Protein profile

KP13_00629

DNA polymerase I

Genome: KpKP13

Gene: AHE47103.1 polA Structure source: AlphaFold + ColabFold UniProt A0A0H3GPI6

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Amino acids 930

Annotations 8

Features 65

PDB binders 35

Druggability 0.408

Overview

Basic information about this protein and its source genome.

Accession: KP13_00629
Assembly: Klebsiella pneumoniae subsp. pneumoniae Kp13, complete sequence
Gene: AHE47103.1 polA
Status: annotated
Amino acids: 930
Structure source: AlphaFold + ColabFold

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.

Target profile

Computed evidence for target prioritization.

Human off-target: hit
Human identity (%): 36.431
Human E-value: 3.6300000000000014e-43
Gut microbiome off-target: hit
Essential (DEG): Y
DEG identity (%): 90.323
DEG E-value: 0.0
Localization: Cytoplasmic
ColabFold pLDDT: 91.17

Selected Druggability evidence

AlphaFold / UniProt model

Selected Druggability is the FPocket score chosen for ranking using the curated structure priority. The 3D viewer may show a different loaded structure, so its 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

Normalized 0.039

Sequence

Primary amino-acid sequence viewer.

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 Features

Domain/signature hits 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; predicted models typically cover the full protein.

Loading 3D structure...

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Structural evidence

0 + 2

Experimental PDB entries and predicted models. Click Switch to display a different structure in the viewer.

Entry	Method	Resolution	Chain	Coverage	Links	Status
AlphaFold AF_A0A0H3GPI6	AlphaFold	—	—	full sequence	—	Viewing
ColabFold KP13_00629	ColabFold	—	—	full sequence	—	Loaded

Pocket details FPocket · P2Rank — toggle visibility and zoom from here, or open full viewer

Pockets (FPOCKET)

Showing top-ranked FPocket candidates by druggability. Druggability is color-coded: high (0.7 or higher), medium (0.4 to 0.69), low (below 0.4).

FPOCKET	Sticks	Spheres	Surfaces	Druggability	Labels	Zoom	Positions
64				0.408

Pockets (P2RANK)

Showing top-ranked P2Rank candidates by probability. Probability is color-coded per P2Rank calibration: high (≥ 0.5), medium (0.2 – 0.49), low (< 0.2).

P2RANK	Score	Probability
1	13.84	0.701
2	3.99	0.159
3	3.45	0.125
4	3.18	0.108
5	3.09	0.103

Pockets (FPOCKET)

Showing top-ranked FPocket candidates by druggability. Druggability is color-coded: high (0.7 or higher), medium (0.4 to 0.69), low (below 0.4).

FPOCKET	Sticks	Spheres	Surfaces	Druggability	Labels	Zoom	Positions
61				0.252

Pockets (P2RANK)

Showing top-ranked P2Rank candidates by probability. Probability is color-coded per P2Rank calibration: high (≥ 0.5), medium (0.2 – 0.49), low (< 0.2).

P2RANK	Score	Probability
1	12.55	0.654
2	11.65	0.62
3	4.47	0.19
4	4.39	0.184
5	2.0	0.043

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

Highest-confidence structural evidence: ligands co-crystallized with this exact protein. If the source PDB is loaded in TPW, 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	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	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	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	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	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	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	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	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	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	3M8R	P19821	1529.8 Da LogP 0.17 TPSA 334.1	2 viol.	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCO…`
5SI	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	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	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	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	1UA1	P52026	181.2 Da LogP 2.84 TPSA 26.0	✓ Ro5	✓ Clean	`c1ccc-2c(c1)Cc3c2ccc(c3)N`
AUL	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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	4DSK	E1C9K5	176.0 Da LogP -2.08 TPSA 129.9	✓ Ro5	✓ Clean	`O[P@@](=O)([O-])O[P@@](=O)(O)[O-]`
SSJ	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	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	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	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	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	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	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	1.000	208.3 Da LogP -0.33 TPSA 57.2	✓ Ro5	✓ Clean	`COCCOCCOCCOCCO`
ZINC16052118	1.000	340.4 Da LogP -0.28 TPSA 84.8	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCO`
ZINC16052257	1.000	384.5 Da LogP -0.26 TPSA 94.1	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC34317654	1.000	472.6 Da LogP -0.23 TPSA 112.5	1 viol.	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC44076059	1.000	428.5 Da LogP -0.24 TPSA 103.3	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC5210101	1.000	252.3 Da LogP -0.31 TPSA 66.4	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCO`
ZINC5997860	1.000	296.4 Da LogP -0.29 TPSA 75.6	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCO`
ZINC8215945	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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	0.727	312.4 Da LogP 0.42 TPSA 66.4	✓ Ro5	✓ Clean	`COCCOCCOCCSCCOCCOCCO`
ZINC218114467	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	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	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	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	0.700	222.3 Da LogP 0.07 TPSA 57.2	✓ Ro5	✓ Clean	`COCCOCCOCCOCCCO`
ZINC258837490	0.700	354.4 Da LogP 0.11 TPSA 84.8	✓ Ro5	✓ Clean	`COCCOCCOCCOCCOCCOCCOCCCO`
ZINC12504413	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	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	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	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	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.