

GNH PDB via homolog Detail RCSB PDB

GNP 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
DOI RCSB PDB	2GCQ	P0A7D4	412.2 Da LogP -0.94 TPSA 206.6	✓ Ro5	✓ Clean	`c1nc2c(c(n1)OP(=O)(O)O)ncn2[C@H]3C[C@@H]([C@H](…`
DPO RCSB PDB	1KKF	P0A7D4	173.9 Da LogP -3.34 TPSA 135.6	✓ Ro5	✓ Clean	`[O-]P(=O)([O-])OP(=O)([O-])[O-]`
GCP RCSB PDB	1HOP	P0A7D4	521.2 Da LogP -2.22 TPSA 289.9	3 viol.	✓ Clean	`c1nc2c(n1[C@H]3[C@@H]([C@@H]([C@H](O3)CO[P@](=O…`
GNH RCSB PDB	1HON	P0A7D4	442.2 Da LogP -2.49 TPSA 258.4	2 viol.	✓ Clean	`c1nc2c(n1[C@H]3[C@@H]([C@@H]([C@H](O3)CO[P@](=O…`
GNP RCSB PDB	1HOO	P0A7D4	522.2 Da LogP -2.76 TPSA 301.9	3 viol.	✓ Clean	`c1nc2c(n1[C@H]3[C@@H]([C@@H]([C@H](O3)CO[P@](=O…`
GPX RCSB PDB	1CH8	P0A7D4	505.2 Da LogP -1.29 TPSA 267.9	3 viol.	✓ Clean	`c1nc2c(n1[C@H]3[C@H]4[C@@H]([C@H](O3)CO[P@](=O)…`
H5P RCSB PDB	1JUY	P0A7D4	298.1 Da LogP -3.25 TPSA 174.6	1 viol.	✓ Clean	`C([C@@H]1[C@H]([C@H]([C@]2(O1)C(=O)NC(=O)N2)O)O…`
HDA RCSB PDB	1CG0	P0A7D4	119.1 Da LogP -1.08 TPSA 77.8	✓ Ro5	✓ Clean	`C(C(=O)O)N(C=O)O`
IMO RCSB PDB	1CG0	P0A7D4	428.2 Da LogP -1.97 TPSA 226.8	2 viol.	✓ Clean	`c1nc2c(c(n1)OP(=O)(O)O)ncn2[C@H]3[C@@H]([C@@H](…`
IMP RCSB PDB	1CH8	P0A7D4	348.2 Da LogP -2.15 TPSA 180.0	✓ Ro5	✓ Clean	`c1nc2c(n1[C@H]3[C@@H]([C@@H]([C@H](O3)COP(=O)(O…`
MLI RCSB PDB	4M9D	Q81JI9	102.0 Da LogP -3.12 TPSA 80.3	✓ Ro5	✓ Clean	`C(C(=O)[O-])C(=O)[O-]`
PG6 RCSB PDB	3HID	Q8ZIV7	266.3 Da LogP 0.35 TPSA 55.4	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOC`
PGS RCSB PDB	1KSZ	P0A7D4	445.3 Da LogP -1.84 TPSA 218.8	1 viol.	✓ Clean	`c1[nH+]c(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H]…`
RPD RCSB PDB	1QF4	P0A7D4	459.3 Da LogP -3.66 TPSA 246.9	2 viol.	✓ Clean	`C(C[C@H](C(=O)O)[N@](CO)O)CN1C(=O)[C@@]2([C@@H]…`
RPL RCSB PDB	1QF5	P0A7D4	459.3 Da LogP -3.66 TPSA 246.9	2 viol.	✓ Clean	`C(C[C@@H](C(=O)O)[N@](CO)O)CN1C(=O)[C@@]2([C@@H…`

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
ZINC14951284 ZINC	1.000	348.2 Da LogP -2.15 TPSA 180.0	✓ Ro5	✓ Clean	`O=c1[nH]cnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C…`
ZINC1532551 ZINC	1.000	348.2 Da LogP -2.15 TPSA 180.0	✓ Ro5	✓ Clean	`O=c1[nH]cnc2c1ncn2[C@H]1O[C@@H](COP(=O)(O)O)[C@…`
ZINC1692489 ZINC	1.000	222.3 Da LogP 0.33 TPSA 46.2	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOC`
ZINC16969369 ZINC	1.000	348.2 Da LogP -2.15 TPSA 180.0	✓ Ro5	✓ Clean	`O=c1[nH]cnc2c1ncn2[C@H]1O[C@@H](COP(=O)(O)O)[C@…`
ZINC4228242 ZINC	1.000	348.2 Da LogP -2.15 TPSA 180.0	✓ Ro5	✓ Clean	`O=c1[nH]cnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@…`
ZINC4353761 ZINC	1.000	348.2 Da LogP -2.15 TPSA 180.0	✓ Ro5	✓ Clean	`O=c1[nH]cnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C…`
ZINC4530388 ZINC	1.000	266.3 Da LogP 0.35 TPSA 55.4	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOC`
ZINC5701172 ZINC	1.000	310.4 Da LogP 0.36 TPSA 64.6	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOC`
ZINC5997861 ZINC	1.000	398.5 Da LogP 0.40 TPSA 83.1	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCOCCOC`
ZINC8614392 ZINC	1.000	348.2 Da LogP -2.15 TPSA 180.0	✓ Ro5	✓ Clean	`O=c1[nH]cnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C…`
ZINC104869865 ZINC	0.850	443.2 Da LogP -2.45 TPSA 252.6	2 viol.	✓ Clean	`Nc1nc2c(ncn2[C@H]2O[C@H](CO[P@@](=O)(O)OP(=O)(O…`
ZINC12504289 ZINC	0.850	443.2 Da LogP -2.45 TPSA 252.6	2 viol.	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@H](CO[P@@](=O)(O)OP(=O)(…`
ZINC34541308 ZINC	0.850	443.2 Da LogP -2.45 TPSA 252.6	2 viol.	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@H](CO[P@@](=O)(O)OP(=O)(…`
ZINC35000839 ZINC	0.850	443.2 Da LogP -2.45 TPSA 252.6	2 viol.	✓ Clean	`Nc1nc2c(ncn2[C@H]2O[C@@H](CO[P@@](=O)(O)OP(=O)(…`
ZINC45284491 ZINC	0.850	443.2 Da LogP -2.45 TPSA 252.6	2 viol.	✓ Clean	`Nc1nc2c(ncn2[C@H]2O[C@@H](CO[P@@](=O)(O)OP(=O)(…`
ZINC80639694 ZINC	0.850	443.2 Da LogP -2.45 TPSA 252.6	2 viol.	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@H](CO[P@@](=O)(O)OP(=O)(…`
ZINC8215481 ZINC	0.850	443.2 Da LogP -2.45 TPSA 252.6	2 viol.	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@H](CO[P@@](=O)(O)OP(=O)(…`
ZINC106686432 ZINC	0.849	428.2 Da LogP -2.03 TPSA 226.5	2 viol.	✓ Clean	`O=c1[nH]cnc2c1ncn2[C@H]1O[C@@H](CO[P@](=O)(O)OP…`
ZINC12958393 ZINC	0.849	428.2 Da LogP -2.03 TPSA 226.5	2 viol.	✓ Clean	`O=c1[nH]cnc2c1ncn2[C@@H]1O[C@@H](CO[P@](=O)(O)O…`
ZINC35024781 ZINC	0.849	428.2 Da LogP -2.03 TPSA 226.5	2 viol.	✓ Clean	`O=c1[nH]cnc2c1ncn2[C@H]1O[C@@H](CO[P@@](=O)(O)O…`
ZINC35024785 ZINC	0.849	428.2 Da LogP -2.03 TPSA 226.5	2 viol.	✓ Clean	`O=c1[nH]cnc2c1ncn2[C@H]1O[C@@H](CO[P@@](=O)(O)O…`
ZINC35024786 ZINC	0.849	428.2 Da LogP -2.03 TPSA 226.5	2 viol.	✓ Clean	`O=c1[nH]cnc2c1ncn2[C@@H]1O[C@@H](CO[P@@](=O)(O)…`
ZINC4261903 ZINC	0.849	428.2 Da LogP -2.03 TPSA 226.5	2 viol.	✓ Clean	`O=c1[nH]cnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)O…`
ZINC80601236 ZINC	0.849	428.2 Da LogP -2.03 TPSA 226.5	2 viol.	✓ Clean	`O=c1[nH]cnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)O…`
ZINC95921560 ZINC	0.849	428.2 Da LogP -2.03 TPSA 226.5	2 viol.	✓ Clean	`O=c1[nH]cnc2c1ncn2[C@H]1O[C@@H](CO[P@@](=O)(O)O…`
ZINC77319466 ZINC	0.792	364.3 Da LogP -0.78 TPSA 163.0	✓ Ro5	✓ Clean	`O=P(O)(O)OC[C@@H]1O[C@H](n2cnc3c(=S)[nH]cnc32)[…`
ZINC12501413 ZINC	0.783	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)…`
ZINC12958448 ZINC	0.783	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)[…`
ZINC1532555 ZINC	0.783	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)[…`
ZINC16546189 ZINC	0.783	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)[…`
ZINC2159505 ZINC	0.783	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)…`
ZINC3073318 ZINC	0.783	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)…`
ZINC3869963 ZINC	0.783	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)…`
ZINC3869965 ZINC	0.783	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…`
ZINC9334496 ZINC	0.783	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)[…`
ZINC13522804 ZINC	0.774	332.2 Da LogP -0.71 TPSA 160.1	✓ Ro5	✓ Clean	`O=P(O)(O)OC[C@H]1O[C@@H](n2cnc3c(O)ncnc32)C[C@@…`
ZINC13531931 ZINC	0.769	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…`
ZINC13531934 ZINC	0.769	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	0.769	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]…`
ZINC12958401 ZINC	0.759	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	0.759	331.2 Da LogP -0.83 TPSA 165.8	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1C[C@@H](O)[C@@H](COP(=O)(O…`
ZINC13538982 ZINC	0.759	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	0.759	331.2 Da LogP -0.83 TPSA 165.8	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1C[C@@H](O)[C@H](COP(=O)(O)…`
ZINC1713574 ZINC	0.759	331.2 Da LogP -0.83 TPSA 165.8	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1C[C@H](O)[C@@H](COP(=O)(O)O…`
ZINC3869813 ZINC	0.759	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	0.759	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	0.759	331.2 Da LogP -0.83 TPSA 165.8	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1C[C@@H](O)[C@H](COP(=O)(O)O…`
ZINC13518964 ZINC	0.755	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	0.755	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	0.755	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[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.