Protein target profile

VK055_3123

biotin operon repressor

Genome: KpATCC43816 Gene: AIK81700.1 3D evidence: Experimental + ColabFold model UniProt A0A0W7ZMT5

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Length 320

Pocket druggability 0.976

Direct ligand evidence 0 57 total records

Functional annotation 1 EC 6 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

Experimental structure available At least one PDB experimental structure is loaded, not just a predicted model - stronger structural coverage than AlphaFold/ColabFold alone. Core gene across strains Marked as conserved by both pan-genome tools: Roary and CoreCruncher. Strong predicted binding pocket FPocket selected-pocket score 0.98. This is a computational pocket signal, not binding validation. Structure available Experimental + 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: Hit
Human identity (%): 32.258 Lower values reduce human off-target concern.
Human E-value: 1.07e-06
Gut microbiome similarity: 2.4% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 84.688 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: 93.59 0-100 confidence; >70 supports local structural interpretation.

Binding-site evidence

PDB experimental structure

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 0.976

Structure 8F8U

Pocket Pocket 1

P2Rank 0.156

Structure 8F8U

Pocket Pocket 1

ColabFold model

FPocket 0.928 · Pocket 1

P2Rank 0.419 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 116 / 4744 genomes with a hit

Prevalence 2.4%

Cross-references

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

Sequence

Primary amino-acid sequence viewer.

MKDHTIPLTLISILADGEFHSGEQLGEQLGMSRAAINKHIQTLRDWGVDVFTVPGKGYSLPEPIHLLDEKKISQEIDHGRVTVLPVIDSTNQYLLDRLDELTSGDACVAEYQQAGRGRRGRKWFSPFGANLYLSMYWRLEQGPAAAIGLSLVIGIVIAEVLQQLGAEQVRVKWPNDIYLQDRKLSGILVELTGKTGDAAQIVSGAGINLVMRRVESDVVNQGWISLQEAGVVIDRNLLAARLIKELRLGLELFEQEGLAPYLPRWEKLDNFIHRPVKLIIGDKEIYGISRGIDAQGALLLEQDGVIKAWVGGEISLRSAE

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 6 GO

Enzyme Commission (EC)

6.3.4.15

Gene Ontology (GO)

GO:0004077 Catalysis of the reaction: ATP + biotin + L-lysyl-[protein] = AMP + diphosphate + H+ + N(6)-biotinyl-L-lysyl-[protein].
GO:0036211 The covalent alteration of one or more amino acids occurring in proteins, peptides and nascent polypeptides (co-translational, post-translational modifications). Includes the modification of charged tRNAs that are destined to occur in a protein (pre-translation modification).
GO:0006355 Any process that modulates the frequency, rate or extent of cellular DNA-templated transcription.
GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
GO:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
GO:0003677 Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

31 records

Show feature table

Start	End	DB	Term	Name
7	317	Hamap	MF_00978	Bifunctional ligase/repressor BirA [birA].
7	317	InterPro	IPR030855	Bifunctional ligase/repressor BirA
84	208	Pfam	PF03099	Biotin/lipoate A/B protein ligase family
84	208	InterPro	IPR004143	Biotinyl protein ligase (BPL) and lipoyl protein ligase (LPL), catalytic domain
274	317	Pfam	PF02237	Biotin protein ligase C terminal domain
274	317	InterPro	IPR003142	Biotin protein ligase, C-terminal
66	254	ProSiteProfiles	PS51733	Biotinyl protein ligase (BPL) and lipoyl protein ligase (LPL) catalytic domain profile.
66	254	InterPro	IPR004143	Biotinyl protein ligase (BPL) and lipoyl protein ligase (LPL), catalytic domain
14	303	PANTHER	PTHR12835	BIOTIN PROTEIN LIGASE
5	60	SUPERFAMILY	SSF46785	Winged helix DNA-binding domain
5	60	InterPro	IPR036390	Winged helix DNA-binding domain superfamily
81	317	NCBIfam	TIGR00121	biotin--[acetyl-CoA-carboxylase] ligase
81	317	InterPro	IPR004408	Biotin--acetyl-CoA-carboxylase ligase
1	64	Gene3D	G3DSA:1.10.10.10	-
1	64	InterPro	IPR036388	Winged helix-like DNA-binding domain superfamily
271	320	Gene3D	G3DSA:2.30.30.100	-
271	320	FunFam	G3DSA:2.30.30.100:FF:000030	Bifunctional ligase/repressor BirA
78	268	SUPERFAMILY	SSF55681	Class II aaRS and biotin synthetases
78	268	InterPro	IPR045864	Class II Aminoacyl-tRNA synthetase/Biotinyl protein ligase (BPL) and lipoyl protein ligase (LPL)
65	270	FunFam	G3DSA:3.30.930.10:FF:000050	Bifunctional ligase/repressor BirA
1	64	FunFam	G3DSA:1.10.10.10:FF:000356	Bifunctional ligase/repressor BirA
65	270	Gene3D	G3DSA:3.30.930.10	Bira Bifunctional Protein; Domain 2
65	270	InterPro	IPR045864	Class II Aminoacyl-tRNA synthetase/Biotinyl protein ligase (BPL) and lipoyl protein ligase (LPL)
80	253	CDD	cd16442	BPL
80	253	InterPro	IPR004408	Biotin--acetyl-CoA-carboxylase ligase
7	73	NCBIfam	TIGR00122	biotin operon repressor
7	73	InterPro	IPR004409	Biotin operon repressor, helix-turn-helix domain
10	58	Pfam	PF08279	HTH domain
10	58	InterPro	IPR013196	Helix-turn-helix, type 11
271	317	SUPERFAMILY	SSF50037	C-terminal domain of transcriptional repressors
271	317	InterPro	IPR008988	Transcriptional repressor, C-terminal

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 #1

0.976

Unusual size

Show in viewer

Surrounding area

Site 2 FPocket #2

0.715

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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

0.156

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Surrounding area

Binding pockets · FPocket

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

Site 1 FPocket #1

0.928

Likely same site as P2Rank 1 3.2 Å 17 shared residues 100% of smaller site

Unusual size

Show in viewer

Surrounding area

Site 2 FPocket #22

0.329

Likely same site as P2Rank 4 1.0 Å 14 shared residues 100% of smaller site

Unusual size

Show in viewer

Surrounding area

Binding pockets · P2Rank

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

Site 1 P2Rank #1

0.419

Likely same site as FPocket 1 3.2 Å 17 shared residues 100% of smaller site

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Surrounding area

Site 2 P2Rank #2

0.113

Likely same site as FPocket 1 5.8 Å 14 shared residues 88% of smaller site

Show in viewer

Surrounding area

Site 3 P2Rank #3

0.035

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Surrounding area

Site 4 P2Rank #4

0.027

Likely same site as FPocket 22 1.0 Å 14 shared residues 100% of smaller site

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Surrounding area

Site 5 P2Rank #5

0.011

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Surrounding area

Residue sets

UniProt: Binding site:112-112

UniProt: Binding site:116-116

UniProt: Binding site:116-118

UniProt: Binding site:118-118

UniProt: Binding site:183-183

UniProt: Binding site:89-89

UniProt: Binding site:89-91

UniProt: Binding site:90-90

All structural evidence 2 experimental · 1 predicted

Structural evidence

2 + 1

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
PDB 8F8U	X-ray	2.85 Å	A,B	100.0% 1-320	PDBe RCSB PDBj File	Viewing
PDB 8FI3	X-ray	2.90 Å	A,B	100.0% 1-320	PDBe RCSB PDBj File	Loaded
ColabFold VK055_3123	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 and bioactivity evidence are both available for this target.

Direct evidence 0 same-protein records

Transferred evidence 7 records from similar proteins

Structural ligands 5 0 loaded crystals

Measured bioactivity 2 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

ADN PDB via homolog 267.2 Da · LogP -1.98 · TPSA 139.5 Open detail RCSB PDB

BQX PDB via homolog Detail RCSB PDB

BT5 PDB via homolog Detail RCSB PDB

N3G PDB via homolog Detail RCSB PDB

POP 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
ADN RCSB PDB	2EJF	O57883	267.2 Da LogP -1.98 TPSA 139.5	✓ Ro5	✓ Clean	`c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)…`
BQX RCSB PDB	6NDL	Q2G258	526.6 Da LogP -0.34 TPSA 198.1	2 viol.	✓ Clean	`c1nc(c2c(n1)n(cn2)CCCCNS(=O)(=O)NC(=O)NCCCC[C@H…`
BT5 RCSB PDB	1WQW	O57883	573.5 Da LogP -0.59 TPSA 233.3	3 viol.	✓ Clean	`c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)…`
N3G RCSB PDB	6ORU	A0A3A5LBF0	511.6 Da LogP -0.13 TPSA 186.0	1 viol.	✓ Clean	`c1nc(c2c(n1)n(cn2)CCCCNS(=O)(=O)NC(=O)CCCC[C@H]…`
POP RCSB PDB	2DKG	O57883	176.0 Da LogP -2.08 TPSA 129.9	✓ Ro5	✓ Clean	`O[P@@](=O)([O-])O[P@@](=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).

Ligand	UniProt (homolog)	pchembl	MW · LogP · TPSA	Lipinski	PAINS	SMILES
BTX ChEMBL	A0A0E7NXW5	7.52 ~30.2 nM	559.5 Da LogP -0.11 TPSA 216.2	3 viol.	✓ Clean	`c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)…`
CHEMBL3701289 ChEMBL	A0A0E7NXW5	6.18 ~660.7 nM	470.6 Da LogP 1.75 TPSA 141.5	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2CCCCn1cc(CCCCC[C@@H]2SC[C@@H]3NC(…`

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
ZINC13783922 ZINC	0.612	392.2 Da LogP -0.77 TPSA 126.7	✓ Ro5	✓ Clean	`Nc1ncnc2c1c(I)cn2[C@@H]1O[C@H](CO)[C@@H](O)[C@@…`
ZINC14806687 ZINC	0.612	392.2 Da LogP -0.77 TPSA 126.7	✓ Ro5	✓ Clean	`Nc1ncnc2c1c(I)cn2[C@@H]1O[C@H](CO)[C@H](O)[C@@H…`
ZINC17418569 ZINC	0.612	345.2 Da LogP -0.61 TPSA 126.7	✓ Ro5	✓ Clean	`Nc1ncnc2c1c(Br)cn2[C@@H]1O[C@H](CO)[C@@H](O)[C@…`
ZINC2516039 ZINC	0.612	392.2 Da LogP -0.77 TPSA 126.7	✓ Ro5	✓ Clean	`Nc1ncnc2c1c(I)cn2[C@H]1O[C@@H](CO)[C@H](O)[C@@H…`
ZINC26737828 ZINC	0.612	392.2 Da LogP -0.77 TPSA 126.7	✓ Ro5	✓ Clean	`Nc1ncnc2c1c(I)cn2[C@@H]1O[C@H](CO)[C@H](O)[C@H]…`
ZINC26740660 ZINC	0.612	345.2 Da LogP -0.61 TPSA 126.7	✓ Ro5	✓ Clean	`Nc1ncnc2c1c(Br)cn2[C@@H]1O[C@H](CO)[C@H](O)[C@@…`
ZINC26740665 ZINC	0.612	345.2 Da LogP -0.61 TPSA 126.7	✓ Ro5	✓ Clean	`Nc1ncnc2c1c(Br)cn2[C@@H]1O[C@H](CO)[C@H](O)[C@H…`
ZINC27646915 ZINC	0.612	392.2 Da LogP -0.77 TPSA 126.7	✓ Ro5	✓ Clean	`Nc1ncnc2c1c(I)cn2[C@H]1O[C@H](CO)[C@@H](O)[C@H]…`
ZINC34441457 ZINC	0.612	284.2 Da LogP -1.24 TPSA 126.7	✓ Ro5	✓ Clean	`Nc1ncnc2c1c(F)cn2[C@@H]1O[C@H](CO)[C@@H](O)[C@H…`
ZINC4743791 ZINC	0.612	346.1 Da LogP -1.22 TPSA 139.5	✓ Ro5	✓ Clean	`Nc1nc(Br)c2ncn([C@H]3O[C@@H](CO)[C@@H](O)[C@H]3…`
ZINC4743792 ZINC	0.612	346.1 Da LogP -1.22 TPSA 139.5	✓ Ro5	✓ Clean	`Nc1nc(Br)c2ncn([C@@H]3O[C@@H](CO)[C@@H](O)[C@H]…`
ZINC4743793 ZINC	0.612	346.1 Da LogP -1.22 TPSA 139.5	✓ Ro5	✓ Clean	`Nc1nc(Br)c2ncn([C@H]3O[C@@H](CO)[C@@H](O)[C@@H]…`
ZINC4743794 ZINC	0.612	346.1 Da LogP -1.22 TPSA 139.5	✓ Ro5	✓ Clean	`Nc1nc(Br)c2ncn([C@@H]3O[C@@H](CO)[C@@H](O)[C@@H…`
ZINC49785288 ZINC	0.612	345.2 Da LogP -0.61 TPSA 126.7	✓ Ro5	✓ Clean	`Nc1ncnc2c1c(Br)cn2[C@H]1O[C@H](CO)[C@@H](O)[C@H…`
ZINC5010881 ZINC	0.612	295.3 Da LogP -1.92 TPSA 152.7	✓ Ro5	✓ Clean	`NCc1cn([C@H]2O[C@@H](CO)[C@@H](O)[C@H]2O)c2ncnc…`
ZINC5010882 ZINC	0.612	295.3 Da LogP -1.92 TPSA 152.7	✓ Ro5	✓ Clean	`NCc1cn([C@@H]2O[C@@H](CO)[C@@H](O)[C@H]2O)c2ncn…`
ZINC5010884 ZINC	0.612	295.3 Da LogP -1.92 TPSA 152.7	✓ Ro5	✓ Clean	`NCc1cn([C@H]2O[C@@H](CO)[C@@H](O)[C@@H]2O)c2ncn…`
ZINC5010885 ZINC	0.612	295.3 Da LogP -1.92 TPSA 152.7	✓ Ro5	✓ Clean	`NCc1cn([C@@H]2O[C@@H](CO)[C@@H](O)[C@@H]2O)c2nc…`
ZINC5161614 ZINC	0.612	345.2 Da LogP -0.61 TPSA 126.7	✓ Ro5	✓ Clean	`Nc1ncnc2c1c(Br)cn2[C@@H]1O[C@H](CO)[C@@H](O)[C@…`
ZINC5161616 ZINC	0.612	392.2 Da LogP -0.77 TPSA 126.7	✓ Ro5	✓ Clean	`Nc1ncnc2c1c(I)cn2[C@@H]1O[C@H](CO)[C@@H](O)[C@H…`
ZINC6585262 ZINC	0.604	283.2 Da LogP -2.44 TPSA 149.6	✓ Ro5	✓ Clean	`N=c1c2ncn([C@@H]3O[C@H](CO)[C@@H](O)[C@H]3O)c2n…`
ZINC31544818 ZINC	0.600	288.7 Da LogP 0.07 TPSA 93.3	✓ Ro5	✓ Clean	`OC[C@H]1O[C@@H](n2cnc3c(Cl)ncnc32)[C@H](F)[C@@H…`
ZINC31728961 ZINC	0.600	300.7 Da LogP -0.72 TPSA 126.7	✓ Ro5	✓ Clean	`Nc1cc(Cl)c2ncn([C@@H]3O[C@@H](CO)[C@@H](O)[C@@H…`
ZINC31728964 ZINC	0.600	300.7 Da LogP -0.72 TPSA 126.7	✓ Ro5	✓ Clean	`Nc1cc(Cl)c2ncn([C@H]3O[C@@H](CO)[C@@H](O)[C@@H]…`
ZINC38981496 ZINC	0.600	288.7 Da LogP 0.07 TPSA 93.3	✓ Ro5	✓ Clean	`OC[C@H]1O[C@@H](n2cnc3c(Cl)ncnc32)[C@@H](F)[C@@…`
ZINC44168239 ZINC	0.600	281.3 Da LogP -2.43 TPSA 171.4	✓ Ro5	✓ Clean	`Nc1nc(N)c2ncn([C@@H]3O[C@H](CO)[C@@H](O)[C@H]3N…`
ZINC53277583 ZINC	0.600	300.7 Da LogP -0.72 TPSA 126.7	✓ Ro5	✓ Clean	`Nc1cc(Cl)c2ncn([C@H]3O[C@@H](CO)[C@@H](O)[C@H]3…`
ZINC53277584 ZINC	0.600	300.7 Da LogP -0.72 TPSA 126.7	✓ Ro5	✓ Clean	`Nc1cc(Cl)c2ncn([C@@H]3O[C@@H](CO)[C@@H](O)[C@H]…`
ZINC1320093 ZINC	0.596	252.2 Da LogP -1.56 TPSA 113.5	✓ Ro5	✓ Clean	`OC[C@H]1O[C@@H](n2cnc3cncnc32)[C@@H](O)[C@@H]1O`
ZINC13542583 ZINC	0.596	258.2 Da LogP -2.82 TPSA 156.8	✓ Ro5	✓ Clean	`NC(=O)c1c(N)ncn1[C@@H]1O[C@H](CO)[C@@H](O)[C@H]…`
ZINC13548142 ZINC	0.596	252.2 Da LogP -1.56 TPSA 113.5	✓ Ro5	✓ Clean	`OC[C@H]1O[C@@H](n2cnc3cncnc32)[C@H](O)[C@H]1O`
ZINC3814314 ZINC	0.596	252.2 Da LogP -1.56 TPSA 113.5	✓ Ro5	✓ Clean	`OC[C@H]1O[C@@H](n2cnc3cncnc32)[C@H](O)[C@@H]1O`
ZINC4758247 ZINC	0.596	252.2 Da LogP -1.56 TPSA 113.5	✓ Ro5	✓ Clean	`OC[C@@H]1O[C@H](n2cnc3cncnc32)[C@H](O)[C@@H]1O`
ZINC4758248 ZINC	0.596	252.2 Da LogP -1.56 TPSA 113.5	✓ Ro5	✓ Clean	`OC[C@@H]1O[C@@H](n2cnc3cncnc32)[C@H](O)[C@@H]1O`
ZINC4758249 ZINC	0.596	252.2 Da LogP -1.56 TPSA 113.5	✓ Ro5	✓ Clean	`OC[C@@H]1O[C@H](n2cnc3cncnc32)[C@@H](O)[C@@H]1O`
ZINC4758250 ZINC	0.596	252.2 Da LogP -1.56 TPSA 113.5	✓ Ro5	✓ Clean	`OC[C@@H]1O[C@@H](n2cnc3cncnc32)[C@@H](O)[C@@H]1O`
ZINC4878189 ZINC	0.596	258.2 Da LogP -2.82 TPSA 156.8	✓ Ro5	✓ Clean	`NC(=O)c1c(N)ncn1[C@H]1O[C@@H](CO)[C@@H](O)[C@H]…`
ZINC4878191 ZINC	0.596	258.2 Da LogP -2.82 TPSA 156.8	✓ Ro5	✓ Clean	`NC(=O)c1c(N)ncn1[C@@H]1O[C@@H](CO)[C@@H](O)[C@H…`
ZINC4878196 ZINC	0.596	258.2 Da LogP -2.82 TPSA 156.8	✓ Ro5	✓ Clean	`NC(=O)c1c(N)ncn1[C@H]1O[C@@H](CO)[C@@H](O)[C@@H…`
ZINC4878200 ZINC	0.596	258.2 Da LogP -2.82 TPSA 156.8	✓ Ro5	✓ Clean	`NC(=O)c1c(N)ncn1[C@@H]1O[C@@H](CO)[C@@H](O)[C@@…`
ZINC65748061 ZINC	0.596	252.2 Da LogP -1.56 TPSA 113.5	✓ Ro5	✓ Clean	`OC[C@H]1O[C@@H](n2cnc3cncnc32)[C@@H](O)[C@H]1O`
ZINC13518964 ZINC	0.595	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	0.595	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	0.595	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	0.595	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	0.595	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	0.595	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	0.595	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@@H](…`
ZINC4806442 ZINC	0.595	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	0.595	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@H](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.