Protein target profile

KP13_00629

DNA polymerase I

Genome: KpKP13 Gene: AHE47103.1 polA 3D evidence: AlphaFold DB model + ColabFold model UniProt A0A0H3GPI6

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Length 930

Pocket druggability 0.408

Direct ligand evidence 0 85 total records

Functional annotation 0 EC 8 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

Moderate predicted binding pocket FPocket selected-pocket score 0.41. This supports review but is not experimental validation. Second pocket predictor agrees P2Rank predicted binding-site probability 0.77. Structure available AlphaFold DB model + ColabFold model Ligand evidence via structure/bioactivity 35 structural and 0 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 (%): 36.431 Lower values reduce human off-target concern.
Human E-value: 3.6300000000000014e-43
Gut microbiome similarity: 3.9% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 90.323 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: 91.17 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 0.408

Structure A0A0H3GPI6

Pocket Pocket 64

P2Rank 0.772

Structure A0A0H3GPI6

Pocket Pocket 1

ColabFold model

FPocket 0.252 · Pocket 61

P2Rank 0.754 · Pocket 1

Core conservation Accessory gene

Roary accessory

CoreCruncher accessory

Gut microbiome 184 / 4744 genomes with a hit

Prevalence 3.9%

Cross-references

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

Sequence

UniProt A0A0H3GPI6

Sequence

Primary amino-acid sequence viewer.

MVQIPENPLILVDGSSYLYRAYHAFPPLTNSAGEPTGAMYGVLNMLRSLILQYQPTHAVVVFDAKGKTFRDELFEHYKSHRPPMPDDLRAQIEPLHKMVKAMGLPLMAVPGVEADDVIGTLAREAERAGRPVLISTGDKDMAQLVTPGITLINTMTNTILGPDEVVTKYGVPPELIIDFLALMGDSSDNIPGVPGVGEKTAQALLQGLGGLDTLYAEPEKIAELSFRGAKTMAAKLEQNKDVAYLSYQLATIKTDVELELTCEELEVQPPAADDLLALFRQYEFKRWTTDVEAGKWLQAKGGKPAAKPAVPAAAAEAEEEVEAATALSAEHYVTILDEATLLTWIDKLKQAPLFAFDTETDSLDNISANMVGLSFAVEPGVAAYVPVAHDYLDAPDQIPRERVLTLLKPLLEDEKVLKVGQNLKYDRGILANYDIELRGIAFDTMLESYILDSVAGRHDMDSLSDRWLKHKTITFEEIAGKGKNQLTFNQIALEEAGRYAAEDADVTLQLHLKMWPKLQQHEGPLNIFQHIEMPLVPVLSRVERNGVKIDPAVLHAHSQEIAQRLVELEQRAHEIAGEAFNLSSTKQLQTILFEKQGIKPLKKTPGGAPSTSEEVLEELALDYPLPKVILEYRGLAKLKSTYTDKLPLMINPKTGRVHTSYHQAVTATGRLSSTDPNLQNIPVRNEEGRRIRQAFIAPEDYVIVSADYSQIELRIMAHLSRDKGLLTAFAEGKDIHRATAAEVFGLPLDSVSSEQRRSAKAINFGLIYGMSAFGLARQLNIPRKEAQKYMDLYFERYPGVLEYMERTRAQAKEQGYVETLDGRRLYLPDIKSSNGARRAGAERAAINAPMQGTAADIIKRAMIAVDEWLRSEKPRVRMIMQVHDELVFEVHKDELDAVSKKIHELMENSTTLAVPLLVEVGSGENWDQAH

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

8 GO

Gene Ontology (GO)

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:0003676 Binding to a nucleic acid.
GO:0003887 Catalysis of the reaction: deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1); DNA-template-directed extension of the 3'-end of a DNA strand by one nucleotide at a time.
GO:0008408 Catalysis of the hydrolysis of ester linkages within nucleic acids by removing nucleotide residues from the 3' end.
GO:0006261 A DNA replication process that uses parental DNA as a template for the DNA-dependent DNA polymerases that synthesize the new strands.
GO:0003824 Catalysis of a biochemical reaction at physiological temperatures. In biologically catalyzed reactions, the reactants are known as substrates, and the catalysts are naturally occurring macromolecular substances known as enzymes. Enzymes possess specific binding sites for substrates, and are usually composed wholly or largely of protein, but RNA that has catalytic activity (ribozyme) is often also regarded as enzymatic.
GO:0006139 Any cellular metabolic process involving nucleobases, nucleosides, nucleotides and nucleic acids.
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.

65 records

Show feature table

Start	End	DB	Term	Name
756	775	ProSitePatterns	PS00447	DNA polymerase family A signature.
756	775	InterPro	IPR019760	DNA-directed DNA polymerase, family A, conserved site
688	894	SMART	SM00482	polaultra3
688	894	InterPro	IPR001098	DNA-directed DNA polymerase, family A, palm domain
173	268	FunFam	G3DSA:1.10.150.20:FF:000003	DNA polymerase I
347	541	CDD	cd06139	DNA_polA_I_Ecoli_like_exo
332	519	SMART	SM00474	35exoneu6
332	519	InterPro	IPR002562	3'-5' exonuclease domain
554	927	Pfam	PF00476	DNA polymerase family A
554	927	InterPro	IPR001098	DNA-directed DNA polymerase, family A, palm domain
332	519	Pfam	PF01612	3'-5' exonuclease
525	930	SUPERFAMILY	SSF56672	DNA/RNA polymerases
525	930	InterPro	IPR043502	DNA/RNA polymerase superfamily
173	208	SMART	SM00279	HhH_4
173	208	InterPro	IPR008918	Helix-hairpin-helix motif, class 2
711	854	FunFam	G3DSA:1.10.150.20:FF:000002	DNA polymerase I
545	660	Gene3D	G3DSA:1.20.1060.10	Taq DNA Polymerase; Chain T, domain 4
173	268	Gene3D	G3DSA:1.10.150.20	-
171	271	Pfam	PF01367	5'-3' exonuclease, C-terminal SAM fold
171	271	InterPro	IPR020045	DNA polymerase I-like, H3TH domain
7	268	SMART	SM00475	53exo3
7	268	InterPro	IPR002421	5'-3' exonuclease
171	291	SUPERFAMILY	SSF47807	5' to 3' exonuclease, C-terminal subdomain
171	291	InterPro	IPR036279	5'-3' exonuclease, C-terminal domain superfamily
11	166	CDD	cd09859	PIN_53EXO
173	252	CDD	cd09898	H3TH_53EXO
173	252	InterPro	IPR020045	DNA polymerase I-like, H3TH domain
9	170	Pfam	PF02739	5'-3' exonuclease, N-terminal resolvase-like domain
9	170	InterPro	IPR020046	5'-3' exonuclease, alpha-helical arch, N-terminal
7	170	SUPERFAMILY	SSF88723	PIN domain-like
7	170	InterPro	IPR029060	PIN-like domain superfamily
888	908	Coils	Coil	Coil
702	725	PRINTS	PR00868	DNA-polymerase family A (pol I) signature
702	725	InterPro	IPR002298	DNA polymerase A
756	781	PRINTS	PR00868	DNA-polymerase family A (pol I) signature
756	781	InterPro	IPR002298	DNA polymerase A
732	745	PRINTS	PR00868	DNA-polymerase family A (pol I) signature
732	745	InterPro	IPR002298	DNA polymerase A
793	804	PRINTS	PR00868	DNA-polymerase family A (pol I) signature
793	804	InterPro	IPR002298	DNA polymerase A
877	890	PRINTS	PR00868	DNA-polymerase family A (pol I) signature
877	890	InterPro	IPR002298	DNA polymerase A
657	679	PRINTS	PR00868	DNA-polymerase family A (pol I) signature
657	679	InterPro	IPR002298	DNA polymerase A
815	826	PRINTS	PR00868	DNA-polymerase family A (pol I) signature
815	826	InterPro	IPR002298	DNA polymerase A
847	863	PRINTS	PR00868	DNA-polymerase family A (pol I) signature
847	863	InterPro	IPR002298	DNA polymerase A
680	695	PRINTS	PR00868	DNA-polymerase family A (pol I) signature
680	695	InterPro	IPR002298	DNA polymerase A
2	171	Gene3D	G3DSA:3.40.50.1010	-
329	520	SUPERFAMILY	SSF53098	Ribonuclease H-like
329	520	InterPro	IPR012337	Ribonuclease H-like superfamily
329	544	FunFam	G3DSA:3.30.420.10:FF:000026	DNA polymerase I
550	927	CDD	cd08637	DNA_pol_A_pol_I_C
9	930	NCBIfam	TIGR00593	DNA polymerase I
9	930	InterPro	IPR018320	DNA polymerase 1
666	926	Gene3D	G3DSA:3.30.70.370	-
2	172	FunFam	G3DSA:3.40.50.1010:FF:000001	DNA polymerase I
711	854	Gene3D	G3DSA:1.10.150.20	-
545	660	FunFam	G3DSA:1.20.1060.10:FF:000001	DNA polymerase I
328	544	Gene3D	G3DSA:3.30.420.10	-
328	544	InterPro	IPR036397	Ribonuclease H superfamily
225	930	PANTHER	PTHR10133	DNA POLYMERASE I
225	930	InterPro	IPR002298	DNA polymerase A

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 #64

0.408

Likely same site as P2Rank 2 1.6 Å 25 shared residues 100% 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

0.772

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Surrounding area

Site 2 P2Rank #2

0.697

Likely same site as FPocket 64 1.6 Å 25 shared residues 100% of smaller site

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Surrounding area

Site 3 P2Rank #3

0.242

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Surrounding area

Site 4 P2Rank #4

0.2

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Surrounding area

Site 5 P2Rank #5

0.117

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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

0.754

Likely same site as FPocket 61 3.9 Å 10 shared residues 67% of smaller site

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Surrounding area

Site 2 P2Rank #2

0.673

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Surrounding area

Site 3 P2Rank #3

0.376

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Surrounding area

Site 4 P2Rank #4

0.236

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Surrounding area

Site 5 P2Rank #5

0.069

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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_A0A0H3GPI6	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold KP13_00629	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.

85 records

Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 same-protein records

Transferred evidence 35 records from similar proteins

Structural ligands 35 0 loaded crystals

Measured bioactivity 0 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

0KL PDB via homolog 549.3 Da · LogP -1.38 · TPSA 270.2 Open detail RCSB PDB

0L3 PDB via homolog Detail RCSB PDB

0L4 PDB via homolog Detail RCSB PDB

0L5 PDB via homolog Detail RCSB PDB

0L6 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
0KL RCSB PDB	4DFJ	P19821	549.3 Da LogP -1.38 TPSA 270.2	3 viol.	✓ Clean	`C1C(C(OC1N2C=C(C(=O)NC2=O)C#CCCCN)COP(=O)(O)OP(…`
0L3 RCSB PDB	4DF4	P19821	741.6 Da LogP 2.37 TPSA 295.3	3 viol.	✓ Clean	`c1c(c2c(ncnc2n1C3CC(C(O3)COP(=O)(O)OP(=O)(O)OP(…`
0L4 RCSB PDB	4DF8	P19821	571.3 Da LogP 0.10 TPSA 272.0	3 viol.	✓ Clean	`c1c(c2c(ncnc2n1C3CC(C(O3)COP(=O)(O)OP(=O)(O)OP(…`
0L5 RCSB PDB	4DFK	P19821	719.5 Da LogP 0.89 TPSA 293.5	3 viol.	✓ Clean	`C1C(C(OC1N2C=C(C(=O)NC2=O)C#CCCCNC(=O)CCCCCCCCC…`
0L6 RCSB PDB	4DFM	P19821	550.3 Da LogP -1.26 TPSA 273.7	3 viol.	✓ Clean	`C1C(C(OC1N2CC(=C(NC2=O)N)C#CCCCN)COP(=O)(O)OP(=…`
0L7 RCSB PDB	4DFP	P19821	587.3 Da LogP -0.61 TPSA 292.0	3 viol.	✓ Clean	`c1c(c2c(n1C3CC(C(O3)COP(=O)(O)OP(=O)(O)OP(=O)(O…`
0R5 RCSB PDB	4ELT	P19821	592.3 Da LogP -0.09 TPSA 244.1	3 viol.	✓ Clean	`C#Cc1ccc(cc1)C#CC2=CN(C(=O)NC2=O)C3CC(C(O3)COP(…`
0R6 RCSB PDB	4ELU	P19821	591.3 Da LogP 0.20 TPSA 250.2	3 viol.	✓ Clean	`C#Cc1ccc(cc1)C#CC2=CN(C(=O)N=C2N)C3CC(C(O3)COP(…`
0R7 RCSB PDB	4ELV	P19821	575.3 Da LogP 1.23 TPSA 230.0	2 viol.	✓ Clean	`C#Cc1ccc(cc1)C#CC2=CN(C(=O)N=C2N)C3CCC(O3)COP(=…`
15P RCSB PDB	3M8R	P19821	1529.8 Da LogP 0.17 TPSA 334.1	2 viol.	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCO…`
5SI RCSB PDB	3SV3	P19821	531.3 Da LogP 2.67 TPSA 194.2	1 viol.	✓ Clean	`Cc1ccc2c(c1)C=CN(C2=S)[C@H]3C[C@@H]([C@H](O3)CO…`
72J RCSB PDB	5SZT	P19821	743.6 Da LogP 3.03 TPSA 295.3	3 viol.	✓ Clean	`c1c(c2c(ncnc2n1[C@H]3C[C@@H]([C@H](O3)COP(=O)(O…`
91R RCSB PDB	5NKL	P19821	566.2 Da LogP -0.52 TPSA 277.8	3 viol.	✓ Clean	`c1c(cn(c1[N+](=O)[O-])C2CC(C(O2)COP(=O)(O)OP(=O…`
A5J RCSB PDB	5W6K	P19821	513.2 Da LogP -0.51 TPSA 292.1	3 viol.	✓ Clean	`c1c(c(nc(c1N(O)O)N)O)[C@H]2C[C@@H]([C@H](O2)COP…`
AF RCSB PDB	1UA1	P52026	181.2 Da LogP 2.84 TPSA 26.0	✓ Ro5	✓ Clean	`c1ccc-2c(c1)Cc3c2ccc(c3)N`
AUL RCSB PDB	5E41	P19821	721.5 Da LogP 1.55 TPSA 293.5	3 viol.	✓ Clean	`C1[C@@H]([C@H](O[C@H]1N2C=C(C(=O)NC2=O)/C=C/CCC…`
BMR RCSB PDB	4C8K	P19821	514.3 Da LogP 2.38 TPSA 198.5	1 viol.	✓ Clean	`COc1cc2ccccc2cc1[C@H]3C[C@@H]([C@H](O3)COP(=O)(…`
D3T RCSB PDB	3HP6	Q5KWC1	466.2 Da LogP -0.13 TPSA 223.9	✓ Ro5	✓ Clean	`CC1=CN(C(=O)NC1=O)[C@H]2CC[C@H](O2)CO[P@@](=O)(…`
DCP RCSB PDB	1LV5	P52026	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@@](=…`
DCT RCSB PDB	6VDD	A0QYZ2	451.2 Da LogP -0.15 TPSA 230.0	1 viol.	✓ Clean	`C1C[C@@H](O[C@@H]1CO[P@](=O)(O)O[P@](=O)(O)OP(=…`
DDS RCSB PDB	1QSY	P19821	475.2 Da LogP 0.43 TPSA 238.7	1 viol.	✓ Clean	`c1nc(c2c(n1)n(cn2)[C@H]3CC[C@H](O3)CO[P@@](=O)(…`
DG3 RCSB PDB	1QSS	P19821	491.2 Da LogP -0.28 TPSA 258.6	2 viol.	✓ Clean	`c1nc2c(n1[C@H]3CC[C@H](O3)CO[P@@](=O)(O)O[P@](=…`
DGT RCSB PDB	5YTD	P19821	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	5YTC	P19821	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@]…`
DZ4 RCSB PDB	6DSU	E1C9K5	490.2 Da LogP -1.03 TPSA 261.7	2 viol.	✓ Clean	`c1nc(c2c(n1)n(cn2)[C@H]3C[C@@H]([C@H](O3)CO[P@@…`
HHZ RCSB PDB	6Q4U	P19821	645.3 Da LogP -1.52 TPSA 304.6	3 viol.	✓ Clean	`c1c(c2c(ncnc2n1C3CC(C(O3)COP(=O)(O)OP(=O)(O)OP(…`
HXB RCSB PDB	3M8S	P19821	496.2 Da LogP -0.77 TPSA 244.1	2 viol.	✓ Clean	`CC1=CN(C(=O)NC1=O)[C@H]2C[C@@H]([C@@](O2)(C)CO[…`
HXZ RCSB PDB	3M8R	P19821	510.2 Da LogP -0.38 TPSA 244.1	3 viol.	✓ Clean	`CC[C@]1([C@H](C[C@@H](O1)N2C=C(C(=O)NC2=O)C)O)C…`
N5P RCSB PDB	3T3F	P19821	518.2 Da LogP 1.54 TPSA 237.3	2 viol.	✓ Clean	`c1cc2c(ccn2C3CC(C(O3)COP(=O)(O)OP(=O)(O)OP(=O)(…`
NZI RCSB PDB	5OXJ	P19821	490.2 Da LogP 0.32 TPSA 227.1	1 viol.	✓ Clean	`c1ccc2c(c1)NC(=O)N2[C@H]3C[C@@H]([C@H](O3)COP(=…`
POP RCSB PDB	4DSK	E1C9K5	176.0 Da LogP -2.08 TPSA 129.9	✓ Ro5	✓ Clean	`O[P@@](=O)([O-])O[P@@](=O)(O)[O-]`
SSJ RCSB PDB	3OJU	P19821	631.4 Da LogP 0.07 TPSA 267.6	3 viol.	✓ Clean	`CC1(C=C(C(N1O)(C)C)C#CC2=CN(C(=O)NC2=O)C3CC(C(O…`
TTP RCSB PDB	1QTM	P19821	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@]…`
XG4 RCSB PDB	6FBC	P19821	506.2 Da LogP -1.73 TPSA 281.7	3 viol.	✓ Clean	`c1nc2c(n1[C@H]3C[C@@H]([C@H](O3)CO[P@@](=O)(N[P…`
XJS RCSB PDB	3OJS	P19821	1044.9 Da LogP -1.09 TPSA 392.4	3 viol.	✓ Clean	`CCN(CC)C(=O)CCC(=O)NCCCN(CCCNC(=O)CCC(=O)N(CC)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).

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
ZINC12503365 ZINC	1.000	467.2 Da LogP -1.18 TPSA 250.2	2 viol.	✓ Clean	`Nc1ccn([C@H]2C[C@@H](O)[C@@H](CO[P@](=O)(O)O[P@…`
ZINC13435050 ZINC	1.000	467.2 Da LogP -1.18 TPSA 250.2	2 viol.	✓ Clean	`Nc1ccn([C@@H]2C[C@H](O)[C@H](CO[P@@](=O)(O)O[P@…`
ZINC13516800 ZINC	1.000	451.2 Da LogP -0.15 TPSA 230.0	1 viol.	✓ Clean	`Nc1ccn([C@H]2CC[C@@H](CO[P@@](=O)(O)O[P@@](=O)(…`
ZINC1580161 ZINC	1.000	208.3 Da LogP -0.33 TPSA 57.2	✓ Ro5	✓ Clean	`COCCOCCOCCOCCO`
ZINC16052118 ZINC	1.000	340.4 Da LogP -0.28 TPSA 84.8	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCO`
ZINC16052257 ZINC	1.000	384.5 Da LogP -0.26 TPSA 94.1	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC34317654 ZINC	1.000	472.6 Da LogP -0.23 TPSA 112.5	1 viol.	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC44076059 ZINC	1.000	428.5 Da LogP -0.24 TPSA 103.3	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC5210101 ZINC	1.000	252.3 Da LogP -0.31 TPSA 66.4	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCO`
ZINC5997860 ZINC	1.000	296.4 Da LogP -0.29 TPSA 75.6	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCO`
ZINC8215945 ZINC	1.000	467.2 Da LogP -1.18 TPSA 250.2	2 viol.	✓ Clean	`Nc1ccn([C@H]2C[C@H](O)[C@@H](CO[P@@](=O)(O)O[P@…`
ZINC13435042 ZINC	0.959	387.2 Da LogP -1.30 TPSA 203.7	✓ Ro5	✓ Clean	`Nc1ccn([C@@H]2C[C@H](O)[C@H](CO[P@](=O)(O)OP(=O…`
ZINC14960508 ZINC	0.959	387.2 Da LogP -1.30 TPSA 203.7	✓ Ro5	✓ Clean	`Nc1ccn([C@@H]2C[C@H](O)[C@@H](CO[P@](=O)(O)OP(=…`
ZINC142514175 ZINC	0.818	483.2 Da LogP 0.19 TPSA 233.1	2 viol.	✓ Clean	`Nc1ccn([C@@H]2C[C@H](O)[C@H](CO[P@@](=O)(O)O[P@…`
ZINC12503923 ZINC	0.804	307.2 Da LogP -1.42 TPSA 157.1	✓ Ro5	✓ Clean	`Nc1ccn([C@@H]2C[C@@H](O)[C@@H](COP(=O)(O)O)O2)c…`
ZINC12503924 ZINC	0.804	307.2 Da LogP -1.42 TPSA 157.1	✓ Ro5	✓ Clean	`Nc1ccn([C@H]2C[C@@H](O)[C@@H](COP(=O)(O)O)O2)c(…`
ZINC1532581 ZINC	0.804	307.2 Da LogP -1.42 TPSA 157.1	✓ Ro5	✓ Clean	`Nc1ccn([C@@H]2C[C@@H](O)[C@H](COP(=O)(O)O)O2)c(…`
ZINC3645374 ZINC	0.804	307.2 Da LogP -1.42 TPSA 157.1	✓ Ro5	✓ Clean	`Nc1ccn([C@@H]2C[C@H](O)[C@@H](COP(=O)(O)O)O2)c(…`
ZINC3861759 ZINC	0.804	307.2 Da LogP -1.42 TPSA 157.1	✓ Ro5	✓ Clean	`Nc1ccn([C@H]2C[C@H](O)[C@@H](COP(=O)(O)O)O2)c(=…`
ZINC3869816 ZINC	0.804	307.2 Da LogP -1.42 TPSA 157.1	✓ Ro5	✓ Clean	`Nc1ccn([C@@H]2C[C@H](O)[C@H](COP(=O)(O)O)O2)c(=…`
ZINC3869817 ZINC	0.804	307.2 Da LogP -1.42 TPSA 157.1	✓ Ro5	✓ Clean	`Nc1ccn([C@H]2C[C@H](O)[C@H](COP(=O)(O)O)O2)c(=O…`
ZINC3869818 ZINC	0.804	307.2 Da LogP -1.42 TPSA 157.1	✓ Ro5	✓ Clean	`Nc1ccn([C@H]2C[C@@H](O)[C@H](COP(=O)(O)O)O2)c(=…`
ZINC71404913 ZINC	0.804	463.2 Da LogP 0.26 TPSA 209.7	1 viol.	✓ Clean	`C[P@@](=O)(O[P@@](=O)(O)OC[C@H]1O[C@@H](n2ccc(N…`
ZINC71404916 ZINC	0.804	463.2 Da LogP 0.26 TPSA 209.7	1 viol.	✓ Clean	`C[P@@](=O)(O)O[P@@](C)(=O)O[P@@](=O)(O)OC[C@H]1…`
ZINC8215971 ZINC	0.796	468.1 Da LogP -1.06 TPSA 244.4	2 viol.	✓ Clean	`O=c1nc(O)ccn1[C@H]1C[C@H](O)[C@@H](CO[P@@](=O)(…`
ZINC169292613 ZINC	0.750	492.2 Da LogP 0.14 TPSA 278.7	1 viol.	Alert	`[N-]=[N+]=N[C@@H]1C[C@H](n2ccc(N)nc2=O)O[C@@H]1…`
ZINC111437949 ZINC	0.741	481.2 Da LogP -0.72 TPSA 236.2	2 viol.	✓ Clean	`CNc1ccn([C@@H]2C[C@H](O)[C@H](CO[P@@](=O)(O)O[P…`
ZINC32016993 ZINC	0.737	451.2 Da LogP -0.15 TPSA 230.0	1 viol.	✓ Clean	`Nc1ccn([C@@H]2CC[C@H](CO[P@@](=O)(O)O[P@](=O)(O…`
ZINC12502055 ZINC	0.732	483.2 Da LogP -2.21 TPSA 270.4	2 viol.	✓ Clean	`Nc1ccn([C@@H]2O[C@@H](CO[P@@](=O)(O)O[P@@](=O)(…`
ZINC12502057 ZINC	0.732	483.2 Da LogP -2.21 TPSA 270.4	2 viol.	✓ Clean	`Nc1ccn([C@H]2O[C@@H](CO[P@@](=O)(O)O[P@@](=O)(O…`
ZINC12502058 ZINC	0.732	483.2 Da LogP -2.21 TPSA 270.4	2 viol.	✓ Clean	`Nc1ccn([C@@H]2O[C@H](CO[P@@](=O)(O)O[P@@](=O)(O…`
ZINC13431057 ZINC	0.732	483.2 Da LogP -2.21 TPSA 270.4	2 viol.	✓ Clean	`Nc1ccn([C@H]2O[C@@H](CO[P@@](=O)(O)O[P@@](=O)(O…`
ZINC13431059 ZINC	0.732	483.2 Da LogP -2.21 TPSA 270.4	2 viol.	✓ Clean	`Nc1ccn([C@@H]2O[C@@H](CO[P@@](=O)(O)O[P@@](=O)(…`
ZINC25726736 ZINC	0.732	483.2 Da LogP -2.21 TPSA 270.4	2 viol.	✓ Clean	`Nc1ccn([C@H]2O[C@@H](CO[P@@](=O)(O)O[P@@](=O)(O…`
ZINC3861746 ZINC	0.732	483.2 Da LogP -2.21 TPSA 270.4	2 viol.	✓ Clean	`Nc1ccn([C@@H]2O[C@H](CO[P@](=O)(O)O[P@@](=O)(O)…`
ZINC53683723 ZINC	0.732	483.2 Da LogP -2.21 TPSA 270.4	2 viol.	✓ Clean	`Nc1ccn([C@@H]2O[C@@H](CO[P@@](=O)(O)O[P@@](=O)(…`
ZINC82142138 ZINC	0.732	483.2 Da LogP -2.21 TPSA 270.4	2 viol.	✓ Clean	`Nc1ccn([C@@H]2O[C@H](CO[P@@](=O)(O)O[P@@](=O)(O…`
ZINC82142140 ZINC	0.732	483.2 Da LogP -2.21 TPSA 270.4	2 viol.	✓ Clean	`Nc1ccn([C@@H]2O[C@H](CO[P@@](=O)(O)O[P@@](=O)(O…`
ZINC575419714 ZINC	0.727	312.4 Da LogP 0.42 TPSA 66.4	✓ Ro5	✓ Clean	`COCCOCCOCCSCCOCCOCCO`
ZINC218114467 ZINC	0.724	467.2 Da LogP -1.18 TPSA 250.2	2 viol.	✓ Clean	`Nc1ccn([C@@H]2O[C@H](CO[P@@](=O)(O)O[P@@](=O)(O…`
ZINC31440313 ZINC	0.724	467.2 Da LogP -1.18 TPSA 250.2	2 viol.	✓ Clean	`Nc1ccn([C@@H]2O[C@H](CO[P@@](=O)(O)O[P@@](=O)(O…`
ZINC142487928 ZINC	0.719	483.2 Da LogP -1.48 TPSA 270.4	2 viol.	✓ Clean	`Nc1nc(=O)n([C@@H]2C[C@H](O)[C@H](CO[P@@](=O)(O)…`
ZINC13588928 ZINC	0.712	469.2 Da LogP -0.24 TPSA 230.0	1 viol.	✓ Clean	`Nc1ccn([C@@H]2CS[C@H](CO[P@](=O)(O)O[P@](=O)(O)…`
ZINC115163232 ZINC	0.700	222.3 Da LogP 0.07 TPSA 57.2	✓ Ro5	✓ Clean	`COCCOCCOCCOCCCO`
ZINC258837490 ZINC	0.700	354.4 Da LogP 0.11 TPSA 84.8	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCCO`
ZINC12504413 ZINC	0.696	403.2 Da LogP -2.33 TPSA 223.9	2 viol.	✓ Clean	`Nc1ccn([C@H]2O[C@@H](CO[P@@](=O)(O)OP(=O)(O)O)[…`
ZINC12504414 ZINC	0.696	403.2 Da LogP -2.33 TPSA 223.9	2 viol.	✓ Clean	`Nc1ccn([C@@H]2O[C@H](CO[P@@](=O)(O)OP(=O)(O)O)[…`
ZINC13431047 ZINC	0.696	403.2 Da LogP -2.33 TPSA 223.9	2 viol.	✓ Clean	`Nc1ccn([C@@H]2O[C@@H](CO[P@@](=O)(O)OP(=O)(O)O)…`
ZINC13548733 ZINC	0.696	403.2 Da LogP -2.33 TPSA 223.9	2 viol.	✓ Clean	`Nc1ccn([C@@H]2O[C@H](CO[P@@](=O)(O)OP(=O)(O)O)[…`
ZINC33913782 ZINC	0.696	403.2 Da LogP -2.33 TPSA 223.9	2 viol.	✓ Clean	`Nc1ccn([C@@H]2O[C@H](CO[P@@](=O)(O)OP(=O)(O)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.