KpKP13 Protein target profile

Nitrite reductase [NAD(P)H] large subunit

Accession: KP13_04718

Gene: AHE44017.1 3D evidence: ColabFold model UniProt A0A2V3K3L0

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Length 1355

Pocket druggability (P2Rank · ColabFold model) 0.884

Direct ligand evidence 0 54 total records

Functional annotation 1 EC 12 GO

Target summary

Promising target candidate with multiple supporting evidence streams.

Automated synthesis of the evidence currently loaded. Review the underlying records before prioritizing this protein.

Main supporting evidence

Independent pocket support: P2Rank + FPocket Both predictors report a high-scoring binding site (P2Rank 0.88, FPocket 0.95). Use the 3D pocket comparison to verify whether they identify the same site. Strong predicted binding pocket FPocket selected-pocket score 0.95. This is a computational pocket signal, not binding validation. Second pocket predictor agrees P2Rank predicted binding-site probability 0.88. Structure available ColabFold model Review the complete evidence below

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 (%): 26.689 Lower values reduce human off-target concern.
Human E-value: 1.41e-16
Gut microbiome similarity: 1.1% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): N
DEG identity (%): 0.0 Higher values support similarity to known essential genes.

Structure confidence

ColabFold pLDDT: 89.5 0-100 confidence; >70 supports local structural interpretation.

Binding-site evidence

ColabFold / curated 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) 0.884

Structure CB_KP13_04718

Pocket Pocket 1

Druggability (FPocket) 0.948

Structure CB_KP13_04718

Pocket Pocket 90

ColabFold model

P2Rank 0.884 · Pocket 1

FPocket 0.948 · Pocket 90

Core conservation Accessory gene

Roary core

CoreCruncher accessory

Gut microbiome 50 / 4744 genomes with a hit

Prevalence 1.1%

Sequence

Primary amino-acid sequence viewer.

MTRRLVVIGNGMAATRLVQRLVERDPARFAITVVGDEPHPAYNRIQLSPLLAGEKTAAQIPLLPAEWYTRHGVCLRSGEAVDEVDIQQRRLRIAETWLPWDELVFATGSRPFIPPLPGIDRPQVMPFRTLADVERILAIPGPAVVIGGGVLGVEAAAALRRHGGEVTLLHRGSGLMAPLTDAFAADELRQQLEARGIRCVLECRIAAIDADGVRLADGRVFRAARVVLATGVQPDSRLAAQSGVLCQRGIVVDRQMASSLPGISAIGECCEIDGQTWGLVAPCLRQAEVLADRLCGAPGEGFVWQDAGTRLKVTGIELFSAGEQQAGEQDDIYTSWDPIDRHYRRLLLRDGRLRGVLLMGDCTAAAALTARLESDEPATVDWLFDPSSTQPQAAGIMTMTKPVLVLVGHGMVGHHFLEQCVSRNLHQQYRIVVFGEERYPAYDRVHLSEYFAGRSAESLSLAAGDFFIEHGIELRLGEAVATIDRDARLVRDAEGHEIHWDKLVLATGSYPFVPPIPGNDLAGCFVYRTLDDLDRIAAHAAAAKSGVVIGGGLLGLEAANALKQLGLETQVVEFAPNLMAVQLDNGGAAMLREKIVALGVGVHTSKATTAIVREADGLRLNFADGGALRTDMVVFSAGIRPQDALARGCALQVGERGGIHIDGQCRTSDPDVLAIGECALWDNKIYGLVAPGYQMARIAAATLAGEDACFSGADMSTKLKLLGVDVASFGDAQGRTPGCQSYQWTDGPQQIYKKIVVSQDGKALLGGVLVGDASDYATLLQMMLNRMALPPRPESLILPALEGAAPKALGVAALPDSAPICSCHNVSKGDICQAVNNGAGDMSAIKSCTRAATGCGGCSALVKQVMEYQLAEQGVEVKKDVCEHFPWSRQEIYHLVRVNHIHTFEQLISRYGQGHGCDVCKPLVASVLASCWNEYLLKPAHLPLQDTNDRYFANIQKDGSYSVVPRMAAGEVTPDGLIAIGQIAKRYQLYSKVTGGQRIDLFGARLEQLPAIWRELADAGFETGHAYGKSLRTVKSCVGSTWCRYGVQDSTGLAVRLEHRYKGLRAPHKIKMAVSGCTRECAEAQGKDIGVIATDKGWNLYVCGNGGMKPRHADLFASDLDEATLIRSIDRLLMFYIRTADRLQRTSTWMDNLEGGVAYLRQVVLEDSLGIGEELEQEMARIVDSYQCEWQTTLNDPQRLALFRSFVNSDQPDEAVQRRDLRGQPQPLLTETLPEGELPSRPWQAVCDLDAIPAQAGIGARLGERQIALFRFGERVYALDNREPGSTANVLSRGLLGDVGGEPVVISPLYKQRIRLRDGWPCDGSEQAVRAWPVKVENGKVWVGNQQLLARAEAS

MTRRLVVIGNGMAATRLVQRLVERDPARFAITVVGDEPHPAYNRIQLSPLLAGEKTAAQIPLLPAEWYTRHGVCLRSGEAVDEVDIQQRRLRIAETWLPWDELVFATGSRPFIPPLPGIDRPQVMPFRTLADVERILAIPGPAVVIGGGVLGVEAAAALRRHGGEVTLLHRGSGLMAPLTDAFAADELRQQLEARGIRCVLECRIAAIDADGVRLADGRVFRAARVVLATGVQPDSRLAAQSGVLCQRGIVVDRQMASSLPGISAIGECCEIDGQTWGLVAPCLRQAEVLADRLCGAPGEGFVWQDAGTRLKVTGIELFSAGEQQAGEQDDIYTSWDPIDRHYRRLLLRDGRLRGVLLMGDCTAAAALTARLESDEPATVDWLFDPSSTQPQAAGIMTMTKPVLVLVGHGMVGHHFLEQCVSRNLHQQYRIVVFGEERYPAYDRVHLSEYFAGRSAESLSLAAGDFFIEHGIELRLGEAVATIDRDARLVRDAEGHEIHWDKLVLATGSYPFVPPIPGNDLAGCFVYRTLDDLDRIAAHAAAAKSGVVIGGGLLGLEAANALKQLGLETQVVEFAPNLMAVQLDNGGAAMLREKIVALGVGVHTSKATTAIVREADGLRLNFADGGALRTDMVVFSAGIRPQDALARGCALQVGERGGIHIDGQCRTSDPDVLAIGECALWDNKIYGLVAPGYQMARIAAATLAGEDACFSGADMSTKLKLLGVDVASFGDAQGRTPGCQSYQWTDGPQQIYKKIVVSQDGKALLGGVLVGDASDYATLLQMMLNRMALPPRPESLILPALEGAAPKALGVAALPDSAPICSCHNVSKGDICQAVNNGAGDMSAIKSCTRAATGCGGCSALVKQVMEYQLAEQGVEVKKDVCEHFPWSRQEIYHLVRVNHIHTFEQLISRYGQGHGCDVCKPLVASVLASCWNEYLLKPAHLPLQDTNDRYFANIQKDGSYSVVPRMAAGEVTPDGLIAIGQIAKRYQLYSKVTGGQRIDLFGARLEQLPAIWRELADAGFETGHAYGKSLRTVKSCVGSTWCRYGVQDSTGLAVRLEHRYKGLRAPHKIKMAVSGCTRECAEAQGKDIGVIATDKGWNLYVCGNGGMKPRHADLFASDLDEATLIRSIDRLLMFYIRTADRLQRTSTWMDNLEGGVAYLRQVVLEDSLGIGEELEQEMARIVDSYQCEWQTTLNDPQRLALFRSFVNSDQPDEAVQRRDLRGQPQPLLTETLPEGELPSRPWQAVCDLDAIPAQAGIGARLGERQIALFRFGERVYALDNREPGSTANVLSRGLLGDVGGEPVVISPLYKQRIRLRDGWPCDGSEQAVRAWPVKVENGKVWVGNQQLLARAEAS

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 12 GO

Subcellular localization

Localization: CytoplasmicMembrane

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 domains and features

Domain and signature matches imported 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; 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

0.884

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Surrounding area

Pocket 2 P2Rank #2

0.845

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Surrounding area

Pocket 3 P2Rank #3

0.715

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Surrounding area

Pocket 4 P2Rank #4

0.65

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Surrounding area

Pocket 5 P2Rank #5

0.563

Likely same site as FPocket 90 5.1 Å 22 shared residues 92% of smaller site

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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 #90

0.948 Unusual size

Likely same site as P2Rank 5 5.1 Å 22 shared residues 92% of smaller site

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Surrounding area

Pocket 2 FPocket #1

0.297 Unusual size

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Surrounding area

Pocket 3 FPocket #75

0.205

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Surrounding area

All structural evidence 0 experimental · 1 predicted

Structural evidence

0 + 1

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
ColabFold KP13_04718	ColabFold	—	—	full sequence	—	Viewing

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

Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 same-protein records

Transferred evidence 4 records from similar proteins

Structural ligands 4 0 loaded crystals

Measured bioactivity 0 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

APR PDB via homolog 559.3 Da · LogP -3.28 · TPSA 291.5 Open detail RCSB PDB

AZI PDB via homolog Detail RCSB PDB

BU3 PDB via homolog Detail RCSB PDB

OXY PDB via homolog Detail RCSB PDB

ZINC12360002 ZINC proposed compound · Tanimoto 0.855 Detail ZINC

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
APR RCSB PDB	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 RCSB PDB	2BCP	Q5XC60	42.0 Da LogP 0.87 TPSA 58.7	✓ Ro5	Alert	`[N-]=[N+]=[N-]`
BU3 RCSB PDB	6TUK	Q47QF8	90.1 Da LogP -0.25 TPSA 40.5	✓ Ro5	✓ Clean	`C[C@H]([C@@H](C)O)O`
OXY RCSB PDB	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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 ZINC	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.

Cross-references

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

Sequence

UniProt A0A2V3K3L0