Protein target profile

KP13_32218

Transcription termination factor rho

Genome: KpKP13 Gene: rho AHE47004.1 3D evidence: AlphaFold DB model + ColabFold model UniProt A0A0H3GH32

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Length 443

Pocket druggability 0.332

Direct ligand evidence 0 61 total records

Functional annotation 1 EC 9 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

Risks to review

Microbiome similarity 2656 of 4744 screened genomes (56.0%) have a significant similarity hit. Weak predicted binding pocket FPocket selected-pocket score 0.33. Weak second pocket-predictor signal P2Rank predicted binding-site probability 0.09.

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: No hit
Gut microbiome similarity: 56.0% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 98.871 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: 91.29 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 0.332

Structure A0A0H3GH32

Pocket Pocket 5

P2Rank 0.093

Structure A0A0H3GH32

Pocket Pocket 1

ColabFold model

FPocket 0.28 · Pocket 3

P2Rank 0.303 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 2656 / 4744 genomes with a hit

Prevalence 56.0%

Cross-references

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

Sequence

UniProt A0A0H3GH32

Sequence

Primary amino-acid sequence viewer.

MEVPAIPFTTLSSRFTPSLRTHTTMNLTELKNTPVSELITLGENMGLENLARMRKQDIIFAILKQHSKSGEDIFGDGVLEILQDGFGFLRSADSSYLAGPDDIYVSPSQIRRFNLRTGDTISGKIRPPKEGERYFALLKVNEVNYDKPENARNKILFENLTPLHANSRLRMERGNGSTEDLTARVLDLASPIGRGQRGLIVAPPKAGKTMLLQNIAQSIAYNHPDCVLMVLLIDERPEEVTEMQRLVKGEVVASTFDEPASRHVQVAEMVIEKAKRLVEHKKDVIILLDSITRLARAYNTVVPASGKVLTGGVDANALHRPKRFFGAARNVEEGGSLTIIATALIDTGSKMDEVIYEEFKGTGNMELHLSRKIAEKRVFPAIDYNRSGTRKEELLTTQEELQKMWILRKIIHPMGEIDAMEFLINKLAMTKTNDDFFDMMKRS

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 9 GO

Enzyme Commission (EC)

3.6.4.-

Gene Ontology (GO)

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:0003676 Binding to a nucleic acid.
GO:0008186 Catalysis of the reaction: ATP + H2O = ADP + phosphate; this reaction requires the presence of RNA, and it drives another reaction.
GO:0003723 Binding to an RNA molecule or a portion thereof.
GO:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
GO:0006353 The completion of transcription: the RNA polymerase pauses, the RNA-DNA hybrid dissociates, followed by the release of the RNA polymerase from its DNA template.
GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
GO:0004386 Catalysis of the reaction: ATP + H2O = ADP + phosphate, to drive the unwinding of a DNA or RNA helix.
GO:0016787 Catalysis of the hydrolysis of various bonds, e.g. C-O, C-N, C-C, phosphoric anhydride bonds, etc.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

37 records

Show feature table

Start	End	DB	Term	Name
154	443	FunFam	G3DSA:3.40.50.300:FF:000072	Transcription termination factor Rho
22	442	PANTHER	PTHR46425	TRANSCRIPTION TERMINATION FACTOR RHO
22	442	InterPro	IPR004665	Transcription termination factor Rho
29	71	SMART	SM00959	Rho_N_2_a
29	71	InterPro	IPR011112	Rho termination factor, N-terminal
75	142	CDD	cd04459	Rho_CSD
75	142	InterPro	IPR011113	Rho termination factor, RNA-binding domain
25	71	FunFam	G3DSA:1.10.720.10:FF:000001	Transcription termination factor Rho
23	71	Gene3D	G3DSA:1.10.720.10	-
72	147	ProSiteProfiles	PS51856	Rho RNA-binding domain profile.
72	147	InterPro	IPR011113	Rho termination factor, RNA-binding domain
114	395	SUPERFAMILY	SSF52540	P-loop containing nucleoside triphosphate hydrolases
114	395	InterPro	IPR027417	P-loop containing nucleoside triphosphate hydrolase
154	443	Gene3D	G3DSA:3.40.50.300	-
154	443	InterPro	IPR027417	P-loop containing nucleoside triphosphate hydrolase
1	443	Hamap	MF_01884	Transcription termination factor Rho [rho].
1	443	InterPro	IPR004665	Transcription termination factor Rho
76	149	Pfam	PF07497	Rho termination factor, RNA-binding domain
76	149	InterPro	IPR011113	Rho termination factor, RNA-binding domain
26	441	NCBIfam	TIGR00767	transcription termination factor Rho
26	441	InterPro	IPR004665	Transcription termination factor Rho
72	149	SUPERFAMILY	SSF50249	Nucleic acid-binding proteins
72	149	InterPro	IPR012340	Nucleic acid-binding, OB-fold
72	146	Gene3D	G3DSA:2.40.50.140	-
72	146	InterPro	IPR012340	Nucleic acid-binding, OB-fold
184	387	Pfam	PF00006	ATP synthase alpha/beta family, nucleotide-binding domain
184	387	InterPro	IPR000194	ATPase, F1/V1/A1 complex, alpha/beta subunit, nucleotide-binding domain
25	70	SUPERFAMILY	SSF68912	Rho N-terminal domain-like
25	70	InterPro	IPR036269	Rho termination factor, N-terminal domain superfamily
72	146	FunFam	G3DSA:2.40.50.140:FF:000010	Transcription termination factor Rho
194	379	SMART	SM00382	AAA_5
194	379	InterPro	IPR003593	AAA+ ATPase domain
29	71	Pfam	PF07498	Rho termination factor, N-terminal domain
180	428	CDD	cd01128	rho_factor_C
180	428	InterPro	IPR041703	Transcription termination factor Rho, ATP binding domain
76	142	SMART	SM00357	csp_8
76	142	InterPro	IPR011129	Cold shock domain

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 #5

0.332

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Surrounding area

Site 2 FPocket #10

0.275

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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

0.093

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Surrounding area

Site 2 P2Rank #2

0.049

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Surrounding area

Site 3 P2Rank #3

0.04

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Surrounding area

Site 4 P2Rank #4

0.031

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Surrounding area

Site 5 P2Rank #5

0.018

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Surrounding area

Residue sets

UniProt: Binding site:169-174

UniProt: Binding site:181-186

UniProt: Binding site:212-212

UniProt: Site:326-326 RNA-binding 2

Binding pockets · P2Rank

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

Site 1 P2Rank #1

0.303

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Surrounding area

Site 2 P2Rank #2

0.068

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Surrounding area

Site 3 P2Rank #3

0.026

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Surrounding area

Site 4 P2Rank #4

0.021

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Surrounding area

Site 5 P2Rank #5

0.018

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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_A0A0H3GH32	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold KP13_32218	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.

61 records

Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 same-protein records

Transferred evidence 11 records from similar proteins

Structural ligands 11 0 loaded crystals

Measured bioactivity 0 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

AF3 PDB via homolog 84.0 Da · LogP 0.88 · TPSA 0.0 Open detail RCSB PDB

AGS PDB via homolog Detail RCSB PDB

ANP PDB via homolog Detail RCSB PDB

BCM PDB via homolog Detail RCSB PDB

BEF 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
AF3 RCSB PDB	6NJO	B7UMA6	84.0 Da LogP 0.88 TPSA 0.0	✓ Ro5	✓ Clean	`F[Al](F)F`
AGS RCSB PDB	1XPO	P0AG30	523.2 Da LogP -1.51 TPSA 262.1	3 viol.	✓ Clean	`c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)…`
ANP RCSB PDB	1PVO	P0AG30	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)…`
BCM RCSB PDB	1XPO	P0AG30	302.3 Da LogP -3.30 TPSA 148.3	1 viol.	✓ Clean	`C[C@](CO)([C@@H]([C@@]12C(=O)N[C@@](C(=C)CCO1)(…`
BEF RCSB PDB	3ICE	P0AG30	66.0 Da LogP 0.88 TPSA 0.0	✓ Ro5	✓ Clean	`[Be-](F)(F)F`
DG RCSB PDB	6Z9R	P0AG30	347.2 Da LogP -1.54 TPSA 185.8	✓ Ro5	✓ Clean	`c1nc2c(n1[C@H]3C[C@@H]([C@H](O3)COP(=O)(O)O)O)N…`
DT RCSB PDB	6Z9T	P0AG30	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…`
FB RCSB PDB	1XPR	P0AG30	330.3 Da LogP -3.73 TPSA 165.4	1 viol.	✓ Clean	`C[C@](CO)([C@@H]([C@@]12C(=O)N[C@@](C(=CC=O)CCO…`
FPD RCSB PDB	1XPU	P0AG30	440.5 Da LogP -1.64 TPSA 165.4	1 viol.	✓ Clean	`C[C@](CO)([C@@H]([C@@]12C(=O)N[C@@]([C@@H](CCO1…`
IUM RCSB PDB	3L0O	P38527	270.0 Da LogP -2.38 TPSA 46.1	✓ Ro5	✓ Clean	`[O-][U+4][O-]`
SPD RCSB PDB	3ICE	P0AG30	145.2 Da LogP -0.34 TPSA 64.1	✓ Ro5	✓ Clean	`C(CCNCCCN)CN`

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
ZINC12296728 ZINC	1.000	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)…`
ZINC13523519 ZINC	1.000	322.2 Da LogP -1.40 TPSA 151.1	✓ Ro5	✓ Clean	`Cc1cn([C@@H]2C[C@@H](O)[C@@H](COP(=O)(O)O)O2)c(…`
ZINC13527599 ZINC	1.000	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	1.000	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)…`
ZINC1481737 ZINC	1.000	302.3 Da LogP -3.30 TPSA 148.3	1 viol.	✓ Clean	`C=C1CCO[C@]2([C@@H](O)[C@@](C)(O)CO)NC(=O)[C@@]…`
ZINC1532627 ZINC	1.000	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)…`
ZINC1532628 ZINC	1.000	322.2 Da LogP -1.40 TPSA 151.1	✓ Ro5	✓ Clean	`Cc1cn([C@@H]2C[C@@H](O)[C@H](COP(=O)(O)O)O2)c(=…`
ZINC1678872 ZINC	1.000	322.2 Da LogP -1.40 TPSA 151.1	✓ Ro5	✓ Clean	`Cc1cn([C@H]2C[C@H](O)[C@@H](COP(=O)(O)O)O2)c(=O…`
ZINC1730395 ZINC	1.000	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…`
ZINC2047010 ZINC	1.000	322.2 Da LogP -1.40 TPSA 151.1	✓ Ro5	✓ Clean	`Cc1cn([C@H]2C[C@@H](O)[C@H](COP(=O)(O)O)O2)c(=O…`
ZINC3869846 ZINC	1.000	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	1.000	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	1.000	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…`
ZINC3870253 ZINC	1.000	322.2 Da LogP -1.40 TPSA 151.1	✓ Ro5	✓ Clean	`Cc1cn([C@@H]2C[C@H](O)[C@H](COP(=O)(O)O)O2)c(=O…`
ZINC3870254 ZINC	1.000	322.2 Da LogP -1.40 TPSA 151.1	✓ Ro5	✓ Clean	`Cc1cn([C@H]2C[C@H](O)[C@H](COP(=O)(O)O)O2)c(=O)…`
ZINC4099038 ZINC	1.000	302.3 Da LogP -3.30 TPSA 148.3	1 viol.	✓ Clean	`C=C1CCO[C@]2([C@@H](O)[C@](C)(O)CO)NC(=O)[C@@]1…`
ZINC4099039 ZINC	1.000	302.3 Da LogP -3.30 TPSA 148.3	1 viol.	✓ Clean	`C=C1CCO[C@]2([C@H](O)[C@](C)(O)CO)NC(=O)[C@@]1(…`
ZINC4099040 ZINC	1.000	302.3 Da LogP -3.30 TPSA 148.3	1 viol.	✓ Clean	`C=C1CCO[C@]2([C@H](O)[C@@](C)(O)CO)NC(=O)[C@@]1…`
ZINC6523446 ZINC	1.000	322.2 Da LogP -1.40 TPSA 151.1	✓ Ro5	✓ Clean	`Cc1cn([C@@H]2C[C@H](O)[C@@H](COP(=O)(O)O)O2)c(=…`
ZINC967753 ZINC	1.000	302.3 Da LogP -3.30 TPSA 148.3	1 viol.	✓ Clean	`C=C1CCO[C@@]2([C@H](O)[C@](C)(O)CO)NC(=O)[C@]1(…`
ZINC967754 ZINC	1.000	302.3 Da LogP -3.30 TPSA 148.3	1 viol.	✓ Clean	`C=C1CCO[C@@]2([C@H](O)[C@@](C)(O)CO)NC(=O)[C@]1…`
ZINC27564039 ZINC	0.933	202.3 Da LogP -0.36 TPSA 76.1	✓ Ro5	✓ Clean	`NCCCCNCCCNCCCN`
ZINC13377742 ZINC	0.929	230.4 Da LogP 0.42 TPSA 76.1	✓ Ro5	✓ Clean	`NCCCCNCCCCNCCCCN`
ZINC1532734 ZINC	0.929	202.3 Da LogP -0.36 TPSA 76.1	✓ Ro5	✓ Clean	`NCCCNCCCCNCCCN`
ZINC1598087 ZINC	0.867	215.4 Da LogP 1.61 TPSA 64.1	✓ Ro5	✓ Clean	`NCCCCCCNCCCCCCN`
ZINC12503703 ZINC	0.860	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	0.860	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…`
ZINC12360002 ZINC	0.855	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	0.855	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	0.855	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	0.855	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	0.855	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	0.855	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	0.855	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	0.855	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	0.855	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	0.855	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	0.855	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@@](=O)(O)OP(=…`
ZINC12503053 ZINC	0.837	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(=…`
ZINC33979243 ZINC	0.837	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	0.837	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	0.837	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	0.837	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	0.837	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…`
ZINC17107637 ZINC	0.833	320.2 Da LogP -1.46 TPSA 162.7	✓ Ro5	✓ Clean	`Cc1cn([C@@H]2C[C@@H](O)[C@@H](COP(N)(N)=O)O2)c(…`
ZINC17107641 ZINC	0.833	320.2 Da LogP -1.46 TPSA 162.7	✓ Ro5	✓ Clean	`Cc1cn([C@@H]2C[C@H](O)[C@@H](COP(N)(N)=O)O2)c(=…`
ZINC5493427 ZINC	0.833	320.2 Da LogP -1.46 TPSA 162.7	✓ Ro5	✓ Clean	`Cc1cn([C@@H]2C[C@H](O)[C@H](COP(N)(N)=O)O2)c(=O…`
ZINC5493430 ZINC	0.833	320.2 Da LogP -1.46 TPSA 162.7	✓ Ro5	✓ Clean	`Cc1cn([C@@H]2C[C@@H](O)[C@H](COP(N)(N)=O)O2)c(=…`
ZINC13507072 ZINC	0.804	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@…`
ZINC33979251 ZINC	0.804	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@@…`

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.