KpATCC43816 Protein target profile

thymidine phosphorylase

Accession: VK055_2593

Gene: AIK81190.1 deoA 3D evidence: AlphaFold DB model + ColabFold model Metabolism 4 reactions UniProt A0A0H3GRD1

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Length 440

Pocket druggability (P2Rank · AlphaFold DB model) 0.915

Metabolic reactions 4

Chokepoint Yes

Direct ligand evidence 0 71 total records

Functional annotation 1 EC 9 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 chokepoint Catalyzes a reaction that is the only producer or consumer of a metabolite in the imported metabolic model. Independent pocket support: P2Rank + FPocket Both predictors report a high-scoring binding site (P2Rank 0.92, FPocket 0.83). Use the 3D pocket comparison to verify whether they identify the same site. Central metabolic position More central than 90.5% of genes in this genome. 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 (%): 51.852 Lower values reduce human off-target concern.
Human E-value: 8.49e-09
Gut microbiome similarity: 3.3% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): N
DEG identity (%): 0.0 Higher values support similarity to known essential genes.

Structure confidence

ColabFold pLDDT: 96.19 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) 0.915

Structure A0A0H3GRD1

Pocket Pocket 1

Druggability (FPocket) 0.835

Structure A0A0H3GRD1

Pocket Pocket 4

ColabFold model

P2Rank 0.902 · Pocket 1

FPocket 0.645 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 155 / 4744 genomes with a hit

Prevalence 3.3%

Metabolic context

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

Explore metabolic network

Attractive metabolic target: catalyzes a consuming chokepoint reaction in Pyrimidine metabolism, more central than 90.5% of genes in this genome.

Relative network centrality 90.5% more central than 90.5% of genes in this genome

Chokepoint Chokepoint gene

Imported from KpATCC43816.sbml · 2026-07-09

Sequence

Primary amino-acid sequence viewer.

MFLAQEIIRKKRDGQALSDEEIRFFINGIRDNTISEGQIAALAMTIFFHDMSMPERVSLTMAMRDSGTVLDWKSLNLNGPIVDKHSTGGVGDVTSLMLGPMVAACGGYVPMISGRGLGHTGGTLDKLEAIPGFDIFPDDNRFREIIKDVGVAIIGQTSSLAPADKRFYATRDITATVDSIPLITASILAKKLAEGLDALVMDVKVGSGAFMPTYELSAALAEAIVGVANGAGVRTTALLTDMNQVLASSAGNAVEVREAVQFLTGEYRNPRLFDVTMALCVEMLISGKLAADDAEARAKLQAVLDNGKAAEVFGRMVAAQKGPSDFVENYANYLPTAMLSKAVYADTEGFISAMDTRALGMAVVSMGGGRRQASDTIDYSVGFTEMARLGDRVDGQRPLAVIHAKDENSWQEAAKAVKAAIKLDDKAAEITPTVYRRITE

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 9 GO

Subcellular localization

Localization: Cytoplasmic

Enzyme Commission (EC)

2.4.2.4

Gene Ontology (GO)

GO:0009032 Catalysis of the reaction: thymidine + phosphate = thymine + 2-deoxy-D-ribose 1-phosphate.
GO:0016763 Catalysis of the transfer of a pentosyl group from one compound (donor) to another (acceptor).
GO:0006213 The chemical reactions and pathways involving any pyrimidine nucleoside, one of a family of organic molecules consisting of a pyrimidine base covalently bonded to ribose (a ribonucleoside) or deoxyribose (a deoxyribonucleoside).
GO:0016154 Catalysis of the reaction: pyrimidine nucleoside + phosphate = pyrimidine + alpha-D-ribose 1-phosphate.
GO:0004645 Catalysis of the reaction: 1,4-alpha-D-glucosyl(n) + phosphate = 1,4-alpha-D-glucosyl(n-1) + alpha-D-glucose 1-phosphate.
GO:0006206 The chemical reactions and pathways involving pyrimidine nucleobases, 1,3-diazine, organic nitrogenous bases.
GO:0016757 Catalysis of the transfer of a glycosyl group from one compound (donor) to another (acceptor).
GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
GO:0046104 The chemical reactions and pathways involving thymidine, deoxyribosylthymine thymine 2-deoxyriboside, a deoxynucleoside very widely distributed but occurring almost entirely as phosphoric esters in deoxynucleotides and deoxyribonucleic acid, DNA.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

32 records

Show feature table

Start	End	DB	Term	Name
70	335	FunFam	G3DSA:3.40.1030.10:FF:000001	Thymidine phosphorylase
74	334	SUPERFAMILY	SSF52418	Nucleoside phosphorylase/phosphoribosyltransferase catalytic domain
74	334	InterPro	IPR035902	Nucleoside phosphorylase/phosphoribosyltransferase catalytic domain superfamily
337	439	SUPERFAMILY	SSF54680	Pyrimidine nucleoside phosphorylase C-terminal domain
337	439	InterPro	IPR036566	Pyrimidine nucleoside phosphorylase-like, C-terminal domain superfamily
6	194	Gene3D	G3DSA:1.20.970.10	Transferase, Pyrimidine Nucleoside Phosphorylase; Chain C
113	128	ProSitePatterns	PS00647	Thymidine and pyrimidine-nucleoside phosphorylases signature.
113	128	InterPro	IPR017872	Pyrimidine-nucleoside phosphorylase, conserved site
3	439	PANTHER	PTHR10515	THYMIDINE PHOSPHORYLASE
3	439	InterPro	IPR000053	Thymidine/pyrimidine-nucleoside phosphorylase
79	309	Pfam	PF00591	Glycosyl transferase family, a/b domain
79	309	InterPro	IPR000312	Glycosyl transferase, family 3
337	433	Gene3D	G3DSA:3.90.1170.30	-
337	433	InterPro	IPR036566	Pyrimidine nucleoside phosphorylase-like, C-terminal domain superfamily
1	439	PIRSF	PIRSF000478	TP_PyNP
1	439	InterPro	IPR000053	Thymidine/pyrimidine-nucleoside phosphorylase
5	423	NCBIfam	TIGR02644	pyrimidine-nucleoside phosphorylase
5	423	InterPro	IPR018090	Pyrimidine-nucleoside phosphorylase, bacterial/eukaryotic
350	423	Pfam	PF07831	Pyrimidine nucleoside phosphorylase C-terminal domain
350	423	InterPro	IPR013102	Pyrimidine nucleoside phosphorylase, C-terminal
70	325	Gene3D	G3DSA:3.40.1030.10	Nucleoside phosphorylase/phosphoribosyltransferase catalytic domain
70	325	InterPro	IPR035902	Nucleoside phosphorylase/phosphoribosyltransferase catalytic domain superfamily
337	433	FunFam	G3DSA:3.90.1170.30:FF:000001	Thymidine phosphorylase
6	67	Pfam	PF02885	Glycosyl transferase family, helical bundle domain
6	67	InterPro	IPR017459	Glycosyl transferase family 3, N-terminal domain
350	424	SMART	SM00941	PYNP_C_2
350	424	InterPro	IPR013102	Pyrimidine nucleoside phosphorylase, C-terminal
2	70	SUPERFAMILY	SSF47648	Nucleoside phosphorylase/phosphoribosyltransferase N-terminal domain
2	70	InterPro	IPR036320	Glycosyl transferase family 3, N-terminal domain superfamily
2	438	Hamap	MF_01628	Thymidine phosphorylase [deoA].
2	438	InterPro	IPR013465	Thymidine phosphorylase
2	438	NCBIfam	TIGR02643	thymidine phosphorylase

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

0.915

Likely same site as FPocket 4 3.9 Å 15 shared residues 94% of smaller site

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Surrounding area

Pocket 2 P2Rank #2

0.309

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Surrounding area

Pocket 3 P2Rank #3

0.021

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Surrounding area

Pocket 4 P2Rank #4

0.015

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Surrounding area

Pocket 5 P2Rank #5

0.005

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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 #4

0.835

Likely same site as P2Rank 1 3.9 Å 15 shared residues 94% of smaller site

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Surrounding area

Binding pockets · P2Rank

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

Pocket 1 P2Rank #1

0.902

Likely same site as FPocket 1 3.2 Å 26 shared residues 100% of smaller site

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Surrounding area

Pocket 2 P2Rank #2

0.149

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Surrounding area

Pocket 3 P2Rank #3

0.132

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Surrounding area

Pocket 4 P2Rank #4

0.054

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Surrounding area

Pocket 5 P2Rank #5

0.002

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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_A0A0H3GRD1	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold VK055_2593	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.

71 records

Chemistry signal

Structural and bioactivity evidence are both available for this target.

Direct evidence 0 same-protein records

Transferred evidence 21 records from similar proteins

Structural ligands 7 0 loaded crystals

Measured bioactivity 14 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

0NP PDB via homolog 272.2 Da · LogP -1.32 · TPSA 134.6 Open detail RCSB PDB

AZZ PDB via homolog Detail RCSB PDB

CTN PDB via homolog Detail RCSB PDB

IUR PDB via homolog Detail RCSB PDB

THM 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
0NP RCSB PDB	4EAD	P07650	272.2 Da LogP -1.32 TPSA 134.6	✓ Ro5	Alert	`C1=CN(C(=O)NC1=O)[C@H]2[C@@H]([C@@H]([C@H](O2)C…`
AZZ RCSB PDB	4LHM	P07650	267.2 Da LogP -0.20 TPSA 133.1	✓ Ro5	Alert	`CC1=CN(C(=O)NC1=O)[C@H]2C[C@@H]([C@H](O2)CO)N=[…`
CTN RCSB PDB	5EY3	Q7CP66	243.2 Da LogP -2.56 TPSA 130.8	✓ Ro5	✓ Clean	`C1=CN(C(=O)N=C1N)[C@H]2[C@@H]([C@@H]([C@H](O2)C…`
IUR RCSB PDB	2WK6	P19971	238.0 Da LogP -0.33 TPSA 65.7	✓ Ro5	✓ Clean	`C1=C(C(=O)NC(=O)N1)I`
THM RCSB PDB	4YEK	Q7CP66	242.2 Da LogP -1.51 TPSA 104.6	✓ Ro5	✓ Clean	`CC1=CN(C(=O)NC1=O)[C@H]2C[C@@H]([C@H](O2)CO)O`
URA RCSB PDB	1BRW	P77836	112.1 Da LogP -0.94 TPSA 65.7	✓ Ro5	✓ Clean	`C1=CNC(=O)NC1=O`
URI RCSB PDB	4YYY	Q7CP66	244.2 Da LogP -2.85 TPSA 124.8	✓ Ro5	✓ Clean	`C1=CN(C(=O)NC1=O)[C@H]2[C@@H]([C@@H]([C@H](O2)C…`

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
CHEMBL597306 ChEMBL	Q5FVR2	7.96 ~11.0 nM	319.2 Da LogP -1.64 TPSA 152.9	✓ Ro5	✓ Clean	`Cc1cn([C@@H]2CN(C(=O)P(=O)(O)O)C[C@@H]2O)c(=O)[…`
CHEMBL609919 ChEMBL	Q5FVR2	7.82 ~15.1 nM	335.3 Da LogP -1.47 TPSA 135.9	✓ Ro5	✓ Clean	`Cc1cn([C@@H]2CN(C(=S)P(=O)(O)O)C[C@@H]2O)c(=O)[…`
CHEMBL599543 ChEMBL	Q5FVR2	7.35 ~44.7 nM	333.2 Da LogP -1.25 TPSA 152.9	✓ Ro5	✓ Clean	`Cc1cn([C@H]2C[C@H](CO)N(C(=O)P(=O)(O)O)C2)c(=O)…`
CHEMBL599563 ChEMBL	Q5FVR2	7.35 ~44.7 nM	305.2 Da LogP -1.80 TPSA 135.9	✓ Ro5	✓ Clean	`Cc1cn([C@@H]2CN(CP(=O)(O)O)C[C@@H]2O)c(=O)[nH]c…`
CHEMBL598328 ChEMBL	Q5FVR2	6.72 ~190.5 nM	319.3 Da LogP -0.45 TPSA 115.6	✓ Ro5	✓ Clean	`Cc1cn(C2CCN(C(=S)P(=O)(O)O)C2)c(=O)[nH]c1=O`
CHEMBL599562 ChEMBL	Q5FVR2	6.66 ~218.8 nM	319.2 Da LogP -1.64 TPSA 152.9	✓ Ro5	✓ Clean	`Cc1cn([C@@H]2CN(C(=O)P(=O)(O)O)C[C@H]2O)c(=O)[n…`
CHEMBL374140 ChEMBL	P19971	6.63 ~234.4 nM	364.2 Da LogP -1.98 TPSA 160.3	✓ Ro5	✓ Clean	`Cc1cn([C@@H]2O[C@H](CO)[C@H]3O[C@@H](CP(=O)(O)O…`
CHEMBL401998 ChEMBL	P19971	6.63 ~234.4 nM	264.2 Da LogP -1.00 TPSA 121.6	✓ Ro5	✓ Clean	`Cc1cn(CCOCP(=O)(O)O)c(=O)[nH]c1=O`
CHEMBL597717 ChEMBL	P19971	6.63 ~234.4 nM	515.3 Da LogP -0.10 TPSA 171.4	1 viol.	✓ Clean	`O=c1c(Br)cn([C@@H]2O[C@H](CO)[C@@H](O)[C@H]2O)c…`
CHEMBL599022 ChEMBL	P19971	6.63 ~234.4 nM	294.2 Da LogP -1.64 TPSA 141.8	✓ Ro5	✓ Clean	`Cc1cn(CC(CO)OCP(=O)(O)O)c(=O)[nH]c1=O`
CHEMBL599755 ChEMBL	P19971	6.63 ~234.4 nM	278.2 Da LogP -0.61 TPSA 121.6	✓ Ro5	✓ Clean	`Cc1cn(CC(C)OCP(=O)(O)O)c(=O)[nH]c1=O`
CHEMBL599544 ChEMBL	Q5FVR2	6.60 ~251.2 nM	319.3 Da LogP -1.41 TPSA 135.9	✓ Ro5	✓ Clean	`Cc1cn([C@H]2C[C@H](CO)N(CP(=O)(O)O)C2)c(=O)[nH]…`
CHEMBL598327 ChEMBL	Q5FVR2	6.46 ~346.7 nM	303.2 Da LogP -0.61 TPSA 132.7	✓ Ro5	✓ Clean	`Cc1cn(C2CCN(C(=O)P(=O)(O)O)C2)c(=O)[nH]c1=O`
CHEMBL373989 ChEMBL	P07650	6.00 ~1.0 µM	362.3 Da LogP -1.31 TPSA 151.1	✓ Ro5	✓ Clean	`Cc1cn([C@@H]2O[C@H](CO)[C@H]3C[C@@H](CP(=O)(O)O…`

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
ZINC1078621 ZINC	1.000	243.2 Da LogP -2.56 TPSA 130.8	✓ Ro5	✓ Clean	`Nc1ccn([C@H]2O[C@H](CO)[C@@H](O)[C@H]2O)c(=O)n1`
ZINC1092752 ZINC	1.000	238.0 Da LogP -0.33 TPSA 65.7	✓ Ro5	✓ Clean	`O=c1[nH]cc(I)c(=O)[nH]1`
ZINC11525575 ZINC	1.000	244.2 Da LogP -2.85 TPSA 124.8	✓ Ro5	✓ Clean	`O=c1ccn([C@H]2O[C@H](CO)[C@H](O)[C@H]2O)c(=O)[n…`
ZINC11525576 ZINC	1.000	244.2 Da LogP -2.85 TPSA 124.8	✓ Ro5	✓ Clean	`O=c1ccn([C@@H]2O[C@H](CO)[C@H](O)[C@H]2O)c(=O)[…`
ZINC12336757 ZINC	1.000	243.2 Da LogP -2.56 TPSA 130.8	✓ Ro5	✓ Clean	`Nc1ccn([C@@H]2O[C@H](CO)[C@H](O)[C@@H]2O)c(=O)n1`
ZINC12336758 ZINC	1.000	243.2 Da LogP -2.56 TPSA 130.8	✓ Ro5	✓ Clean	`Nc1ccn([C@H]2O[C@H](CO)[C@H](O)[C@@H]2O)c(=O)n1`
ZINC1446448 ZINC	1.000	244.2 Da LogP -2.85 TPSA 124.8	✓ Ro5	✓ Clean	`O=c1ccn([C@H]2O[C@H](CO)[C@@H](O)[C@H]2O)c(=O)[…`
ZINC16969357 ZINC	1.000	243.2 Da LogP -2.56 TPSA 130.8	✓ Ro5	✓ Clean	`Nc1ccn([C@H]2O[C@@H](CO)[C@H](O)[C@H]2O)c(=O)n1`
ZINC1842580 ZINC	1.000	242.2 Da LogP -1.51 TPSA 104.5	✓ Ro5	✓ Clean	`Cc1cn([C@@H]2C[C@H](O)[C@H](CO)O2)c(=O)[nH]c1=O`
ZINC2159 ZINC	1.000	242.2 Da LogP -1.51 TPSA 104.5	✓ Ro5	✓ Clean	`Cc1cn([C@@H]2C[C@@H](O)[C@H](CO)O2)c(=O)[nH]c1=O`
ZINC2545102 ZINC	1.000	242.2 Da LogP -1.51 TPSA 104.5	✓ Ro5	✓ Clean	`Cc1cn([C@H]2C[C@@H](O)[C@H](CO)O2)c(=O)[nH]c1=O`
ZINC2565479 ZINC	1.000	244.2 Da LogP -2.85 TPSA 124.8	✓ Ro5	✓ Clean	`O=c1ccn([C@@H]2O[C@@H](CO)[C@H](O)[C@@H]2O)c(=O…`
ZINC25672 ZINC	1.000	242.2 Da LogP -1.51 TPSA 104.5	✓ Ro5	✓ Clean	`Cc1cn([C@H]2C[C@H](O)[C@@H](CO)O2)c(=O)[nH]c1=O`
ZINC2572653 ZINC	1.000	242.2 Da LogP -1.51 TPSA 104.5	✓ Ro5	✓ Clean	`Cc1cn([C@@H]2C[C@@H](O)[C@@H](CO)O2)c(=O)[nH]c1…`
ZINC2583632 ZINC	1.000	243.2 Da LogP -2.56 TPSA 130.8	✓ Ro5	✓ Clean	`Nc1ccn([C@@H]2O[C@H](CO)[C@@H](O)[C@H]2O)c(=O)n1`
ZINC2583633 ZINC	1.000	244.2 Da LogP -2.85 TPSA 124.8	✓ Ro5	✓ Clean	`O=c1ccn([C@@H]2O[C@H](CO)[C@@H](O)[C@H]2O)c(=O)…`
ZINC3795098 ZINC	1.000	243.2 Da LogP -2.56 TPSA 130.8	✓ Ro5	✓ Clean	`Nc1ccn([C@@H]2O[C@H](CO)[C@@H](O)[C@@H]2O)c(=O)…`
ZINC3830623 ZINC	1.000	243.2 Da LogP -2.56 TPSA 130.8	✓ Ro5	✓ Clean	`Nc1ccn([C@H]2O[C@@H](CO)[C@@H](O)[C@H]2O)c(=O)n1`
ZINC3830624 ZINC	1.000	243.2 Da LogP -2.56 TPSA 130.8	✓ Ro5	✓ Clean	`Nc1ccn([C@@H]2O[C@@H](CO)[C@@H](O)[C@H]2O)c(=O)…`
ZINC3831529 ZINC	1.000	242.2 Da LogP -1.51 TPSA 104.5	✓ Ro5	✓ Clean	`Cc1cn([C@H]2C[C@H](O)[C@H](CO)O2)c(=O)[nH]c1=O`
ZINC3831621 ZINC	1.000	267.2 Da LogP -0.20 TPSA 133.1	✓ Ro5	Alert	`Cc1cn([C@H]2C[C@@H](N=[N+]=[N-])[C@H](CO)O2)c(=…`
ZINC3834164 ZINC	1.000	244.2 Da LogP -2.85 TPSA 124.8	✓ Ro5	✓ Clean	`O=c1ccn([C@@H]2O[C@H](CO)[C@@H](O)[C@@H]2O)c(=O…`
ZINC3870261 ZINC	1.000	244.2 Da LogP -2.85 TPSA 124.8	✓ Ro5	✓ Clean	`O=c1ccn([C@H]2O[C@@H](CO)[C@@H](O)[C@H]2O)c(=O)…`
ZINC3870262 ZINC	1.000	244.2 Da LogP -2.85 TPSA 124.8	✓ Ro5	✓ Clean	`O=c1ccn([C@@H]2O[C@@H](CO)[C@@H](O)[C@H]2O)c(=O…`
ZINC3870263 ZINC	1.000	244.2 Da LogP -2.85 TPSA 124.8	✓ Ro5	✓ Clean	`O=c1ccn([C@H]2O[C@@H](CO)[C@@H](O)[C@@H]2O)c(=O…`
ZINC3870264 ZINC	1.000	244.2 Da LogP -2.85 TPSA 124.8	✓ Ro5	✓ Clean	`O=c1ccn([C@@H]2O[C@@H](CO)[C@@H](O)[C@@H]2O)c(=…`
ZINC3978018 ZINC	1.000	243.2 Da LogP -2.56 TPSA 130.8	✓ Ro5	✓ Clean	`Nc1ccn([C@H]2O[C@H](CO)[C@@H](O)[C@@H]2O)c(=O)n1`
ZINC5765078 ZINC	1.000	242.2 Da LogP -1.51 TPSA 104.5	✓ Ro5	✓ Clean	`Cc1cn([C@H]2C[C@@H](O)[C@@H](CO)O2)c(=O)[nH]c1=O`
ZINC6072455 ZINC	1.000	242.2 Da LogP -1.51 TPSA 104.5	✓ Ro5	✓ Clean	`Cc1cn([C@@H]2C[C@H](O)[C@@H](CO)O2)c(=O)[nH]c1=O`
ZINC6091549 ZINC	1.000	244.2 Da LogP -2.85 TPSA 124.8	✓ Ro5	✓ Clean	`O=c1ccn([C@H]2O[C@@H](CO)[C@H](O)[C@H]2O)c(=O)[…`
ZINC6091575 ZINC	1.000	243.2 Da LogP -2.56 TPSA 130.8	✓ Ro5	✓ Clean	`Nc1ccn([C@@H]2O[C@H](CO)[C@H](O)[C@H]2O)c(=O)n1`
ZINC6234828 ZINC	1.000	243.2 Da LogP -2.56 TPSA 130.8	✓ Ro5	✓ Clean	`Nc1ccn([C@H]2O[C@H](CO)[C@H](O)[C@H]2O)c(=O)n1`
ZINC6524831 ZINC	1.000	244.2 Da LogP -2.85 TPSA 124.8	✓ Ro5	✓ Clean	`O=c1ccn([C@@H]2O[C@@H](CO)[C@H](O)[C@H]2O)c(=O)…`
ZINC6524892 ZINC	1.000	243.2 Da LogP -2.56 TPSA 130.8	✓ Ro5	✓ Clean	`Nc1ccn([C@@H]2O[C@@H](CO)[C@H](O)[C@H]2O)c(=O)n1`
ZINC7998085 ZINC	1.000	244.2 Da LogP -2.85 TPSA 124.8	✓ Ro5	✓ Clean	`O=c1ccn([C@H]2O[C@H](CO)[C@@H](O)[C@@H]2O)c(=O)…`
ZINC8613151 ZINC	1.000	244.2 Da LogP -2.85 TPSA 124.8	✓ Ro5	✓ Clean	`O=c1ccn([C@@H]2O[C@H](CO)[C@H](O)[C@@H]2O)c(=O)…`
ZINC8613153 ZINC	1.000	244.2 Da LogP -2.85 TPSA 124.8	✓ Ro5	✓ Clean	`O=c1ccn([C@H]2O[C@H](CO)[C@H](O)[C@@H]2O)c(=O)[…`
ZINC895165 ZINC	1.000	244.2 Da LogP -2.85 TPSA 124.8	✓ Ro5	✓ Clean	`O=c1ccn([C@H]2O[C@@H](CO)[C@H](O)[C@@H]2O)c(=O)…`
ZINC895248 ZINC	1.000	243.2 Da LogP -2.56 TPSA 130.8	✓ Ro5	✓ Clean	`Nc1ccn([C@H]2O[C@@H](CO)[C@H](O)[C@@H]2O)c(=O)n1`
ZINC4804742 ZINC	0.854	272.3 Da LogP -2.15 TPSA 124.8	✓ Ro5	✓ Clean	`Cc1cn([C@@H]2C[C@H](O)[C@H](O)[C@H](CO)O2)c(=O)…`
ZINC4804743 ZINC	0.854	272.3 Da LogP -2.15 TPSA 124.8	✓ Ro5	✓ Clean	`Cc1cn([C@H]2C[C@H](O)[C@H](O)[C@H](CO)O2)c(=O)[…`
ZINC4804744 ZINC	0.854	272.3 Da LogP -2.15 TPSA 124.8	✓ Ro5	✓ Clean	`Cc1cn([C@@H]2C[C@@H](O)[C@H](O)[C@H](CO)O2)c(=O…`
ZINC4804745 ZINC	0.854	272.3 Da LogP -2.15 TPSA 124.8	✓ Ro5	✓ Clean	`Cc1cn([C@H]2C[C@@H](O)[C@H](O)[C@H](CO)O2)c(=O)…`
ZINC34085615 ZINC	0.829	242.2 Da LogP -2.60 TPSA 136.6	✓ Ro5	✓ Clean	`Nc1ccn([C@@H]2O[C@H](CO)[C@@H](O)[C@H]2N)c(=O)n1`
ZINC13546396 ZINC	0.810	245.2 Da LogP -1.59 TPSA 110.6	✓ Ro5	✓ Clean	`Nc1ccn([C@@H]2O[C@H](CO)[C@H](O)[C@H]2F)c(=O)n1`
ZINC16928956 ZINC	0.810	258.3 Da LogP -0.14 TPSA 87.5	✓ Ro5	✓ Clean	`Cc1cn([C@H]2C[C@@H](O)[C@@H](CO)O2)c(=O)[nH]c1=S`
ZINC2522524 ZINC	0.810	245.2 Da LogP -1.59 TPSA 110.6	✓ Ro5	✓ Clean	`Nc1ccn([C@H]2O[C@@H](CO)[C@H](O)[C@@H]2F)c(=O)n1`
ZINC3817231 ZINC	0.810	245.2 Da LogP -1.59 TPSA 110.6	✓ Ro5	✓ Clean	`Nc1ccn([C@@H]2O[C@H](CO)[C@@H](O)[C@H]2F)c(=O)n1`
ZINC57331 ZINC	0.810	245.2 Da LogP -1.59 TPSA 110.6	✓ Ro5	✓ Clean	`Nc1ccn([C@@H]2O[C@@H](CO)[C@@H](O)[C@H]2F)c(=O)…`
ZINC59201305 ZINC	0.810	245.2 Da LogP -1.59 TPSA 110.6	✓ Ro5	✓ Clean	`Nc1ccn([C@@H]2O[C@H](CO)[C@H](O)[C@@H]2F)c(=O)n1`

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.

thymidine phosphorylase

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

Main supporting evidence

Risks to review

Evidence coverage

Prioritization evidence

Off-target risk

Essentiality

Structure confidence

Binding-site evidence

Metabolic context

Sequence

Functional annotations

Subcellular localization

Enzyme Commission (EC)

Gene Ontology (GO)

Sequence domains and features

3D structure

Binding pockets · P2Rank

Binding pockets · FPocket

Binding pockets · P2Rank

Binding pockets · FPocket

Structural evidence

Ligand evidence

Cross-references

Sequence

Chemistry

Pathways