Protein profile

KP13_00712

Nitrite reductase [NAD(P)H] large subunit

Genome: KpKP13

Gene: AHE42330.1 nirB Structure source: AlphaFold + ColabFold UniProt A0A0H3GYE4

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Amino acids 847

Annotations 12

Features 57

PDB binders 4

Druggability 0.967

Overview

Basic information about this protein and its source genome.

Accession: KP13_00712
Assembly: Klebsiella pneumoniae subsp. pneumoniae Kp13, complete sequence
Gene: AHE42330.1 nirB
Status: annotated
Amino acids: 847
Structure source: AlphaFold + ColabFold

GO:0050660 Binding to FAD, flavin-adenine dinucleotide, the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes, in either the oxidized form, FAD, or the reduced form, FADH2. GO:0042128 The nitrogen metabolic process that encompasses the uptake of nitrate from the environment and reduction to ammonia, and results in the incorporation of nitrogen derived from nitrate into cellular substances. GO:0008942 Catalysis of the reaction: NH4+ + 3 NAD(P)+ + 2 H2O = nitrite + 3 NAD(P)H + 5 H+. GO:0016491 Catalysis of an oxidation-reduction (redox) reaction, a reversible chemical reaction in which the oxidation state of an atom or atoms within a molecule is altered. One substrate acts as a hydrogen or electron donor and becomes oxidized, while the other acts as hydrogen or electron acceptor and becomes reduced. GO:0051536 Binding to an iron-sulfur cluster, a combination of iron and sulfur atoms. GO:0050661 Binding to nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions; binding may be to either the oxidized form, NADP+, or the reduced form, NADPH.

Target profile

Computed evidence for target prioritization.

Human off-target: hit
Human identity (%): 28.615
Human E-value: 3.68e-23
Gut microbiome off-target: hit
Essential (DEG): N
DEG identity (%): 0.0
Localization: Cytoplasmic
ColabFold pLDDT: 90.64

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 0.967

Structure A0A0H3GYE4

Pocket Pocket 20

P2Rank 0.819

Structure A0A0H3GYE4

Pocket Pocket 1

ColabFold model

FPocket 1 · Pocket 2

P2Rank 0.802 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 129 / 4744 genomes with a hit

Normalized 0.027

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

12 GO

Gene Ontology (GO)

GO:0050660 Binding to FAD, flavin-adenine dinucleotide, the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes, in either the oxidized form, FAD, or the reduced form, FADH2.
GO:0042128 The nitrogen metabolic process that encompasses the uptake of nitrate from the environment and reduction to ammonia, and results in the incorporation of nitrogen derived from nitrate into cellular substances.
GO:0008942 Catalysis of the reaction: NH4+ + 3 NAD(P)+ + 2 H2O = nitrite + 3 NAD(P)H + 5 H+.
GO:0016491 Catalysis of an oxidation-reduction (redox) reaction, a reversible chemical reaction in which the oxidation state of an atom or atoms within a molecule is altered. One substrate acts as a hydrogen or electron donor and becomes oxidized, while the other acts as hydrogen or electron acceptor and becomes reduced.
GO:0051536 Binding to an iron-sulfur cluster, a combination of iron and sulfur atoms.
GO:0050661 Binding to nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions; binding may be to either the oxidized form, NADP+, or the reduced form, NADPH.
GO:0020037 Binding to a heme, a compound composed of iron complexed in a porphyrin (tetrapyrrole) ring.
GO:0051537 Binding to a 2 iron, 2 sulfur (2Fe-2S) cluster; this cluster consists of two iron atoms, with two inorganic sulfur atoms found between the irons and acting as bridging ligands.
GO:0051539 Binding to a 4 iron, 4 sulfur (4Fe-4S) cluster; this cluster consists of four iron atoms, with the inorganic sulfur atoms found between the irons and acting as bridging ligands.
GO:0046872 Binding to a metal ion.
GO:0098809 Catalysis of the reaction: nitrite + acceptor = product(s) of nitrate reduction + reduced acceptor.
GO:0015980 The chemical reactions and pathways by which a cell derives energy from organic compounds; results in the oxidation of the compounds from which energy is released.

Sequence Features

Domain/signature hits from InterPro and related databases.

57 records

Show feature table

Start	End	DB	Term	Name
423	475	FunFam	G3DSA:1.10.10.1100:FF:000002	Nitrite reductase large subunit
638	761	FunFam	G3DSA:3.30.413.10:FF:000007	Nitrite reductase [NAD(P)H] large subunit
769	789	Coils	Coil	Coil
423	476	Gene3D	G3DSA:1.10.10.1100	-
423	476	InterPro	IPR041854	BFD-like [2Fe-2S]-binding domain superfamily
8	283	Gene3D	G3DSA:3.50.50.60	-
8	283	InterPro	IPR036188	FAD/NAD(P)-binding domain superfamily
144	310	SUPERFAMILY	SSF51905	FAD/NAD(P)-binding domain
144	310	InterPro	IPR036188	FAD/NAD(P)-binding domain superfamily
320	401	Gene3D	G3DSA:3.30.390.30	-
320	401	InterPro	IPR016156	FAD/NAD-linked reductase, dimerisation domain superfamily
110	246	Gene3D	G3DSA:3.50.50.60	-
110	246	InterPro	IPR036188	FAD/NAD(P)-binding domain superfamily
633	767	Pfam	PF01077	Nitrite and sulphite reductase 4Fe-4S domain
633	767	InterPro	IPR006067	Nitrite/sulphite reductase 4Fe-4S domain
261	283	PRINTS	PR00368	FAD-dependent pyridine nucleotide reductase signature
102	120	PRINTS	PR00368	FAD-dependent pyridine nucleotide reductase signature
6	25	PRINTS	PR00368	FAD-dependent pyridine nucleotide reductase signature
147	165	PRINTS	PR00368	FAD-dependent pyridine nucleotide reductase signature
234	250	PRINTS	PR00368	FAD-dependent pyridine nucleotide reductase signature
110	246	FunFam	G3DSA:3.50.50.60:FF:000033	Nitrite reductase [NAD(P)H], large subunit
639	761	Gene3D	G3DSA:3.30.413.10	Sulfite Reductase Hemoprotein, domain 1
639	761	InterPro	IPR045854	Nitrite and sulphite reductase 4Fe-4S domain-like superfamily
5	292	Pfam	PF07992	Pyridine nucleotide-disulphide oxidoreductase
5	292	InterPro	IPR023753	FAD/NAD(P)-binding domain
2	833	PANTHER	PTHR43809	NITRITE REDUCTASE (NADH) LARGE SUBUNIT
424	471	Pfam	PF04324	BFD-like [2Fe-2S] binding domain
424	471	InterPro	IPR007419	BFD-like [2Fe-2S]-binding domain
545	638	FunFam	G3DSA:3.90.480.20:FF:000001	Nitrite reductase [NAD(P)H] large subunit
320	401	FunFam	G3DSA:3.30.390.30:FF:000006	Nitrite reductase large subunit
321	387	Pfam	PF18267	Rubredoxin NAD+ reductase C-terminal domain
321	387	InterPro	IPR041575	NADH-rubredoxin oxidoreductase, C-terminal
542	638	Gene3D	G3DSA:3.90.480.20	-
633	808	SUPERFAMILY	SSF56014	Nitrite and sulphite reductase 4Fe-4S domain-like
633	808	InterPro	IPR045854	Nitrite and sulphite reductase 4Fe-4S domain-like superfamily
679	695	ProSitePatterns	PS00365	Nitrite and sulfite reductases iron-sulfur/siroheme-binding site.
679	695	InterPro	IPR006066	Nitrite/sulphite reductase iron-sulphur/sirohaem-binding site
560	622	Pfam	PF03460	Nitrite/Sulfite reductase ferredoxin-like half domain
560	622	InterPro	IPR005117	Nitrite/Sulfite reductase ferredoxin-like domain
679	697	PRINTS	PR00397	Sirohaem Fe-binding site signature
679	697	InterPro	IPR006066	Nitrite/sulphite reductase iron-sulphur/sirohaem-binding site
636	654	PRINTS	PR00397	Sirohaem Fe-binding site signature
636	654	InterPro	IPR006066	Nitrite/sulphite reductase iron-sulphur/sirohaem-binding site
6	801	NCBIfam	TIGR02374	nitrite reductase large subunit NirB
6	801	InterPro	IPR012744	Nitrite reductase [NAD(P)H] large subunit, NirB
2	189	SUPERFAMILY	SSF51905	FAD/NAD(P)-binding domain
2	189	InterPro	IPR036188	FAD/NAD(P)-binding domain superfamily
483	532	CDD	cd19944	NirB_Fer2_BFD-like_2
419	470	CDD	cd19943	NirB_Fer2_BFD-like_1
1	835	PIRSF	PIRSF037149	NirB
1	835	InterPro	IPR017121	Nitrite reductase [NAD(P)H], large subunit
502	627	SUPERFAMILY	SSF55124	Nitrite/Sulfite reductase N-terminal domain-like
502	627	InterPro	IPR036136	Nitrite/Sulfite reductase ferredoxin-like domain superfamily
276	283	PRINTS	PR00411	Pyridine nucleotide disulphide reductase class-I signature
235	249	PRINTS	PR00411	Pyridine nucleotide disulphide reductase class-I signature
147	172	PRINTS	PR00411	Pyridine nucleotide disulphide reductase class-I signature
105	114	PRINTS	PR00411	Pyridine nucleotide disulphide reductase class-I signature

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_A0A0H3GYE4	AlphaFold	—	—	full sequence	—	Viewing
ColabFold KP13_00712	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
20				0.967
23				0.373

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	13.88	0.702
2	11.27	0.603
3	6.01	0.296
4	3.0	0.098
5	1.94	0.04

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
2				1.0
58				0.519

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	11.61	0.618
2	10.83	0.581
3	4.85	0.216
4	3.94	0.156
5	2.38	0.063

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.

72 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
APR	2GR2	Q52437	559.3 Da LogP -3.28 TPSA 291.5	3 viol.	✓ Clean	`c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)…`
AZI	2BCP	Q5XC60	42.0 Da LogP 0.87 TPSA 58.7	✓ Ro5	Alert	`[N-]=[N+]=[N-]`
BU3	6TUK	Q47QF8	90.1 Da LogP -0.25 TPSA 40.5	✓ Ro5	✓ Clean	`C[C@H]([C@@H](C)O)O`
OXY	5ER0	Q03Q85	32.0 Da LogP 0.07 TPSA 34.1	✓ Ro5	✓ Clean	`O=O`

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
CHEMBL1836603	P39051	6.72	355.9 Da LogP 5.06 TPSA 18.8	1 viol.	✓ Clean	`CC1=Nc2ccc(Cl)cc2C(c2ccc(C)cc2)N1CCCN(C)C`
CHEMBL1836570	P39051	6.57	454.0 Da LogP 3.50 TPSA 42.4	✓ Ro5	✓ Clean	`CC1=Nc2ccc(Cl)cc2C(c2ccccc2)N1CCN1CCN(C(=O)CN(C…`
CHEMBL1836378	P39051	6.50	382.9 Da LogP 4.04 TPSA 22.1	✓ Ro5	✓ Clean	`CC1=Nc2ccc(Cl)cc2C(c2ccccc2)N1CCN1CCN(C)CC1`
CHEMBL1836574	P39051	6.46	459.4 Da LogP 5.23 TPSA 18.8	1 viol.	✓ Clean	`CC1=Nc2ccc(I)cc2C(c2ccccc2)N1CCN1CCCCC1`
CHEMBL1836567	P39051	6.38	463.0 Da LogP 4.85 TPSA 52.3	✓ Ro5	✓ Clean	`CC1=Nc2ccc(Cl)cc2C(c2ccccc2)N1CCN1CCN(C(=O)c2cc…`
CHEMBL1836559	P39051	6.36	393.9 Da LogP 4.82 TPSA 57.8	✓ Ro5	✓ Clean	`CC1=Nc2ccc(Cl)cc2C(c2ccccc2)N1CCNC(=O)c1ccco1`
CHEMBL1836615	P39051	6.23	382.0 Da LogP 5.59 TPSA 18.8	1 viol.	✓ Clean	`CC1=Nc2ccc(Cl)cc2C(c2ccc(C)cc2)N1CCN1CCCCC1`
CHEMBL1836612	P39051	6.14	402.4 Da LogP 5.93 TPSA 18.8	1 viol.	✓ Clean	`CC1=Nc2ccc(Cl)cc2C(c2ccc(Cl)cc2)N1CCN1CCCCC1`
CHEMBL1836571	P39051	6.11	333.5 Da LogP 4.63 TPSA 18.8	✓ Ro5	✓ Clean	`CC1=Nc2ccccc2C(c2ccccc2)N1CCN1CCCCC1`
CHEMBL1836572	P39051	6.10	412.4 Da LogP 5.39 TPSA 18.8	1 viol.	✓ Clean	`CC1=Nc2ccc(Br)cc2C(c2ccccc2)N1CCN1CCCCC1`
CHEMBL1836577	P39051	6.10	415.6 Da LogP 6.36 TPSA 18.8	1 viol.	✓ Clean	`CC1=Nc2ccc(-c3ccsc3)cc2C(c2ccccc2)N1CCN1CCCCC1`
CHEMBL1836371	P39051	6.09	389.9 Da LogP 6.06 TPSA 18.8	1 viol.	✓ Clean	`CC1=Nc2ccc(Cl)cc2C(c2ccccc2)N1Cc1cccc(N(C)C)c1`
CHEMBL1836562	P39051	6.09	384.9 Da LogP 3.47 TPSA 47.9	✓ Ro5	✓ Clean	`CC1=Nc2ccc(Cl)cc2C(c2ccccc2)N1CCNC(=O)CN(C)C`
CHEMBL1836606	P39051	6.05	385.9 Da LogP 5.42 TPSA 18.8	1 viol.	✓ Clean	`CC1=Nc2ccc(Cl)cc2C(c2cccc(F)c2)N1CCN1CCCCC1`
CHEMBL1836365	P39051	6.03	346.9 Da LogP 6.00 TPSA 15.6	1 viol.	✓ Clean	`CC1=Nc2ccc(Cl)cc2C(c2ccccc2)N1Cc1ccccc1`
CHEMBL1836368	P39051	6.03	364.9 Da LogP 6.13 TPSA 15.6	1 viol.	✓ Clean	`CC1=Nc2ccc(Cl)cc2C(c2ccccc2)N1Cc1ccccc1F`
CHEMBL1836380	P39051	6.00	341.9 Da LogP 4.75 TPSA 18.8	✓ Ro5	✓ Clean	`CC1=Nc2ccc(Cl)cc2C(c2ccccc2)N1CCCN(C)C`
CHEMBL4859269	P39051	6.00	1157.2 Da LogP 7.07 TPSA 297.0	4 viol.	✓ Clean	`NCCCCc1cn(-c2ccc(-c3nc(-c4cccc(-c5csc(-c6ccc(-n…`

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
ZINC12360002	0.855	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)OP(=O…`
ZINC12360703	0.855	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)OP(=O…`
ZINC12503599	0.855	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)OP(=O…`
ZINC16546165	0.855	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@H](CO[P@](=O)(O)OP(=O)(…`
ZINC31977053	0.855	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO[P@](=O)(O)OP(=O)…`
ZINC4806433	0.855	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)OP(=O…`
ZINC53683898	0.855	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@@](=O)(O)OP(=…`
ZINC8586019	0.855	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO[P@](=O)(O)OP(=O)…`
ZINC8586020	0.855	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@@](=O)(O)OP(=…`
ZINC8586021	0.855	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO[P@@](=O)(O)OP(=O…`
ZINC8586022	0.855	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@@](=O)(O)OP(=…`
ZINC13518964	0.782	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C@H](…`
ZINC1532515	0.782	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](COP(=O)(O)O)[C@H](O…`
ZINC1571045	0.782	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C@@H]…`
ZINC1842158	0.782	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](COP(=O)(O)O)[C@H](O…`
ZINC2046931	0.782	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C@H](…`
ZINC2126310	0.782	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@@H](…`
ZINC3201891	0.782	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C@@H]…`
ZINC3201893	0.782	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](COP(=O)(O)O)[C@@H](…`
ZINC3830180	0.782	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](COP(=O)(O)O)[C@@H](…`
ZINC3860156	0.782	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@@H](…`
ZINC3977897	0.782	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@H](COP(=O)(O)O)[C@@H](O…`
ZINC4806442	0.782	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@H](O…`
ZINC8613167	0.782	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@H](O…`
ZINC4096224	0.768	346.2 Da LogP -1.90 TPSA 191.9	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@](N)(=O)O)[C@@…`
ZINC12503850	0.763	427.3 Da LogP -2.04 TPSA 229.4	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@](=O)(O)OS(=O)…`
ZINC141161066	0.763	427.3 Da LogP -2.04 TPSA 229.4	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@](=O)(O)OS(=O)…`
ZINC141163786	0.763	427.3 Da LogP -2.04 TPSA 229.4	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@](=O)(O)OS(=O)…`
ZINC4228246	0.763	427.3 Da LogP -2.04 TPSA 229.4	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)OS(=O…`
ZINC105372833	0.750	345.3 Da LogP -1.93 TPSA 197.6	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(N)(N)=O)[C@H](O…`
ZINC105372837	0.750	345.3 Da LogP -1.93 TPSA 197.6	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(N)(N)=O)[C@H](O…`
ZINC17107643	0.750	345.3 Da LogP -1.93 TPSA 197.6	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(N)(N)=O)[C@@H](…`
ZINC204538551	0.750	345.3 Da LogP -1.93 TPSA 197.6	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(N)(N)=O)[C@@H](…`
ZINC31475423	0.738	434.3 Da LogP -2.99 TPSA 238.4	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@H](CO[P@@](=O)(O)OC(=O)…`
ZINC105469665	0.729	425.2 Da LogP -1.64 TPSA 223.4	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)CP(=O…`
ZINC13527614	0.729	425.2 Da LogP -1.64 TPSA 223.4	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@](=O)(O)CP(=O)…`
ZINC219330894	0.729	425.2 Da LogP -1.64 TPSA 223.4	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@](=O)(O)CP(=O)…`
ZINC3873852	0.729	425.2 Da LogP -1.64 TPSA 223.4	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO[P@](=O)(O)CP(=O)…`
ZINC3873853	0.729	425.2 Da LogP -1.64 TPSA 223.4	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@](=O)(O)CP(=O…`
ZINC3873854	0.729	425.2 Da LogP -1.64 TPSA 223.4	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO[P@](=O)(O)CP(=O)…`
ZINC3873855	0.729	425.2 Da LogP -1.64 TPSA 223.4	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@](=O)(O)CP(=O…`
ZINC5615251	0.712	375.3 Da LogP -0.55 TPSA 164.1	1 viol.	✓ Clean	`COP(=O)(OC)OC[C@H]1O[C@@H](n2cnc3c(N)ncnc32)[C@…`
ZINC5615253	0.712	375.3 Da LogP -0.55 TPSA 164.1	1 viol.	✓ Clean	`COP(=O)(OC)OC[C@@H]1O[C@@H](n2cnc3c(N)ncnc32)[C…`
ZINC5615258	0.712	375.3 Da LogP -0.55 TPSA 164.1	1 viol.	✓ Clean	`COP(=O)(OC)OC[C@H]1O[C@@H](n2cnc3c(N)ncnc32)[C@…`
ZINC5615263	0.712	375.3 Da LogP -0.55 TPSA 164.1	1 viol.	✓ Clean	`COP(=O)(OC)OC[C@@H]1O[C@@H](n2cnc3c(N)ncnc32)[C…`
ZINC31516918	0.703	446.4 Da LogP -1.33 TPSA 218.2	1 viol.	✓ Clean	`CC(C)[C@H](N)C(=O)O[P@](=O)(O)OC[C@H]1O[C@@H](n…`
ZINC1582675	0.700	403.3 Da LogP 0.23 TPSA 164.1	1 viol.	✓ Clean	`CCOP(=O)(OCC)OC[C@H]1O[C@@H](n2cnc3c(N)ncnc32)[…`
ZINC5486730	0.700	403.3 Da LogP 0.23 TPSA 164.1	1 viol.	✓ Clean	`CCOP(=O)(OCC)OC[C@H]1O[C@@H](n2cnc3c(N)ncnc32)[…`
ZINC5486734	0.700	403.3 Da LogP 0.23 TPSA 164.1	1 viol.	✓ Clean	`CCOP(=O)(OCC)OC[C@@H]1O[C@@H](n2cnc3c(N)ncnc32)…`
ZINC5486740	0.700	403.3 Da LogP 0.23 TPSA 164.1	1 viol.	✓ Clean	`CCOP(=O)(OCC)OC[C@@H]1O[C@@H](n2cnc3c(N)ncnc32)…`

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.