KpKP13 Protein target profile

Ribonucleoside-diphosphate reductase 1 subunit alpha

Accession: KP13_00958

Gene: AHE43514.1 nrdA 3D evidence: AlphaFold DB model + ColabFold model UniProt A0A0H3GW79

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Length 761

Pocket druggability (P2Rank · AlphaFold DB model) 0.788

Direct ligand evidence 0 75 total records

Functional annotation 1 EC 5 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. Second pocket predictor agrees P2Rank predicted binding-site probability 0.79. Structure available AlphaFold DB model + ColabFold model Ligand evidence via structure/bioactivity 16 structural and 9 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 (%): 27.586 Lower values reduce human off-target concern.
Human E-value: 6.44e-51
Gut microbiome similarity: 3.2% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 94.744 Higher values support similarity to known essential genes.
DEG E-value: 0.0 Smaller values mean stronger essential-gene similarity.

Structure confidence

ColabFold pLDDT: 93.21 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) 0.788

Structure A0A0H3GW79

Pocket Pocket 1

Druggability (FPocket) 0.354

Structure A0A0H3GW79

Pocket Pocket 22

ColabFold model

P2Rank 0.802 · Pocket 1

FPocket 0.663 · Pocket 43

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 153 / 4744 genomes with a hit

Prevalence 3.2%

Sequence

Primary amino-acid sequence viewer.

MNQSLLVTKRDGTTERINLDKIHRVLDWAAEGLNNVSISQVELRSHIQFYDGIKTADIHETIIKAAADLISRDAPDYQYLAARLAIFHLRKKAFGQFEPPALYDHVVKMVEKGKYDHHLLEDYTEEEFQQMDGFLDHWRDMNFSYAAVKQLEGKYLVQNRVTGEIYESAQFLYILVAACLFSNYPRETRLDYIKRFYDAVSTFKISLPTPIMSGVRTPTRQFSSCVLIECGDSLDSINATSSAIVKYVSQRAGIGINAGRIRALGSPIRGGEAFHTGCIPFYKHFQTAVKSCSQGGVRGGAATLFYPMWHLEVESLLVLKNNRGTDANRVRHMDYGVQINKLMYTRLLKGGDITLFSPSDVPGLYDAFFADQDEFERLYTQYEQDDSIRKQRIKAVELFSLMMQERASTGRIYIQNVDHCNTHSPFDPVVAPVRQSNLCLEIALPTKPLEDVNDENGEIALCTLSAFNLGAIDSLDELEELAVLAVRALDALLDYQDYPIPAAKRGAMGRRTLGIGVINFAYYLAKHGKRYSDGSANNLTHKTFEAIQYYLLKASNELAIEQGACPWFNETTYAQGILPIDTYKKDLDGIVSEPLHYDWEALRESIKTHGLRNSTLSALMPSETSSQISNATNGIEPPRGHVSIKASKDGILRQVVPDYENLQNAYELLWEMPNNDGYLQLVGIMQKFIDQSISANTNYDPTRFPSGKVPMQQLLKDLLNAYKFGVKTLYYHNTRDGAEDAQDDLAPSIQDDGCESGACKI

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 5 GO

Subcellular localization

Localization: Cytoplasmic

Enzyme Commission (EC)

1.17.4.1

Gene Ontology (GO)

GO:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
GO:0006260 The cellular metabolic process in which a cell duplicates one or more molecules of DNA. DNA replication begins when specific sequences, known as origins of replication, are recognized and bound by the origin recognition complex, and ends when the original DNA molecule has been completely duplicated and the copies topologically separated. The unit of replication usually corresponds to the genome of the cell, an organelle, or a virus. The template for replication can either be an existing DNA molecule or RNA.
GO:0004748 Catalysis of the reaction: 2'-deoxyribonucleoside diphosphate + thioredoxin disulfide + H2O = ribonucleoside diphosphate + thioredoxin. Thioredoxin disulfide is the oxidized form of thioredoxin.
GO:0005971 An enzyme complex composed of 2-4 or more subunits, which usually contains nonheme iron and requires ATP for catalysis. Catalyzes the formation of 2'-deoxyribonucleoside diphosphate from ribonucleoside diphosphate, using either thioredoxin disulfide or glutaredoxin disulfide as an acceptor.
GO:0009263 The chemical reactions and pathways resulting in the formation of a deoxyribonucleotide, a compound consisting of deoxyribonucleoside (a base linked to a deoxyribose sugar) esterified with a phosphate group at either the 3' or 5'-hydroxyl group of the sugar.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

32 records

Show feature table

Start	End	DB	Term	Name
6	92	Pfam	PF03477	ATP cone domain
6	92	InterPro	IPR005144	ATP-cone domain
142	219	Pfam	PF00317	Ribonucleotide reductase, all-alpha domain
142	219	InterPro	IPR013509	Ribonucleotide reductase large subunit, N-terminal
6	746	PANTHER	PTHR11573	RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE LARGE CHAIN
6	746	InterPro	IPR039718	Ribonucleoside-diphosphate reductase large subunit
145	735	NCBIfam	TIGR02506	ribonucleoside-diphosphate reductase subunit alpha
145	735	InterPro	IPR013346	Ribonucleotide reductase, class I, alpha subunit, C-terminal
223	731	Pfam	PF02867	Ribonucleotide reductase, barrel domain
223	731	InterPro	IPR000788	Ribonucleotide reductase large subunit, C-terminal
599	621	ProSitePatterns	PS00089	Ribonucleotide reductase large subunit signature.
599	621	InterPro	IPR013346	Ribonucleotide reductase, class I, alpha subunit, C-terminal
342	395	Gene3D	G3DSA:1.10.1650.20	-
473	496	PRINTS	PR01183	Ribonucleotide reductase large chain signature
473	496	InterPro	IPR000788	Ribonucleotide reductase large subunit, C-terminal
610	637	PRINTS	PR01183	Ribonucleotide reductase large chain signature
610	637	InterPro	IPR000788	Ribonucleotide reductase large subunit, C-terminal
511	533	PRINTS	PR01183	Ribonucleotide reductase large chain signature
511	533	InterPro	IPR000788	Ribonucleotide reductase large subunit, C-terminal
433	444	PRINTS	PR01183	Ribonucleotide reductase large chain signature
433	444	InterPro	IPR000788	Ribonucleotide reductase large subunit, C-terminal
539	562	PRINTS	PR01183	Ribonucleotide reductase large chain signature
539	562	InterPro	IPR000788	Ribonucleotide reductase large subunit, C-terminal
298	317	PRINTS	PR01183	Ribonucleotide reductase large chain signature
298	317	InterPro	IPR000788	Ribonucleotide reductase large subunit, C-terminal
5	95	ProSiteProfiles	PS51161	ATP-cone domain profile.
5	95	InterPro	IPR005144	ATP-cone domain
342	395	FunFam	G3DSA:1.10.1650.20:FF:000001	Ribonucleoside-diphosphate reductase
209	733	Gene3D	G3DSA:3.20.70.20	-
10	221	SUPERFAMILY	SSF48168	R1 subunit of ribonucleotide reductase, N-terminal domain
10	221	InterPro	IPR008926	Ribonucleotide reductase R1 subunit, N-terminal
222	740	SUPERFAMILY	SSF51998	PFL-like glycyl radical enzymes

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

0.788

Likely same site as FPocket 5 5.4 Å 7 shared residues 88% of smaller site

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Surrounding area

Pocket 2 P2Rank #2

0.529

Likely same site as FPocket 22 1.3 Å 14 shared residues 93% of smaller site

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Surrounding area

Pocket 3 P2Rank #3

0.511

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Surrounding area

Pocket 4 P2Rank #4

0.362

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Surrounding area

Pocket 5 P2Rank #5

0.166

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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 #22

0.354

Likely same site as P2Rank 2 1.3 Å 14 shared residues 93% of smaller site

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Surrounding area

Pocket 2 FPocket #5

0.325

Likely same site as P2Rank 1 5.4 Å 7 shared residues 88% 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

0.802

Likely same site as FPocket 15 4.8 Å 24 shared residues 89% of smaller site

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Surrounding area

Pocket 2 P2Rank #2

0.434

Likely same site as FPocket 43 1.0 Å 17 shared residues 100% of smaller site

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Surrounding area

Pocket 3 P2Rank #3

0.311

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Surrounding area

Pocket 4 P2Rank #4

0.3

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Surrounding area

Pocket 5 P2Rank #5

0.088

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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 #43

0.663 Unusual size

Likely same site as P2Rank 2 1.0 Å 17 shared residues 100% of smaller site

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Surrounding area

Pocket 2 FPocket #15

0.623 Unusual size

Likely same site as P2Rank 1 4.8 Å 24 shared residues 89% of smaller site

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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_A0A0H3GW79	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold KP13_00958	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.

75 records

Chemistry signal

Structural and bioactivity evidence are both available for this target.

Direct evidence 0 same-protein records

Transferred evidence 25 records from similar proteins

Structural ligands 16 0 loaded crystals

Measured bioactivity 9 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

2A5 PDB via homolog 455.3 Da · LogP -1.11 · TPSA 232.6 Open detail RCSB PDB

3X4 PDB via homolog Detail RCSB PDB

7LL PDB via homolog Detail RCSB PDB

ANP PDB via homolog Detail RCSB PDB

DAT 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
2A5 RCSB PDB	3K8T	P21524	455.3 Da LogP -1.11 TPSA 232.6	2 viol.	✓ Clean	`c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)…`
3X4 RCSB PDB	4X3V	P23921	418.5 Da LogP -0.12 TPSA 158.9	✓ Ro5	✓ Clean	`CC(C)(C(=O)NCCCC[C@H](C(=O)O)N)NC(=O)CN1C(=O)c2…`
7LL RCSB PDB	5TUS	P23921	306.3 Da LogP 3.01 TPSA 81.9	✓ Ro5	Alert	`c1ccc2c(c1)ccc(c2/C=N\NC(=O)c3ccccc3O)O`
ANP RCSB PDB	2CVT	P21524	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)…`
DAT RCSB PDB	4ERM	P00452	411.2 Da LogP -0.72 TPSA 212.4	1 viol.	✓ Clean	`c1nc(c2c(n1)n(cn2)[C@H]3C[C@@H]([C@H](O3)CO[P@]…`
DCP RCSB PDB	1PEO	Q08698	467.2 Da LogP -1.18 TPSA 250.2	2 viol.	✓ Clean	`C1[C@@H]([C@H](O[C@H]1N2C=CC(=NC2=O)N)CO[P@@](=…`
DGT RCSB PDB	5CNU	P00452	507.2 Da LogP -1.31 TPSA 278.9	3 viol.	✓ Clean	`c1nc2c(n1[C@H]3C[C@@H]([C@H](O3)CO[P@@](=O)(O)O…`
DTP RCSB PDB	3UUS	P00452	491.2 Da LogP -0.60 TPSA 258.9	2 viol.	✓ Clean	`c1nc(c2c(n1)n(cn2)[C@H]3C[C@@H]([C@H](O3)CO[P@]…`
E4X RCSB PDB	6L3R	P23921	488.4 Da LogP 4.10 TPSA 105.1	✓ Ro5	✓ Clean	`C[C@H](c1cccc2c1cccc2)[C@@H](C3=NNC(=O)O3)NS(=O…`
E6O RCSB PDB	6L7L	P23921	476.9 Da LogP 2.43 TPSA 148.2	✓ Ro5	✓ Clean	`C[C@H](c1cccc2c1CCC2)[C@@H](C3=NNC(=O)O3)NS(=O)…`
EJ6 RCSB PDB	6LKM	P23921	511.0 Da LogP 3.42 TPSA 117.5	1 viol.	✓ Clean	`Cc1ccc(c(c1C)[C@@H](C)[C@@H](C2=NNC(=O)O2)NS(=O…`
FEO RCSB PDB	4ERM	P00452	127.7 Da LogP -0.07 TPSA 9.2	✓ Ro5	✓ Clean	`O([Fe])[Fe]`
GCQ RCSB PDB	2EUD	P21524	423.2 Da LogP -1.05 TPSA 203.7	✓ Ro5	✓ Clean	`C1=CN(C(=O)N=C1N)[C@H]2C([C@@H]([C@H](O2)CO[P@]…`
MRT RCSB PDB	2ZLG	P21524	1031.2 Da LogP 4.98 TPSA 286.9	3 viol.	✓ Clean	`CC(C)C[C@@H](C(=O)N[C@@H](CC(=O)O)C(=O)N[C@@H](…`
N5P RCSB PDB	3RSR	P21524	518.2 Da LogP 1.54 TPSA 237.3	2 viol.	✓ Clean	`c1cc2c(ccn2C3CC(C(O3)COP(=O)(O)OP(=O)(O)OP(=O)(…`
TTP RCSB PDB	2R1R	P00452	482.2 Da LogP -1.16 TPSA 244.1	2 viol.	✓ Clean	`CC1=CN(C(=O)NC1=O)[C@H]2C[C@@H]([C@H](O2)CO[P@]…`

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
CHEMBL3235141 ChEMBL	P23921	—	342.3 Da LogP 0.10 TPSA 115.5	✓ Ro5	✓ Clean	`Nc1ccn([C@@H]2O[C@H](CNCc3ccco3)[C@@H](O)C2(F)F…`
CHEMBL3235142 ChEMBL	P23921	—	373.4 Da LogP -1.07 TPSA 122.7	✓ Ro5	✓ Clean	`Nc1ccn([C@@H]2O[C@H](CNCCN3CCCC3=O)[C@@H](O)C2(…`
CHEMBL3235143 ChEMBL	P23921	—	370.4 Da LogP -0.20 TPSA 120.2	✓ Ro5	✓ Clean	`C[C@H](NC[C@H]1O[C@@H](n2ccc(N)nc2=O)C(F)(F)[C@…`
CHEMBL3235144 ChEMBL	P23921	—	368.3 Da LogP -0.57 TPSA 111.4	✓ Ro5	✓ Clean	`Nc1ccn([C@@H]2O[C@H](CN3CCn4nccc4C3)[C@@H](O)C2…`
CHEMBL4059739 ChEMBL	P23921	—	399.2 Da LogP 4.08 TPSA 70.9	✓ Ro5	Alert	`COc1cc(Br)ccc1C(=O)N/N=C/c1c(O)ccc2ccccc12`
CHEMBL4067105 ChEMBL	P23921	—	306.3 Da LogP 3.01 TPSA 81.9	✓ Ro5	Alert	`O=C(N/N=C/c1c(O)ccc2ccccc12)c1ccccc1O`
CHEMBL4073197 ChEMBL	P23921	—	339.8 Da LogP 3.54 TPSA 87.7	✓ Ro5	Alert	`Nc1ccc(C(=O)N/N=C/c2c(O)ccc3ccccc23)cc1Cl`
CHEMBL4100050 ChEMBL	P23921	—	306.3 Da LogP 3.01 TPSA 81.9	✓ Ro5	✓ Clean	`O=C(N/N=C/c1ccc2cc(O)ccc2c1)c1ccccc1O`
GEO ChEMBL	P23921	—	263.2 Da LogP -1.29 TPSA 110.6	✓ Ro5	✓ Clean	`C1=CN(C(=O)N=C1N)[C@H]2C([C@@H]([C@H](O2)CO)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
ZINC12495199 ZINC	1.000	411.2 Da LogP -0.72 TPSA 212.4	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1C[C@H](O)[C@@H](CO[P@@](=O…`
ZINC13434873 ZINC	1.000	411.2 Da LogP -0.72 TPSA 212.4	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1C[C@H](O)[C@H](CO[P@@](=O)…`
ZINC13434875 ZINC	1.000	411.2 Da LogP -0.72 TPSA 212.4	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1C[C@H](O)[C@H](CO[P@@](=O)(…`
ZINC13434876 ZINC	1.000	411.2 Da LogP -0.72 TPSA 212.4	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1C[C@@H](O)[C@H](CO[P@](=O)…`
ZINC13434878 ZINC	1.000	411.2 Da LogP -0.72 TPSA 212.4	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1C[C@@H](O)[C@H](CO[P@@](=O)…`
ZINC13507072 ZINC	1.000	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	1.000	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@@…`
ZINC8215728 ZINC	1.000	411.2 Da LogP -0.72 TPSA 212.4	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1C[C@H](O)[C@@H](CO[P@@](=O)…`
ZINC12503703 ZINC	0.982	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	0.982	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…`
ZINC13434879 ZINC	0.981	491.2 Da LogP -0.60 TPSA 258.9	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1C[C@H](O)[C@H](CO[P@@](=O)…`
ZINC13434881 ZINC	0.981	491.2 Da LogP -0.60 TPSA 258.9	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1C[C@H](O)[C@H](CO[P@@](=O)(…`
ZINC13434883 ZINC	0.981	491.2 Da LogP -0.60 TPSA 258.9	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1C[C@@H](O)[C@H](CO[P@@](=O…`
ZINC13434884 ZINC	0.981	491.2 Da LogP -0.60 TPSA 258.9	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1C[C@@H](O)[C@H](CO[P@@](=O)…`
ZINC8215662 ZINC	0.981	491.2 Da LogP -0.60 TPSA 258.9	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1C[C@H](O)[C@@H](CO[P@@](=O)…`
ZINC8664605 ZINC	0.981	491.2 Da LogP -0.60 TPSA 258.9	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1C[C@H](O)[C@@H](CO[P@@](=O…`
ZINC12503053 ZINC	0.959	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	0.959	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	0.959	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	0.959	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	0.959	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	0.959	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…`
ZINC12958401 ZINC	0.849	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	0.849	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	0.849	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	0.849	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	0.849	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	0.849	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	0.849	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	0.849	331.2 Da LogP -0.83 TPSA 165.8	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1C[C@@H](O)[C@H](COP(=O)(O)O…`
ZINC12296728 ZINC	0.845	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)…`
ZINC13527599 ZINC	0.845	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	0.845	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)…`
ZINC1532627 ZINC	0.845	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)…`
ZINC1730395 ZINC	0.845	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…`
ZINC3869846 ZINC	0.845	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	0.845	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	0.845	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…`
ZINC111459735 ZINC	0.836	481.2 Da LogP -1.20 TPSA 249.9	2 viol.	✓ Clean	`Cc1cn([C@@H]2C[C@H](N)[C@H](CO[P@@](=O)(O)O[P@@…`
ZINC138164075 ZINC	0.836	498.2 Da LogP 0.21 TPSA 227.1	2 viol.	✓ Clean	`Cc1cn([C@@H]2C[C@H](O)[C@H](CO[P@@](=O)(O)O[P@@…`
ZINC196576711 ZINC	0.825	490.2 Da LogP -0.63 TPSA 264.7	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1C[C@H](N)[C@H](CO[P@@](=O)…`
ZINC142512519 ZINC	0.818	498.2 Da LogP 0.21 TPSA 227.1	2 viol.	✓ Clean	`Cc1cn([C@@H]2C[C@H](O)[C@H](CO[P@@](=O)(O)O[P@@…`
ZINC13523519 ZINC	0.804	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(…`
ZINC1532628 ZINC	0.804	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	0.804	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…`
ZINC2047010 ZINC	0.804	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…`
ZINC3870253 ZINC	0.804	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	0.804	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)…`
ZINC6523446 ZINC	0.804	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(=…`
ZINC113218151 ZINC	0.800	486.1 Da LogP -1.33 TPSA 244.1	2 viol.	✓ Clean	`O=c1[nH]c(=O)n([C@H]2C[C@H](O)[C@@H](CO[P@](=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.

Cross-references

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

Sequence

UniProt A0A0H3GW79

Chemistry

ChEMBL CHEMBL3235141 ChEMBL CHEMBL3235142 ChEMBL CHEMBL3235143 ChEMBL CHEMBL3235144 ChEMBL CHEMBL4059739 ChEMBL CHEMBL4067105 ChEMBL CHEMBL4073197 ChEMBL CHEMBL4100050 ChEMBL GEO