Protein profile

KP13_04718

Nitrite reductase [NAD(P)H] large subunit

Genome: KpKP13

Gene: AHE44017.1 Structure source: ColabFold UniProt A0A2V3K3L0

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Amino acids 1355

Annotations 13

Features 73

PDB binders 4

Druggability 0.948

Overview

Basic information about this protein and its source genome.

Accession: KP13_04718
Assembly: Klebsiella pneumoniae subsp. pneumoniae Kp13, complete sequence
Gene: AHE44017.1
Status: annotated
Amino acids: 1355
Structure source: ColabFold

1.18.1.3

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 (%): 26.689
Human E-value: 1.41e-16
Gut microbiome off-target: hit
Essential (DEG): N
DEG identity (%): 0.0
Localization: CytoplasmicMembrane
ColabFold pLDDT: 89.5

Selected Druggability evidence

ColabFold / curated 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 0.948

Structure CB_KP13_04718

Pocket Pocket 90

P2Rank 0.884

Structure CB_KP13_04718

Pocket Pocket 1

ColabFold model

FPocket 0.948 · Pocket 90

P2Rank 0.884 · Pocket 1

Core conservation Accessory gene

Roary core

CoreCruncher accessory

Gut microbiome 50 / 4744 genomes with a hit

Normalized 0.011

Sequence

Primary amino-acid sequence viewer.

MTRRLVVIGNGMAATRLVQRLVERDPARFAITVVGDEPHPAYNRIQLSPLLAGEKTAAQIPLLPAEWYTRHGVCLRSGEAVDEVDIQQRRLRIAETWLPWDELVFATGSRPFIPPLPGIDRPQVMPFRTLADVERILAIPGPAVVIGGGVLGVEAAAALRRHGGEVTLLHRGSGLMAPLTDAFAADELRQQLEARGIRCVLECRIAAIDADGVRLADGRVFRAARVVLATGVQPDSRLAAQSGVLCQRGIVVDRQMASSLPGISAIGECCEIDGQTWGLVAPCLRQAEVLADRLCGAPGEGFVWQDAGTRLKVTGIELFSAGEQQAGEQDDIYTSWDPIDRHYRRLLLRDGRLRGVLLMGDCTAAAALTARLESDEPATVDWLFDPSSTQPQAAGIMTMTKPVLVLVGHGMVGHHFLEQCVSRNLHQQYRIVVFGEERYPAYDRVHLSEYFAGRSAESLSLAAGDFFIEHGIELRLGEAVATIDRDARLVRDAEGHEIHWDKLVLATGSYPFVPPIPGNDLAGCFVYRTLDDLDRIAAHAAAAKSGVVIGGGLLGLEAANALKQLGLETQVVEFAPNLMAVQLDNGGAAMLREKIVALGVGVHTSKATTAIVREADGLRLNFADGGALRTDMVVFSAGIRPQDALARGCALQVGERGGIHIDGQCRTSDPDVLAIGECALWDNKIYGLVAPGYQMARIAAATLAGEDACFSGADMSTKLKLLGVDVASFGDAQGRTPGCQSYQWTDGPQQIYKKIVVSQDGKALLGGVLVGDASDYATLLQMMLNRMALPPRPESLILPALEGAAPKALGVAALPDSAPICSCHNVSKGDICQAVNNGAGDMSAIKSCTRAATGCGGCSALVKQVMEYQLAEQGVEVKKDVCEHFPWSRQEIYHLVRVNHIHTFEQLISRYGQGHGCDVCKPLVASVLASCWNEYLLKPAHLPLQDTNDRYFANIQKDGSYSVVPRMAAGEVTPDGLIAIGQIAKRYQLYSKVTGGQRIDLFGARLEQLPAIWRELADAGFETGHAYGKSLRTVKSCVGSTWCRYGVQDSTGLAVRLEHRYKGLRAPHKIKMAVSGCTRECAEAQGKDIGVIATDKGWNLYVCGNGGMKPRHADLFASDLDEATLIRSIDRLLMFYIRTADRLQRTSTWMDNLEGGVAYLRQVVLEDSLGIGEELEQEMARIVDSYQCEWQTTLNDPQRLALFRSFVNSDQPDEAVQRRDLRGQPQPLLTETLPEGELPSRPWQAVCDLDAIPAQAGIGARLGERQIALFRFGERVYALDNREPGSTANVLSRGLLGDVGGEPVVISPLYKQRIRLRDGWPCDGSEQAVRAWPVKVENGKVWVGNQQLLARAEAS

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 12 GO

Enzyme Commission (EC)

1.18.1.3

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:0008860 Catalysis of the reaction: 2 reduced [2Fe-2S]-[ferredoxin] + NAD+ + H+ = 2 oxidized [2Fe-2S]-[ferredoxin] + NADH.
GO:0046872 Binding to a metal ion.
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.

73 records

Show feature table

Start	End	DB	Term	Name
2	183	SUPERFAMILY	SSF51905	FAD/NAD(P)-binding domain
2	183	InterPro	IPR036188	FAD/NAD(P)-binding domain superfamily
1027	1191	Gene3D	G3DSA:3.30.413.10	Sulfite Reductase Hemoprotein, domain 1
1027	1191	InterPro	IPR045854	Nitrite and sulphite reductase 4Fe-4S domain-like superfamily
6	296	Gene3D	G3DSA:3.50.50.60	-
6	296	InterPro	IPR036188	FAD/NAD(P)-binding domain superfamily
820	867	Pfam	PF04324	BFD-like [2Fe-2S] binding domain
820	867	InterPro	IPR007419	BFD-like [2Fe-2S]-binding domain
508	642	Gene3D	G3DSA:3.50.50.60	-
508	642	InterPro	IPR036188	FAD/NAD(P)-binding domain superfamily
1243	1343	ProSiteProfiles	PS51296	Rieske [2Fe-2S] iron-sulfur domain profile.
1243	1343	InterPro	IPR017941	Rieske [2Fe-2S] iron-sulphur domain
1239	1347	Gene3D	G3DSA:2.102.10.10	-
1239	1347	InterPro	IPR036922	Rieske [2Fe-2S] iron-sulphur domain superfamily
1075	1093	PRINTS	PR00397	Sirohaem Fe-binding site signature
1075	1093	InterPro	IPR006066	Nitrite/sulphite reductase iron-sulphur/sirohaem-binding site
1032	1050	PRINTS	PR00397	Sirohaem Fe-binding site signature
1032	1050	InterPro	IPR006066	Nitrite/sulphite reductase iron-sulphur/sirohaem-binding site
956	1018	Pfam	PF03460	Nitrite/Sulfite reductase ferredoxin-like half domain
956	1018	InterPro	IPR005117	Nitrite/Sulfite reductase ferredoxin-like domain
308	382	Gene3D	G3DSA:3.30.390.30	-
308	382	InterPro	IPR016156	FAD/NAD-linked reductase, dimerisation domain superfamily
716	794	Gene3D	G3DSA:3.30.390.30	-
716	794	InterPro	IPR016156	FAD/NAD-linked reductase, dimerisation domain superfamily
113	230	Gene3D	G3DSA:3.50.50.60	-
113	230	InterPro	IPR036188	FAD/NAD(P)-binding domain superfamily
1240	1345	ProSiteProfiles	PS51300	NADH-nitrite reductase subunit D family profile.
3	372	PANTHER	PTHR43809	NITRITE REDUCTASE (NADH) LARGE SUBUNIT
547	706	SUPERFAMILY	SSF51905	FAD/NAD(P)-binding domain
547	706	InterPro	IPR036188	FAD/NAD(P)-binding domain superfamily
1075	1091	ProSitePatterns	PS00365	Nitrite and sulfite reductases iron-sulfur/siroheme-binding site.
1075	1091	InterPro	IPR006066	Nitrite/sulphite reductase iron-sulphur/sirohaem-binding site
4	273	Pfam	PF07992	Pyridine nucleotide-disulphide oxidoreductase
4	273	InterPro	IPR023753	FAD/NAD(P)-binding domain
716	797	FunFam	G3DSA:3.30.390.30:FF:000006	Nitrite reductase large subunit
404	685	Pfam	PF07992	Pyridine nucleotide-disulphide oxidoreductase
404	685	InterPro	IPR023753	FAD/NAD(P)-binding domain
404	1197	NCBIfam	TIGR02374	nitrite reductase large subunit NirB
404	1197	InterPro	IPR012744	Nitrite reductase [NAD(P)H] large subunit, NirB
405	679	Gene3D	G3DSA:3.50.50.60	-
405	679	InterPro	IPR036188	FAD/NAD(P)-binding domain superfamily
879	928	CDD	cd19944	NirB_Fer2_BFD-like_2
309	374	Pfam	PF18267	Rubredoxin NAD+ reductase C-terminal domain
309	374	InterPro	IPR041575	NADH-rubredoxin oxidoreductase, C-terminal
716	785	Pfam	PF18267	Rubredoxin NAD+ reductase C-terminal domain
716	785	InterPro	IPR041575	NADH-rubredoxin oxidoreductase, C-terminal
1029	1201	SUPERFAMILY	SSF56014	Nitrite and sulphite reductase 4Fe-4S domain-like
1029	1201	InterPro	IPR045854	Nitrite and sulphite reductase 4Fe-4S domain-like superfamily
508	642	FunFam	G3DSA:3.50.50.60:FF:000033	Nitrite reductase [NAD(P)H], large subunit
1243	1343	Pfam	PF13806	Rieske-like [2Fe-2S] domain
1243	1343	InterPro	IPR012748	Rieske-like [2Fe-2S] domain, NirD-type
399	588	SUPERFAMILY	SSF51905	FAD/NAD(P)-binding domain
399	588	InterPro	IPR036188	FAD/NAD(P)-binding domain superfamily
898	1037	SUPERFAMILY	SSF55124	Nitrite/Sulfite reductase N-terminal domain-like
898	1037	InterPro	IPR036136	Nitrite/Sulfite reductase ferredoxin-like domain superfamily
1028	1166	Pfam	PF01077	Nitrite and sulphite reductase 4Fe-4S domain
1028	1166	InterPro	IPR006067	Nitrite/sulphite reductase 4Fe-4S domain
1243	1344	NCBIfam	TIGR02378	nitrite reductase small subunit NirD
1243	1344	InterPro	IPR012748	Rieske-like [2Fe-2S] domain, NirD-type
1243	1344	CDD	cd03529	Rieske_NirD
1242	1345	SUPERFAMILY	SSF50022	ISP domain
1242	1345	InterPro	IPR036922	Rieske [2Fe-2S] iron-sulphur domain superfamily
143	297	SUPERFAMILY	SSF51905	FAD/NAD(P)-binding domain
143	297	InterPro	IPR036188	FAD/NAD(P)-binding domain superfamily
819	872	Gene3D	G3DSA:1.10.10.1100	-
819	872	InterPro	IPR041854	BFD-like [2Fe-2S]-binding domain superfamily
819	871	FunFam	G3DSA:1.10.10.1100:FF:000002	Nitrite reductase large subunit
223	239	PRINTS	PR00368	FAD-dependent pyridine nucleotide reductase signature
5	24	PRINTS	PR00368	FAD-dependent pyridine nucleotide reductase signature
142	160	PRINTS	PR00368	FAD-dependent pyridine nucleotide reductase signature
248	270	PRINTS	PR00368	FAD-dependent pyridine nucleotide reductase signature
100	118	PRINTS	PR00368	FAD-dependent pyridine nucleotide reductase signature
1034	1157	FunFam	G3DSA:3.30.413.10:FF:000007	Nitrite reductase [NAD(P)H] large subunit

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 + 1

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

Entry	Method	Resolution	Chain	Coverage	Links	Status
ColabFold KP13_04718	ColabFold	—	—	full sequence	—	Viewing

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
90				0.948
1				0.297

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	11.39	0.609
2	9.61	0.517
3	8.54	0.456
4	8.14	0.433
5	8.14	0.433

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.

54 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).

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
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.