Protein target profile

VK055_0238

nitrate reductase, alpha subunit

Genome: KpATCC43816 Gene: AIK78866.1 3D evidence: AlphaFold DB model + ColabFold model Metabolism 2 reactions UniProt A0A0H3GUA4

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Length 1247

Pocket druggability 0.983

Metabolic reactions 2

Chokepoint No

Direct ligand evidence 0 63 total records

Functional annotation 1 EC 11 GO

Target summary

Strong target candidate with converging metabolic, structural and chemical evidence.

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

Main supporting evidence

Independent pocket support: FPocket + P2Rank Both predictors report a high-scoring binding site (FPocket 0.98, P2Rank 0.92). Use the 3D pocket comparison to verify whether they identify the same site. No similar human protein detected The current BLAST sequence screen did not find a significant human match, lowering apparent off-target risk. Core gene across strains Marked as conserved by both pan-genome tools: Roary and CoreCruncher. Strong predicted binding pocket FPocket selected-pocket score 0.98. This is a computational pocket signal, not binding validation. Review the complete evidence below

Risks to review

Evidence coverage

Core evidence streams are available for this target.

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: No hit
Gut microbiome similarity: 3.9% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 51.569 Higher values support similarity to known essential genes.
DEG E-value: 0.0 Smaller values mean stronger essential-gene similarity.

Localization

Localization: CytoplasmicMembrane

Structure confidence

ColabFold pLDDT: 98.3 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 0.983

Structure A0A0H3GUA4

Pocket Pocket 2

P2Rank 0.916

Structure A0A0H3GUA4

Pocket Pocket 1

ColabFold model

FPocket 0.978 · Pocket 2

P2Rank 0.886 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

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 A0A0H3GUA4

Pathways

KEGG R00794 BioCyc NITRATE-REDUCTASE-NADH-RXN KEGG R00796 BioCyc NITRATE-REDUCTASE-NADPH-RXN

Metabolic context

Reactions catalyzed, pathway membership, and centrality in the genome-scale metabolic network.

Explore metabolic network

Metabolic context: no human homolog detected.

Relative network centrality 0.0% more central than 0.0% of genes in this genome

Chokepoint Not a chokepoint

Imported from KpATCC43816.sbml · 2026-07-09

Sequence

Primary amino-acid sequence viewer.

MSKFLDRFRYFKQKGETFADGHGQLLNTNRDWEDGYRQRWQHDKIVRSTHGVNCTGSCSWKIYVKNGLVTWETQQTDYPRTRPDLPNHEPRGCPRGASYSWYLYSANRLKYPLMRKRLMKMWREAKVQHSDPVEAWASIIEDADKAKSFKQARGRGGFVRSSWQEVNELIAASNVYTVKTYGPDRVAGFSPIPAMSMVSYASGARYLSLIGGTCLSFYDWYCDLPPASPMTWGEQTDVPESADWYNSSYIIAWGSNVPQTRTPDAHFFTEVRYKGTKTVAITPDYAEIAKLCDLWLAPKQGTDAAMALAMGHVMLREFHLDKPSQYFTDYVRRYTDMPMLVMLEERDGYYAAGRTLRASDLVDSLGQENNPEWKTVAFDEKGDMTVPNGSLGFRWGDKGKWNLEQRDGKTGEEIELRLSLLGSHDEVANVGFPYFGGEGSEHFNKVDLENILLHKLPAKRLQLADGSTALVTTVYDLTMANYGLERGLNDDNCAAGYDEVKAYTPAWAEKITGVSRAHIIRTAREFADNADKTHGRSMIIVGAGLNHWFHLDMNYRGLINMLIFCGCVGQSGGGWAHYVGQEKLRPQTGWQPLAFALDWQRPARHMNSTSYFYNHSSQWRYETVTAQELLSPMADKSRYSGHLIDFNVRAERMGWLPSAPQLGVNPLRIADEAKKAGMTPVDYTVKSLKEGSIRFAAEQPENGKNHPRNLFIWRSNLLGSSGKGHEYMLKYLLGTENGIQGKDLGKQGGVKPEEVEWRDNGLDGKLDLVVTLDFRLSSTCLYSDIVLPTATWYEKDDMNTSDMHPFIHPLSAAVDPAWESKSDWEIYKGIAKKFSEVCVGHLGKETDVVTLPIQHDSAAEMAQPLDVKDWKKGECDLIPGKTAPHIIPVERDYPATYERFTSIGPLLETIGNGGKGIAWNTQSEMDLLRKLNYTKAEGPAKGQPKLETAIDAAEMILTLAPETNGQVAVKAWQALSEITGREHTHLALNKEDEKIRFRDIQAQPRKIISSPTWSGLEDEHVSYNAGYTNVHELIPWRTLSGRQSLYQDHQWMRDFGESLLVYRPPIDTRSVKAVMGEKSNGNPEKALNFLTPHQKWGIHSTYSDNLLMLTLSRGGPIVWMSEADAKDLGIEDNDWIEVFNANGALTARAVVSQRVPAGMTMMYHAQERIVNLPGSEITGQRGGIHNSVTRITPKPTHMIGGYGHLAYGFNYYGTVGSNRDEFVVVRKMKNINWLDGEGNDQVQESVK

MSKFLDRFRYFKQKGETFADGHGQLLNTNRDWEDGYRQRWQHDKIVRSTHGVNCTGSCSWKIYVKNGLVTWETQQTDYPRTRPDLPNHEPRGCPRGASYSWYLYSANRLKYPLMRKRLMKMWREAKVQHSDPVEAWASIIEDADKAKSFKQARGRGGFVRSSWQEVNELIAASNVYTVKTYGPDRVAGFSPIPAMSMVSYASGARYLSLIGGTCLSFYDWYCDLPPASPMTWGEQTDVPESADWYNSSYIIAWGSNVPQTRTPDAHFFTEVRYKGTKTVAITPDYAEIAKLCDLWLAPKQGTDAAMALAMGHVMLREFHLDKPSQYFTDYVRRYTDMPMLVMLEERDGYYAAGRTLRASDLVDSLGQENNPEWKTVAFDEKGDMTVPNGSLGFRWGDKGKWNLEQRDGKTGEEIELRLSLLGSHDEVANVGFPYFGGEGSEHFNKVDLENILLHKLPAKRLQLADGSTALVTTVYDLTMANYGLERGLNDDNCAAGYDEVKAYTPAWAEKITGVSRAHIIRTAREFADNADKTHGRSMIIVGAGLNHWFHLDMNYRGLINMLIFCGCVGQSGGGWAHYVGQEKLRPQTGWQPLAFALDWQRPARHMNSTSYFYNHSSQWRYETVTAQELLSPMADKSRYSGHLIDFNVRAERMGWLPSAPQLGVNPLRIADEAKKAGMTPVDYTVKSLKEGSIRFAAEQPENGKNHPRNLFIWRSNLLGSSGKGHEYMLKYLLGTENGIQGKDLGKQGGVKPEEVEWRDNGLDGKLDLVVTLDFRLSSTCLYSDIVLPTATWYEKDDMNTSDMHPFIHPLSAAVDPAWESKSDWEIYKGIAKKFSEVCVGHLGKETDVVTLPIQHDSAAEMAQPLDVKDWKKGECDLIPGKTAPHIIPVERDYPATYERFTSIGPLLETIGNGGKGIAWNTQSEMDLLRKLNYTKAEGPAKGQPKLETAIDAAEMILTLAPETNGQVAVKAWQALSEITGREHTHLALNKEDEKIRFRDIQAQPRKIISSPTWSGLEDEHVSYNAGYTNVHELIPWRTLSGRQSLYQDHQWMRDFGESLLVYRPPIDTRSVKAVMGEKSNGNPEKALNFLTPHQKWGIHSTYSDNLLMLTLSRGGPIVWMSEADAKDLGIEDNDWIEVFNANGALTARAVVSQRVPAGMTMMYHAQERIVNLPGSEITGQRGGIHNSVTRITPKPTHMIGGYGHLAYGFNYYGTVGSNRDEFVVVRKMKNINWLDGEGNDQVQESVK

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 11 GO

Enzyme Commission (EC)

1.7.5.1

Gene Ontology (GO)

GO:0042126 The chemical reactions and pathways involving nitrates, inorganic or organic salts and esters of nitric acid.
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:0043546 Binding to a molybdopterin cofactor (Moco), essential for the catalytic activity of some enzymes, e.g. sulfite oxidase, xanthine dehydrogenase, and aldehyde oxidase. The cofactor consists of a mononuclear molybdenum (Mo-molybdopterin) or tungsten ion (W-molybdopterin) coordinated by one or two molybdopterin 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:0008940 Catalysis of the reaction: nitrite + acceptor = nitrate + reduced acceptor.
GO:0009325 An enzyme complex that catalyzes the formation of nitrate from nitrite with the concomitant reduction of an acceptor.
GO:0005886 The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.
GO:0046872 Binding to a metal ion.
GO:0160182 Catalysis of the reaction: a quinol + nitrate = a quinone + H2O + nitrite.
GO:0019645 A process in which a series of electron carriers operate together to transfer electrons from donors such as NADH and FADH2 to any of several different terminal electron acceptors other than oxygen to generate a transmembrane electrochemical gradient.
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.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

30 records

Show feature table

Start	End	DB	Term	Name
44	1245	Gene3D	G3DSA:3.40.50.12440	-
1087	1226	CDD	cd02776	MopB_CT_Nitrate-R-NarG-like
1087	1226	InterPro	IPR037943	Nitrate reductase alpha subunit-like, MopB domain
777	794	ProSitePatterns	PS00490	Prokaryotic molybdopterin oxidoreductases signature 2.
777	794	InterPro	IPR006655	Molybdopterin oxidoreductase, prokaryotic, conserved site
48	66	ProSitePatterns	PS00551	Prokaryotic molybdopterin oxidoreductases signature 1.
48	66	InterPro	IPR027467	Molybdopterin oxidoreductase, molybdopterin cofactor binding site
43	107	ProSiteProfiles	PS51669	Prokaryotic molybdopterin oxidoreductases 4Fe-4S domain profile.
43	107	InterPro	IPR006963	Molybdopterin oxidoreductase, 4Fe-4S domain
2	1235	NCBIfam	TIGR01580	nitrate reductase subunit alpha
2	1235	InterPro	IPR006468	Nitrate reductase, alpha subunit
1087	1202	Pfam	PF01568	Molydopterin dinucleotide binding domain
1087	1202	InterPro	IPR006657	Molybdopterin dinucleotide-binding domain
43	105	SMART	SM00926	Molybdop_Fe4S4_2
43	105	InterPro	IPR006963	Molybdopterin oxidoreductase, 4Fe-4S domain
1125	1152	ProSitePatterns	PS00932	Prokaryotic molybdopterin oxidoreductases signature 3.
1125	1152	InterPro	IPR006655	Molybdopterin oxidoreductase, prokaryotic, conserved site
6	1226	PANTHER	PTHR43105	RESPIRATORY NITRATE REDUCTASE
43	834	CDD	cd02750	MopB_Nitrate-R-NarG-like
44	1236	FunFam	G3DSA:3.40.50.12440:FF:000001	Nitrate reductase subunit alpha
2	43	FunFam	G3DSA:4.10.1200.10:FF:000001	Respiratory nitrate reductase subunit alpha
1082	1235	SUPERFAMILY	SSF50692	ADC-like
1082	1235	InterPro	IPR009010	Aspartate decarboxylase-like domain superfamily
108	833	Pfam	PF00384	Molybdopterin oxidoreductase
108	833	InterPro	IPR006656	Molybdopterin oxidoreductase
4	1070	SUPERFAMILY	SSF53706	Formate dehydrogenase/DMSO reductase, domains 1-3
2	43	Gene3D	G3DSA:4.10.1200.10	nitrate reductase tail
2	43	InterPro	IPR044906	Nitrate reductase, alpha subunit, N-terminal domain superfamily
3	40	Pfam	PF14710	Respiratory nitrate reductase alpha N-terminal
3	40	InterPro	IPR028189	Nitrate reductase, alpha subunit, N-terminal

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 #2

0.983

Likely same site as P2Rank 3 0.4 Å 30 shared residues 94% of smaller site

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Surrounding area

Site 2 FPocket #1

0.966

Likely same site as P2Rank 2 0.3 Å 31 shared residues 100% of smaller site

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Surrounding area

Site 3 FPocket #8

0.701

Likely same site as P2Rank 5 2.6 Å 10 shared residues 83% of smaller site

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Surrounding area

Site 4 FPocket #58

0.555

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

0.916

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Surrounding area

Site 2 P2Rank #2

0.863

Likely same site as FPocket 1 0.3 Å 31 shared residues 100% of smaller site

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Surrounding area

Site 3 P2Rank #3

0.826

Likely same site as FPocket 2 0.4 Å 30 shared residues 94% of smaller site

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Surrounding area

Site 4 P2Rank #4

0.34

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Surrounding area

Site 5 P2Rank #5

0.202

Likely same site as FPocket 8 2.6 Å 10 shared residues 83% of smaller site

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Surrounding area

Binding pockets · FPocket

Druggability: high ≥ 0.7 · medium 0.4–0.69 · low < 0.4

Site 1 FPocket #2

0.978

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Surrounding area

Site 2 FPocket #1

0.965

Likely same site as P2Rank 3 0.4 Å 31 shared residues 97% of smaller site

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Surrounding area

Site 3 FPocket #9

0.897

Likely same site as P2Rank 1 3.0 Å 22 shared residues 92% of smaller site

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Surrounding area

Site 4 FPocket #10

0.417

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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

0.886

Likely same site as FPocket 9 3.0 Å 22 shared residues 92% of smaller site

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Surrounding area

Site 2 P2Rank #2

0.885

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Surrounding area

Site 3 P2Rank #3

0.859

Likely same site as FPocket 1 0.4 Å 31 shared residues 97% of smaller site

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Surrounding area

Site 4 P2Rank #4

0.277

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Surrounding area

Site 5 P2Rank #5

0.191

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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_A0A0H3GUA4	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold VK055_0238	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.

63 records

Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 same-protein records

Transferred evidence 13 records from similar proteins

Structural ligands 13 0 loaded crystals

Measured bioactivity 0 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

2MD PDB via homolog 742.6 Da · LogP -2.53 · TPSA 346.6 Open detail RCSB PDB

2MO PDB via homolog Detail RCSB PDB

3PH PDB via homolog Detail RCSB PDB

6MO PDB via homolog Detail RCSB PDB

AGA 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
2MD RCSB PDB	1TMO	O87948	742.6 Da LogP -2.53 TPSA 346.6	3 viol.	✓ Clean	`c1nc2c(n1[C@H]3[C@@H]([C@@H]([C@H](O3)CO[P@@](=…`
2MO RCSB PDB	1TMO	O87948	127.9 Da LogP -0.24 TPSA 34.1	✓ Ro5	✓ Clean	`O=[Mo]=O`
3PH RCSB PDB	1Q16	P09152	705.0 Da LogP 12.07 TPSA 119.4	2 viol.	✓ Clean	`CCCCCCCCCCCCCCCCCC(=O)OC[C@H](COP(=O)(O)O)OC(=O…`
6MO RCSB PDB	1Q16	P09152	95.9 Da LogP -0.00 TPSA 0.0	✓ Ro5	✓ Clean	`[Mo+6]`
AGA RCSB PDB	1Q16	P09152	455.5 Da LogP 1.85 TPSA 151.7	✓ Ro5	✓ Clean	`CCCCCCCC(=O)O[C@H](COC(=O)CCCC)COP(=O)([O-])OC[…`
BSY RCSB PDB	5CHC	G8QM55	128.0 Da LogP -2.25 TPSA 60.4	✓ Ro5	✓ Clean	`O[Se](=O)[O-]`
F3S RCSB PDB	1Q16	P09152	295.8 Da LogP 2.59 TPSA 0.0	✓ Ro5	✓ Clean	`S1[Fe]2S[Fe]3[S]2[Fe]1S3`
H2S RCSB PDB	6SDV	Q72EJ1	34.1 Da LogP 0.11 TPSA 0.0	✓ Ro5	✓ Clean	`S`
MD1 RCSB PDB	1Q16	P09152	740.6 Da LogP -2.13 TPSA 358.0	3 viol.	✓ Clean	`c1nc2c(n1[C@H]3[C@@H]([C@@H]([C@H](O3)CO[P@](=O…`
MGD RCSB PDB	1R27	P09152	740.6 Da LogP -2.06 TPSA 346.6	3 viol.	✓ Clean	`c1nc2c(n1[C@H]3[C@@H]([C@@H]([C@H](O3)CO[P@@](=…`
MO RCSB PDB	1R27	P09152	95.9 Da LogP -0.00 TPSA 0.0	✓ Ro5	✓ Clean	`[Mo]`
PCI RCSB PDB	1Y4Z	P09152	266.3 Da LogP 4.66 TPSA 20.2	✓ Ro5	✓ Clean	`c1(c(c(c(c(c1Cl)Cl)Cl)Cl)Cl)O`
W RCSB PDB	6SDV	Q72EJ1	183.8 Da LogP -0.00 TPSA 0.0	✓ Ro5	✓ Clean	`[W+6]`

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
ZINC1529471 ZINC	1.000	266.3 Da LogP 4.66 TPSA 20.2	✓ Ro5	✓ Clean	`Oc1c(Cl)c(Cl)c(Cl)c(Cl)c1Cl`
ZINC36178999 ZINC	1.000	424.5 Da LogP 4.27 TPSA 119.4	✓ Ro5	✓ Clean	`CCCCCCCC(=O)OC[C@@H](COP(=O)(O)O)OC(=O)CCCCCCC`
ZINC36179002 ZINC	1.000	424.5 Da LogP 4.27 TPSA 119.4	✓ Ro5	✓ Clean	`CCCCCCCC(=O)OC[C@H](COP(=O)(O)O)OC(=O)CCCCCCC`
ZINC5820131 ZINC	0.971	368.4 Da LogP 2.71 TPSA 119.4	✓ Ro5	✓ Clean	`CCCCCC(=O)OC[C@@H](COP(=O)(O)O)OC(=O)CCCCC`
ZINC5820134 ZINC	0.971	368.4 Da LogP 2.71 TPSA 119.4	✓ Ro5	✓ Clean	`CCCCCC(=O)OC[C@H](COP(=O)(O)O)OC(=O)CCCCC`
ZINC225408 ZINC	0.900	247.9 Da LogP 3.71 TPSA 40.5	✓ Ro5	✓ Clean	`Oc1c(Cl)c(Cl)c(O)c(Cl)c1Cl`
ZINC154748 ZINC	0.818	247.9 Da LogP 3.71 TPSA 40.5	✓ Ro5	Alert	`Oc1c(O)c(Cl)c(Cl)c(Cl)c1Cl`
ZINC102191119 ZINC	0.792	498.6 Da LogP 3.65 TPSA 148.8	✓ Ro5	✓ Clean	`CCCCCCCC(=O)OC[C@H](CO[P@@](=O)(O)OC[C@@H](O)CO…`
ZINC58649551 ZINC	0.792	498.6 Da LogP 3.65 TPSA 148.8	✓ Ro5	✓ Clean	`CCCCCCCC(=O)OC[C@H](CO[P@@](=O)(O)OC[C@H](O)CO)…`
ZINC4521879 ZINC	0.743	386.5 Da LogP 4.73 TPSA 78.9	✓ Ro5	✓ Clean	`CCCCCC(=O)OCC(COC(=O)CCCCC)OC(=O)CCCCC`
ZINC102190506 ZINC	0.727	467.5 Da LogP 4.25 TPSA 134.4	✓ Ro5	✓ Clean	`CCCCCCCC(=O)OC[C@H](CO[P@@](=O)(O)OCCN)OC(=O)CC…`
ZINC102190512 ZINC	0.727	467.5 Da LogP 4.25 TPSA 134.4	✓ Ro5	✓ Clean	`CCCCCCCC(=O)OC[C@@H](CO[P@@](=O)(O)OCCN)OC(=O)C…`
ZINC27416437 ZINC	0.705	411.4 Da LogP 2.69 TPSA 134.4	✓ Ro5	✓ Clean	`CCCCCC(=O)OC[C@H](CO[P@](=O)(O)OCCN)OC(=O)CCCCC`
ZINC33902364 ZINC	0.705	411.4 Da LogP 2.69 TPSA 134.4	✓ Ro5	✓ Clean	`CCCCCC(=O)OC[C@@H](CO[P@@](=O)(O)OCCN)OC(=O)CCC…`
ZINC137999083 ZINC	0.700	424.5 Da LogP 4.87 TPSA 113.3	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCCCCC(=O)OC[C@H](O)COP(=O)(O)O`
ZINC42851452 ZINC	0.700	424.5 Da LogP 4.87 TPSA 113.3	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCCCCC(=O)OC[C@@H](O)COP(=O)(O)O`
ZINC62624856 ZINC	0.700	382.4 Da LogP 3.70 TPSA 113.3	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCC(=O)OC[C@H](O)COP(=O)(O)O`
ZINC62624861 ZINC	0.700	382.4 Da LogP 3.70 TPSA 113.3	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCC(=O)OC[C@@H](O)COP(=O)(O)O`
ZINC8218993 ZINC	0.700	410.5 Da LogP 4.48 TPSA 113.3	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCCCC(=O)OC[C@H](O)COP(=O)(O)O`
ZINC8219000 ZINC	0.700	410.5 Da LogP 4.48 TPSA 113.3	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCCCC(=O)OC[C@@H](O)COP(=O)(O)O`
ZINC13543394 ZINC	0.689	455.4 Da LogP 2.15 TPSA 171.7	✓ Ro5	✓ Clean	`CCCCCC(=O)OC[C@H](CO[P@@](=O)(O)OC[C@H](N)C(=O)…`
ZINC104869865 ZINC	0.684	443.2 Da LogP -2.45 TPSA 252.6	2 viol.	✓ Clean	`Nc1nc2c(ncn2[C@H]2O[C@H](CO[P@@](=O)(O)OP(=O)(O…`
ZINC12504289 ZINC	0.684	443.2 Da LogP -2.45 TPSA 252.6	2 viol.	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@H](CO[P@@](=O)(O)OP(=O)(…`
ZINC34541308 ZINC	0.684	443.2 Da LogP -2.45 TPSA 252.6	2 viol.	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@H](CO[P@@](=O)(O)OP(=O)(…`
ZINC35000839 ZINC	0.684	443.2 Da LogP -2.45 TPSA 252.6	2 viol.	✓ Clean	`Nc1nc2c(ncn2[C@H]2O[C@@H](CO[P@@](=O)(O)OP(=O)(…`
ZINC45284491 ZINC	0.684	443.2 Da LogP -2.45 TPSA 252.6	2 viol.	✓ Clean	`Nc1nc2c(ncn2[C@H]2O[C@@H](CO[P@@](=O)(O)OP(=O)(…`
ZINC80639694 ZINC	0.684	443.2 Da LogP -2.45 TPSA 252.6	2 viol.	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@H](CO[P@@](=O)(O)OP(=O)(…`
ZINC8215481 ZINC	0.684	443.2 Da LogP -2.45 TPSA 252.6	2 viol.	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@H](CO[P@@](=O)(O)OP(=O)(…`
ZINC13544781 ZINC	0.681	482.6 Da LogP 4.22 TPSA 108.4	✓ Ro5	✓ Clean	`CCCCCCC(=O)OC[C@@H](CO[P@](=O)(O)OCC[N+](C)(C)C…`
ZINC13544783 ZINC	0.681	482.6 Da LogP 4.22 TPSA 108.4	✓ Ro5	✓ Clean	`CCCCCCC(=O)OC[C@H](CO[P@](=O)(O)OCC[N+](C)(C)C)…`
ZINC13552119 ZINC	0.675	270.2 Da LogP 0.58 TPSA 113.3	✓ Ro5	✓ Clean	`CCCCCC(=O)OC[C@@H](O)COP(=O)(O)O`
ZINC36079847 ZINC	0.667	344.5 Da LogP 4.15 TPSA 72.8	✓ Ro5	✓ Clean	`CCCCCCCC(=O)OC[C@@H](CO)OC(=O)CCCCCCC`
ZINC4521911 ZINC	0.667	344.4 Da LogP 3.56 TPSA 78.9	✓ Ro5	✓ Clean	`CCCCC(=O)OCC(COC(=O)CCCC)OC(=O)CCCC`
ZINC8214428 ZINC	0.667	344.5 Da LogP 4.15 TPSA 72.8	✓ Ro5	✓ Clean	`CCCCCCCC(=O)OC[C@H](CO)OC(=O)CCCCCCC`
ZINC13543439 ZINC	0.660	454.5 Da LogP 3.44 TPSA 108.4	✓ Ro5	✓ Clean	`CCCCCC(=O)OC[C@@H](CO[P@](=O)(O)OCC[N+](C)(C)C)…`
ZINC13543441 ZINC	0.660	454.5 Da LogP 3.44 TPSA 108.4	✓ Ro5	✓ Clean	`CCCCCC(=O)OC[C@H](CO[P@](=O)(O)OCC[N+](C)(C)C)O…`
ZINC103659671 ZINC	0.641	358.5 Da LogP 3.95 TPSA 78.9	✓ Ro5	✓ Clean	`CCCCCCCCCCCC(=O)OC(COC(C)=O)COC(C)=O`
ZINC5820130 ZINC	0.641	288.4 Da LogP 2.59 TPSA 72.8	✓ Ro5	✓ Clean	`CCCCCC(=O)OC[C@@H](CO)OC(=O)CCCCC`
ZINC5820133 ZINC	0.641	288.4 Da LogP 2.59 TPSA 72.8	✓ Ro5	✓ Clean	`CCCCCC(=O)OC[C@H](CO)OC(=O)CCCCC`
ZINC27646150 ZINC	0.625	274.4 Da LogP 2.20 TPSA 72.8	✓ Ro5	✓ Clean	`CCCCCC(=O)OC[C@H](CO)OC(=O)CCCC`
ZINC102191158 ZINC	0.620	456.5 Da LogP 3.08 TPSA 142.8	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCC(=O)OC[C@H](O)CO[P@@](=O)(O)OC[C@…`
ZINC14880758 ZINC	0.620	484.6 Da LogP 3.86 TPSA 142.8	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCCCC(=O)OC[C@@H](O)CO[P@](=O)(O)OC[…`
ZINC14880760 ZINC	0.620	484.6 Da LogP 3.86 TPSA 142.8	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCCCC(=O)OC[C@H](O)CO[P@](=O)(O)OC[C…`
ZINC53683910 ZINC	0.620	484.6 Da LogP 3.86 TPSA 142.8	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCCCC(=O)OC[C@H](O)CO[P@@](=O)(O)OC[…`
ZINC62592202 ZINC	0.620	456.5 Da LogP 3.08 TPSA 142.8	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCC(=O)OC[C@H](O)CO[P@@](=O)(O)OC[C@…`
ZINC62592203 ZINC	0.620	456.5 Da LogP 3.08 TPSA 142.8	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCC(=O)OC[C@@H](O)CO[P@@](=O)(O)OC[C…`
ZINC62592204 ZINC	0.620	484.6 Da LogP 3.86 TPSA 142.8	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCCCC(=O)OC[C@@H](O)CO[P@@](=O)(O)OC…`
ZINC96094841 ZINC	0.620	456.5 Da LogP 3.08 TPSA 142.8	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCC(=O)OC[C@@H](O)CO[P@@](=O)(O)OC[C…`
ZINC12958448 ZINC	0.610	363.2 Da LogP -2.57 TPSA 206.0	1 viol.	✓ Clean	`Nc1nc2c(ncn2[C@@H]2O[C@H](COP(=O)(O)O)[C@H](O)[…`
ZINC3073318 ZINC	0.610	363.2 Da LogP -2.57 TPSA 206.0	1 viol.	✓ Clean	`Nc1nc2c(ncn2[C@H]2O[C@@H](COP(=O)(O)O)[C@@H](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.