KpKP13 Protein target profile

1-deoxy-D-xylulose 5-phosphate reductoisomerase

Accession: KP13_01807

Gene: dxr AHE46247.1 3D evidence: AlphaFold DB model + ColabFold model UniProt A0A0H3GJN7

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Length 400

Pocket druggability (P2Rank · AlphaFold DB model) 0.943

Direct ligand evidence 0 99 total records

Functional annotation 1 EC 7 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: P2Rank + FPocket Both predictors report a high-scoring binding site (P2Rank 0.94, FPocket 0.96). 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 0.96. This is a computational pocket signal, not binding validation. 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: No hit
Gut microbiome similarity: 4.3% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 80.402 Higher values support similarity to known essential genes.
DEG E-value: 0.0 Smaller values mean stronger essential-gene similarity.

Structure confidence

ColabFold pLDDT: 97.11 0-100 confidence; >70 supports local structural interpretation.

Binding-site evidence

AlphaFold DB / UniProt 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) 0.943

Structure A0A0H3GJN7

Pocket Pocket 1

Druggability (FPocket) 0.956

Structure A0A0H3GJN7

Pocket Pocket 1

ColabFold model

P2Rank 0.948 · Pocket 1

FPocket 0.905 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 205 / 4744 genomes with a hit

Prevalence 4.3%

Sequence

Primary amino-acid sequence viewer.

MKQLTVLGSTGSIGCSTLDVVRHNPGRFSVAALVAGKNVDRMVEQCLEFTPRYAVMDDAQSAERLRTRLHEHGCRTEVLSGQQAAAEVAALDEVDQVMAAIVGAAGLVPTLAAIRAGKTVLLANKESLVTCGRLFMEAVQQSGARLLPVDSEHNAIFQSMPETIQQHLGYADLARNGVSSILLTGSGGPFRETAVAELAAMTPDQACRHPNWSMGRKISVDSATMMNKGLEYIEARWLFNASAQQMEVLIHPQSVIHSMVRYQDGSVLAQLGEPDMRTPIAHTMGWPQRLNSGVKPLDFCQLSNLSFSAPDYTRYPCLKLAMDAFDVGQAATTTLNAANEESVAAFLHGDIRFTDIAAVNLAVLDKMDLQEPQSIDDVLVIDAEARAIAHQQLQRLVAQA

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 7 GO

Subcellular localization

Localization: CytoplasmicMembrane

Enzyme Commission (EC)

1.1.1.267

Gene Ontology (GO)

GO:0070402 Binding to the reduced form, NADPH, of nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions.
GO:0046872 Binding to a metal ion.
GO:0030604 Catalysis of the reaction: 2-C-methyl-D-erythritol 4-phosphate + NADP+ = 1-deoxy-D-xylulose 5-phosphate + H+ + NADPH.
GO:0005515 Binding to a protein.
GO:0008299 The chemical reactions and pathways resulting in the formation of an isoprenoid compound, isoprene (2-methylbuta-1,3-diene) or compounds containing or derived from linked isoprene (3-methyl-2-butenylene) residues.
GO:0030145 Binding to a manganese ion (Mn).
GO:0051484 OBSOLETE. The chemical reactions and pathways resulting in the formation of isopentenyl diphosphate by the mevalonate-independent pathway that contributes to terpenoid biosynthesis. Isopentenyl diphosphate (IPP) is the fundamental unit in isoprenoid biosynthesis and is biosynthesized from pyruvate and glyceraldehyde 3-phosphate via intermediates, including 1-deoxy-D-xylulose 5-phosphate.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

24 records

Show feature table

Start	End	DB	Term	Name
2	150	SUPERFAMILY	SSF51735	NAD(P)-binding Rossmann-fold domains
2	150	InterPro	IPR036291	NAD(P)-binding domain superfamily
301	395	SUPERFAMILY	SSF69055	1-deoxy-D-xylulose-5-phosphate reductoisomerase, C-terminal domain
301	395	InterPro	IPR036169	DXP reductoisomerase, C-terminal domain superfamily
4	392	Hamap	MF_00183	1-deoxy-D-xylulose 5-phosphate reductoisomerase [dxr].
4	392	InterPro	IPR003821	1-deoxy-D-xylulose 5-phosphate reductoisomerase
1	15	ProSiteProfiles	PS51257	Prokaryotic membrane lipoprotein lipid attachment site profile.
271	387	Pfam	PF13288	DXP reductoisomerase C-terminal domain
271	387	InterPro	IPR026877	DXP reductoisomerase C-terminal domain
1	150	Gene3D	G3DSA:3.40.50.720	-
1	399	PIRSF	PIRSF006205	Dxp_reductoisomrs
1	399	InterPro	IPR003821	1-deoxy-D-xylulose 5-phosphate reductoisomerase
312	398	Gene3D	G3DSA:1.10.1740.10	-
4	132	Pfam	PF02670	1-deoxy-D-xylulose 5-phosphate reductoisomerase
4	132	InterPro	IPR013512	1-deoxy-D-xylulose 5-phosphate reductoisomerase, N-terminal
1	150	FunFam	G3DSA:3.40.50.720:FF:000045	1-deoxy-D-xylulose 5-phosphate reductoisomerase
126	274	SUPERFAMILY	SSF55347	Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain
1	397	NCBIfam	TIGR00243	1-deoxy-D-xylulose-5-phosphate reductoisomerase
1	397	InterPro	IPR003821	1-deoxy-D-xylulose 5-phosphate reductoisomerase
146	239	Pfam	PF08436	1-deoxy-D-xylulose 5-phosphate reductoisomerase C-terminal domain
146	239	InterPro	IPR013644	1-deoxy-D-xylulose 5-phosphate reductoisomerase, C-terminal
2	393	PANTHER	PTHR30525	1-DEOXY-D-XYLULOSE 5-PHOSPHATE REDUCTOISOMERASE
2	393	InterPro	IPR003821	1-deoxy-D-xylulose 5-phosphate reductoisomerase
312	397	FunFam	G3DSA:1.10.1740.10:FF:000004	1-deoxy-D-xylulose 5-phosphate reductoisomerase

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

0.943

Likely same site as FPocket 1 4.1 Å 29 shared residues 97% of smaller site

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Surrounding area

Pocket 2 P2Rank #2

0.028

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Surrounding area

Pocket 3 P2Rank #3

0.003

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Surrounding area

Pocket 4 P2Rank #4

0.001

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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 #1

0.956 Unusual size

Likely same site as P2Rank 1 4.1 Å 29 shared residues 97% of smaller site

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Surrounding area

Pocket 2 FPocket #4

0.488

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Surrounding area

Pocket 3 FPocket #22

0.341

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Surrounding area

Residue sets

UniProt: Binding site:10-10

UniProt: Binding site:11-11

UniProt: Binding site:12-12

UniProt: Binding site:124-124

UniProt: Binding site:125-125

UniProt: Binding site:126-126

UniProt: Binding site:13-13

UniProt: Binding site:150-150

UniProt: Binding site:151-151

UniProt: Binding site:152-152

UniProt: Binding site:186-186

UniProt: Binding site:209-209

UniProt: Binding site:215-215

UniProt: Binding site:222-222

UniProt: Binding site:227-227

UniProt: Binding site:228-228

UniProt: Binding site:231-231

UniProt: Binding site:36-36

UniProt: Binding site:37-37

UniProt: Binding site:38-38

Binding pockets · P2Rank

Druggability (P2Rank): high ≥ 0.5 · medium 0.2–0.49 · low < 0.2

Pocket 1 P2Rank #1

0.948

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Surrounding area

Pocket 2 P2Rank #2

0.08

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Surrounding area

Pocket 3 P2Rank #3

0.015

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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_A0A0H3GJN7	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold KP13_01807	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.

99 records

Chemistry signal

Structural and bioactivity evidence are both available for this target.

Direct evidence 0 same-protein records

Transferred evidence 49 records from similar proteins

Structural ligands 7 0 loaded crystals

Measured bioactivity 42 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

C0K PDB via homolog 309.2 Da · LogP 1.81 · TPSA 98.1 Open detail RCSB PDB

CBQ PDB via homolog Detail RCSB PDB

DXP PDB via homolog Detail RCSB PDB

IMB PDB via homolog Detail RCSB PDB

SRT 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
C0K RCSB PDB	3R0I	P45568	309.2 Da LogP 1.81 TPSA 98.1	✓ Ro5	✓ Clean	`CN(C(=O)CC[C@@H](c1ccc(c(c1)F)F)P(=O)(O)O)O`
CBQ RCSB PDB	1T1S	P45568	302.5 Da LogP 0.79 TPSA 140.0	✓ Ro5	✓ Clean	`c1cc(ncc1Cl)NC(P(=O)(O)O)P(=O)(O)O`
DXP RCSB PDB	1Q0Q	P45568	214.1 Da LogP -1.59 TPSA 124.3	✓ Ro5	✓ Clean	`CC(=O)[C@H]([C@@H](COP(=O)(O)O)O)O`
IMB RCSB PDB	1T1R	P45568	318.2 Da LogP 1.29 TPSA 140.0	✓ Ro5	✓ Clean	`c1ccc2c(c1)ccnc2NC(P(=O)(O)O)P(=O)(O)O`
SRT RCSB PDB	5KRV	Q8DBF5	150.1 Da LogP -2.12 TPSA 115.1	✓ Ro5	✓ Clean	`[C@H]([C@H](C(=O)O)O)(C(=O)O)O`
SYC RCSB PDB	3ANL	P45568	173.1 Da LogP 0.76 TPSA 70.4	✓ Ro5	✓ Clean	`c1ccnc(c1)CP(=O)(O)O`
SYE RCSB PDB	3ANN	P45568	223.2 Da LogP 1.91 TPSA 70.4	✓ Ro5	✓ Clean	`c1ccc2c(c1)ccc(n2)CP(=O)(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
CHEMBL4567904 ChEMBL	W8T2T2	7.89 ~12.9 nM	313.2 Da LogP 1.38 TPSA 106.9	✓ Ro5	✓ Clean	`O=C(CSC(c1cc(F)cc(F)c1)P(=O)(O)O)NO`
CHEMBL4590343 ChEMBL	W8T2T2	7.75 ~17.8 nM	327.2 Da LogP 1.72 TPSA 98.1	✓ Ro5	✓ Clean	`CN(O)C(=O)CSC(c1cc(F)cc(F)c1)P(=O)(O)O`
FOM ChEMBL	P45568	7.70 ~20.0 nM	183.1 Da LogP -0.60 TPSA 98.1	✓ Ro5	✓ Clean	`C(CN(C=O)O)CP(=O)(O)O`
CHEMBL4474216 ChEMBL	W8T2T2	7.66 ~21.9 nM	323.3 Da LogP 1.82 TPSA 106.9	✓ Ro5	✓ Clean	`CSc1ccc(C(SCC(=O)NO)P(=O)(O)O)cc1`
F98 ChEMBL	P45568	7.55 ~28.2 nM	197.1 Da LogP -0.21 TPSA 98.1	✓ Ro5	✓ Clean	`CC(=O)N(CCCP(=O)(O)O)O`
CHEMBL258981 ChEMBL	P45568	7.32 ~47.9 nM	197.1 Da LogP -0.21 TPSA 98.1	✓ Ro5	✓ Clean	`CN(O)C(=O)CCCP(=O)(O)O`
CHEMBL204406 ChEMBL	P45568	7.30 ~50.1 nM	209.1 Da LogP -0.21 TPSA 98.1	✓ Ro5	✓ Clean	`CC(=O)N(O)C[C@@H]1C[C@H]1P(=O)(O)O`
CHEMBL607359 ChEMBL	P45568	7.27 ~53.7 nM	211.2 Da LogP 0.18 TPSA 98.1	✓ Ro5	✓ Clean	`CC(=O)N(O)CCC(C)P(=O)(O)O`
CHEMBL204106 ChEMBL	P45568	7.23 ~58.9 nM	328.1 Da LogP 2.45 TPSA 98.1	✓ Ro5	✓ Clean	`O=CN(O)CCC(c1ccc(Cl)c(Cl)c1)P(=O)(O)O`
CHEMBL606521 ChEMBL	P45568	7.19 ~64.6 nM	195.1 Da LogP -0.08 TPSA 98.1	✓ Ro5	✓ Clean	`CC(=O)N(O)C/C=C/P(=O)(O)O`
CHEMBL3341763 ChEMBL	P45568	7.16 ~69.2 nM	303.3 Da LogP 1.54 TPSA 107.3	✓ Ro5	✓ Clean	`COc1ccc(C(CCC(=O)N(C)O)P(=O)(O)O)cc1`
CHEMBL1651835 ChEMBL	P45568	7.00 ~100.0 nM	307.7 Da LogP 2.19 TPSA 98.1	✓ Ro5	✓ Clean	`CC(=O)N(O)CC[C@H](c1ccc(Cl)cc1)P(=O)(O)O`
CHEMBL206189 ChEMBL	P45568	7.00 ~100.0 nM	307.7 Da LogP 2.19 TPSA 98.1	✓ Ro5	✓ Clean	`CC(=O)N(O)CCC(c1ccc(Cl)cc1)P(=O)(O)O`
CHEMBL607492 ChEMBL	P45568	7.00 ~100.0 nM	259.2 Da LogP 1.09 TPSA 98.1	✓ Ro5	✓ Clean	`O=C(c1ccccc1)N(O)CCCP(=O)(O)O`
CHEMBL204107 ChEMBL	P45568	6.92 ~120.2 nM	342.1 Da LogP 2.84 TPSA 98.1	✓ Ro5	✓ Clean	`CC(=O)N(O)CCC(c1ccc(Cl)c(Cl)c1)P(=O)(O)O`
DCV ChEMBL	P45568	6.92 ~120.2 nM	342.1 Da LogP 2.84 TPSA 98.1	✓ Ro5	✓ Clean	`CC(=O)N(CC[C@H](c1ccc(c(c1)Cl)Cl)P(=O)(O)O)O`
CHEMBL3342259 ChEMBL	P45568	6.85 ~141.3 nM	289.2 Da LogP 1.20 TPSA 116.1	✓ Ro5	✓ Clean	`COc1ccc(C(CCC(=O)NO)P(=O)(O)O)cc1`
CHEMBL205339 ChEMBL	P45568	6.81 ~154.9 nM	289.2 Da LogP 1.15 TPSA 107.3	✓ Ro5	✓ Clean	`COc1ccc(C(CCN(O)C=O)P(=O)(O)O)cc1`
CHEMBL380319 ChEMBL	P45568	6.80 ~158.5 nM	209.1 Da LogP -0.21 TPSA 98.1	✓ Ro5	✓ Clean	`CC(=O)N(O)CC1CC1P(=O)(O)O`
CHEMBL4592986 ChEMBL	W8T2T2	6.80 ~158.5 nM	351.3 Da LogP 1.46 TPSA 116.5	✓ Ro5	✓ Clean	`COc1cc(OC)cc(C(SCC(=O)N(C)O)P(=O)(O)O)c1`
CHEMBL1161784 ChEMBL	P45568	6.77 ~169.8 nM	183.1 Da LogP -0.55 TPSA 106.9	✓ Ro5	✓ Clean	`O=C(CCCP(=O)(O)O)NO`
CHEMBL607488 ChEMBL	P45568	6.75 ~177.8 nM	266.0 Da LogP 0.58 TPSA 98.1	✓ Ro5	✓ Clean	`O=C(C(Cl)Cl)N(O)CCCP(=O)(O)O`
CHEMBL2164257 ChEMBL	W8T2T2	6.66 ~218.8 nM	205.1 Da LogP -4.23 TPSA 100.9	✓ Ro5	✓ Clean	`O=CN(O)CCCP(=O)([O-])O.[Na+]`
CHEMBL607412 ChEMBL	P45568	6.64 ~229.1 nM	309.3 Da LogP 2.24 TPSA 98.1	✓ Ro5	✓ Clean	`O=C(c1cccc2ccccc12)N(O)CCCP(=O)(O)O`
CHEMBL205052 ChEMBL	P45568	6.55 ~281.8 nM	273.2 Da LogP 1.53 TPSA 98.1	✓ Ro5	✓ Clean	`CC(=O)N(O)CCC(c1ccccc1)P(=O)(O)O`
CHEMBL2164256 ChEMBL	P45568	6.54 ~288.4 nM	287.3 Da LogP 1.84 TPSA 98.1	✓ Ro5	✓ Clean	`Cc1ccc(C(CCC(=O)N(C)O)P(=O)(O)O)cc1`
CHEMBL4447571 ChEMBL	W8T2T2	6.54 ~288.4 nM	291.3 Da LogP 1.41 TPSA 106.9	✓ Ro5	✓ Clean	`Cc1ccc(C(SCC(=O)NO)P(=O)(O)O)cc1`
CHEMBL1651834 ChEMBL	P45568	6.51 ~309.0 nM	273.2 Da LogP 1.53 TPSA 98.1	✓ Ro5	✓ Clean	`CC(=O)N(O)CC[C@H](c1ccccc1)P(=O)(O)O`
CHEMBL205091 ChEMBL	P45568	6.50 ~316.2 nM	195.1 Da LogP -0.60 TPSA 98.1	✓ Ro5	✓ Clean	`O=CN(O)C[C@@H]1C[C@H]1P(=O)(O)O`
CHEMBL3342260 ChEMBL	P45568	6.50 ~316.2 nM	333.3 Da LogP 1.55 TPSA 116.5	✓ Ro5	✓ Clean	`COc1ccc(C(CCC(=O)N(C)O)P(=O)(O)O)cc1OC`
CHEMBL1651833 ChEMBL	P45568	6.40 ~398.1 nM	287.3 Da LogP 1.84 TPSA 98.1	✓ Ro5	✓ Clean	`CC(=O)N(O)CC[C@H](c1ccc(C)cc1)P(=O)(O)O`
CHEMBL205053 ChEMBL	P45568	6.40 ~398.1 nM	287.3 Da LogP 1.84 TPSA 98.1	✓ Ro5	✓ Clean	`CC(=O)N(O)CCC(c1ccc(C)cc1)P(=O)(O)O`
CHEMBL3342262 ChEMBL	P45568	6.35 ~446.7 nM	305.2 Da LogP 0.74 TPSA 116.5	✓ Ro5	✓ Clean	`COc1ccc(C(OCC(=O)N(C)O)P(=O)(O)O)cc1`
CHEMBL1651832 ChEMBL	P45568	6.34 ~457.1 nM	303.3 Da LogP 1.54 TPSA 107.3	✓ Ro5	✓ Clean	`COc1ccc([C@@H](CCN(O)C(C)=O)P(=O)(O)O)cc1`
CHEMBL380142 ChEMBL	P45568	6.34 ~457.1 nM	303.3 Da LogP 1.54 TPSA 107.3	✓ Ro5	✓ Clean	`COc1ccc(C(CCN(O)C(C)=O)P(=O)(O)O)cc1`
CHEMBL606611 ChEMBL	P45568	6.19 ~645.7 nM	211.2 Da LogP 0.04 TPSA 98.1	✓ Ro5	✓ Clean	`CC(=O)N(O)CC(C)CP(=O)(O)O`
CHEMBL4544750 ChEMBL	W8T2T2	6.17 ~676.1 nM	337.3 Da LogP 1.12 TPSA 125.3	✓ Ro5	✓ Clean	`COc1cc(OC)cc(C(SCC(=O)NO)P(=O)(O)O)c1`
CHEMBL3342258 ChEMBL	P45568	6.16 ~691.8 nM	273.2 Da LogP 1.50 TPSA 106.9	✓ Ro5	✓ Clean	`Cc1ccc(C(CCC(=O)NO)P(=O)(O)O)cc1`
CHEMBL607413 ChEMBL	P45568	6.15 ~707.9 nM	225.2 Da LogP 0.57 TPSA 98.1	✓ Ro5	✓ Clean	`CCC(CCN(O)C(C)=O)P(=O)(O)O`
SYD ChEMBL	P45568	6.08 ~831.8 nM	249.2 Da LogP 2.43 TPSA 70.4	✓ Ro5	✓ Clean	`c1ccc(cc1)c2ccc(nc2)CP(=O)(O)O`
CHEMBL607353 ChEMBL	P45568	6.00 ~1.0 µM	374.3 Da LogP 0.75 TPSA 136.4	✓ Ro5	✓ Clean	`O=C(CCCOc1ccccc1)NCC(=O)N(O)CCCP(=O)(O)O`
CHEMBL3422253 ChEMBL	W8T2T2	—	309.2 Da LogP -2.37 TPSA 100.9	✓ Ro5	✓ Clean	`CN(O)C(=O)CC(Cc1ccccc1)CP(=O)([O-])O.[Na+]`

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
ZINC1532902 ZINC	0.700	206.2 Da LogP -0.86 TPSA 132.1	✓ Ro5	✓ Clean	`O=C(O)CC[C@@](O)(CC(=O)O)C(=O)O`
ZINC2018106 ZINC	0.700	206.2 Da LogP -0.86 TPSA 132.1	✓ Ro5	✓ Clean	`O=C(O)CC[C@](O)(CC(=O)O)C(=O)O`
ZINC12359024 ZINC	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@H](O)[C@H](O)[C@@H](O)C(=O)O`
ZINC13533920 ZINC	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@H](O)[C@@H](O)[C@@H](O)C(=O)O`
ZINC1532740 ZINC	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@H](O)[C@@H](O)[C@H](O)C(=O)O`
ZINC1549593 ZINC	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@H](O)[C@H](O)[C@@H](O)[C@@H](O)C(=O)O`
ZINC2013424 ZINC	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@@H](O)[C@@H](O)[C@H](O)C(=O)O`
ZINC3581021 ZINC	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@H](O)[C@@H](O)[C@@H](O)[C@@H](O)C(=O)O`
ZINC3860635 ZINC	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@@H](O)[C@H](O)[C@H](O)C(=O)O`
ZINC5783661 ZINC	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@@H](O)[C@H](O)[C@@H](O)C(=O)O`
ZINC6072527 ZINC	0.692	210.1 Da LogP -3.40 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@@H](O)[C@@H](O)[C@@H](O)C(=O)O`
ZINC3593496 ZINC	0.652	206.2 Da LogP -1.16 TPSA 121.1	✓ Ro5	✓ Clean	`COC(=O)C[C@@](O)(CC(=O)O)C(=O)O`
ZINC3593497 ZINC	0.652	206.2 Da LogP -1.16 TPSA 121.1	✓ Ro5	✓ Clean	`COC(=O)C[C@](O)(CC(=O)O)C(=O)O`
ZINC1999562 ZINC	0.645	267.1 Da LogP 0.31 TPSA 128.0	✓ Ro5	✓ Clean	`O=P(O)(O)C(Cc1ccccn1)P(=O)(O)O`
ZINC1529626 ZINC	0.633	230.1 Da LogP -2.62 TPSA 144.5	✓ Ro5	✓ Clean	`O=C(CO)[C@H](O)[C@@H](O)COP(=O)(O)O`
ZINC1532567 ZINC	0.633	230.1 Da LogP -2.62 TPSA 144.5	✓ Ro5	✓ Clean	`O=C(CO)[C@H](O)[C@H](O)COP(=O)(O)O`
ZINC1532851 ZINC	0.633	230.1 Da LogP -2.62 TPSA 144.5	✓ Ro5	✓ Clean	`O=C(CO)[C@@H](O)[C@@H](O)COP(=O)(O)O`
ZINC30320708 ZINC	0.633	230.1 Da LogP -2.62 TPSA 144.5	✓ Ro5	✓ Clean	`O=C(CO)[C@@H](O)[C@H](O)COP(=O)(O)O`
ZINC3870277 ZINC	0.633	310.1 Da LogP -2.50 TPSA 191.0	1 viol.	✓ Clean	`O=C(COP(=O)(O)O)[C@H](O)[C@H](O)COP(=O)(O)O`
ZINC14686440 ZINC	0.625	436.4 Da LogP -2.64 TPSA 247.9	1 viol.	✓ Clean	`O=C(O)C[C@](O)(CC(=O)NCCCCNC(=O)C[C@@](O)(CC(=O…`
ZINC14686442 ZINC	0.625	436.4 Da LogP -2.64 TPSA 247.9	1 viol.	✓ Clean	`O=C(O)C[C@@](O)(CC(=O)NCCCCNC(=O)C[C@](O)(CC(=O…`
ZINC14686444 ZINC	0.625	436.4 Da LogP -2.64 TPSA 247.9	1 viol.	✓ Clean	`O=C(O)C[C@@](O)(CC(=O)NCCCCNC(=O)C[C@@](O)(CC(=…`
ZINC27644247 ZINC	0.618	230.3 Da LogP 0.09 TPSA 111.2	✓ Ro5	✓ Clean	`CCCCNC(=N)NCCC[C@H](N)C(=O)O`
ZINC5830339 ZINC	0.613	231.1 Da LogP -2.68 TPSA 156.5	1 viol.	✓ Clean	`O=C(NO)[C@H](O)[C@H](O)COP(=O)(O)O`
ZINC5497290 ZINC	0.600	260.3 Da LogP 1.80 TPSA 81.1	✓ Ro5	✓ Clean	`CN(O)C(=O)CCCCCCCCC(=O)N(C)O`
ZINC1560405156 ZINC	0.588	208.1 Da LogP -1.79 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)/C(O)=C(\O)[C@H](O)[C@H](O)C(=O)O`
ZINC1560405157 ZINC	0.588	208.1 Da LogP -1.79 TPSA 155.5	1 viol.	✓ Clean	`O=C(O)/C(O)=C(/O)[C@H](O)[C@H](O)C(=O)O`
ZINC196899382 ZINC	0.588	228.2 Da LogP -0.14 TPSA 92.4	✓ Ro5	✓ Clean	`N[C@@H](CCCNC(=O)C(F)(F)F)C(=O)O`
ZINC4155291 ZINC	0.583	216.2 Da LogP -1.37 TPSA 130.8	✓ Ro5	✓ Clean	`CC(=O)/N=C(\N)NCCC[C@H](N)C(=O)O`
ZINC4155299 ZINC	0.583	216.2 Da LogP -1.37 TPSA 130.8	✓ Ro5	✓ Clean	`CC(=O)/N=C(\N)NCCC[C@@H](N)C(=O)O`
ZINC13398039 ZINC	0.577	234.2 Da LogP -0.38 TPSA 121.1	✓ Ro5	✓ Clean	`CC(C)OC(=O)C[C@](O)(CC(=O)O)C(=O)O`
ZINC2528012 ZINC	0.577	234.2 Da LogP -0.38 TPSA 121.1	✓ Ro5	✓ Clean	`CC(C)OC(=O)C[C@@](O)(CC(=O)O)C(=O)O`
ZINC5940604 ZINC	0.576	283.1 Da LogP -0.37 TPSA 148.2	✓ Ro5	✓ Clean	`O=P(O)(O)C(O)(Cc1ccccn1)P(=O)(O)O`
ZINC1529718 ZINC	0.571	202.3 Da LogP -0.74 TPSA 102.4	✓ Ro5	✓ Clean	`CN(C)C(=N)NCCC[C@H](N)C(=O)O`
ZINC1546170 ZINC	0.571	216.3 Da LogP -0.30 TPSA 111.2	✓ Ro5	✓ Clean	`CCCNC(=N)NCCC[C@H](N)C(=O)O`
ZINC2560273 ZINC	0.571	202.3 Da LogP -0.69 TPSA 111.2	✓ Ro5	✓ Clean	`CCNC(=N)NCCC[C@H](N)C(=O)O`
ZINC4543782 ZINC	0.571	202.3 Da LogP -0.74 TPSA 102.4	✓ Ro5	✓ Clean	`CN(C)C(=N)NCCC[C@@H](N)C(=O)O`
ZINC7997269 ZINC	0.571	205.3 Da LogP 0.07 TPSA 99.2	✓ Ro5	✓ Clean	`CSC(=N)NCCC[C@@H](N)C(=O)O`
ZINC13283860 ZINC	0.567	284.4 Da LogP 4.57 TPSA 25.8	✓ Ro5	✓ Clean	`c1ccc2nc(CCc3ccc4ccccc4n3)ccc2c1`
ZINC1744468 ZINC	0.567	270.3 Da LogP 4.37 TPSA 25.8	✓ Ro5	✓ Clean	`c1ccc2nc(Cc3ccc4ccccc4n3)ccc2c1`
ZINC3873635 ZINC	0.565	204.2 Da LogP 0.34 TPSA 98.7	✓ Ro5	✓ Clean	`O=C(CCCCCCC(=O)NO)NO`
ZINC5178518 ZINC	0.565	218.3 Da LogP 0.73 TPSA 98.7	✓ Ro5	✓ Clean	`O=C(CCCCCCCC(=O)NO)NO`
ZINC5496762 ZINC	0.565	232.3 Da LogP 1.12 TPSA 98.7	✓ Ro5	✓ Clean	`O=C(CCCCCCCCC(=O)NO)NO`
ZINC5496778 ZINC	0.565	260.3 Da LogP 1.90 TPSA 98.7	✓ Ro5	✓ Clean	`O=C(CCCCCCCCCCC(=O)NO)NO`
ZINC3122018 ZINC	0.564	297.3 Da LogP 3.98 TPSA 39.2	✓ Ro5	✓ Clean	`CO[P@@](=O)(Cc1ccc2ccccc2n1)c1ccccc1`
ZINC391654 ZINC	0.564	297.3 Da LogP 3.98 TPSA 39.2	✓ Ro5	✓ Clean	`CO[P@](=O)(Cc1ccc2ccccc2n1)c1ccccc1`
ZINC146315135 ZINC	0.560	204.2 Da LogP 0.86 TPSA 94.8	✓ Ro5	✓ Clean	`CCCCC[C@@](O)(CC(=O)O)C(=O)O`
ZINC146315336 ZINC	0.560	204.2 Da LogP 0.86 TPSA 94.8	✓ Ro5	✓ Clean	`CCCCC[C@](O)(CC(=O)O)C(=O)O`
ZINC13209107 ZINC	0.559	229.2 Da LogP 2.85 TPSA 48.4	✓ Ro5	✓ Clean	`CCOP(=O)(Cc1ccccn1)OCC`
ZINC218922593 ZINC	0.559	204.2 Da LogP -1.32 TPSA 112.6	✓ Ro5	✓ Clean	`N[C@@H](CCCCNC(=O)CO)C(=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.

Cross-references

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

Sequence

UniProt A0A0H3GJN7

Chemistry

ChEMBL CHEMBL4567904 ChEMBL CHEMBL4590343 ChEMBL FOM ChEMBL CHEMBL4474216 ChEMBL F98 ChEMBL CHEMBL258981 ChEMBL CHEMBL204406 ChEMBL CHEMBL607359 ChEMBL CHEMBL204106 ChEMBL CHEMBL606521 ChEMBL CHEMBL3341763 ChEMBL CHEMBL1651835 ChEMBL CHEMBL206189 ChEMBL CHEMBL607492 ChEMBL CHEMBL204107 ChEMBL DCV ChEMBL CHEMBL3342259 ChEMBL CHEMBL205339 ChEMBL CHEMBL380319 ChEMBL CHEMBL4592986 ChEMBL CHEMBL1161784 ChEMBL CHEMBL607488 ChEMBL CHEMBL2164257 ChEMBL CHEMBL607412 ChEMBL CHEMBL205052 ChEMBL CHEMBL2164256 ChEMBL CHEMBL4447571 ChEMBL CHEMBL1651834 ChEMBL CHEMBL205091 ChEMBL CHEMBL3342260 ChEMBL CHEMBL1651833 ChEMBL CHEMBL205053 ChEMBL CHEMBL3342262 ChEMBL CHEMBL1651832 ChEMBL CHEMBL380142 ChEMBL CHEMBL606611 ChEMBL CHEMBL4544750 ChEMBL CHEMBL3342258 ChEMBL CHEMBL607413 ChEMBL SYD ChEMBL CHEMBL607353 ChEMBL CHEMBL3422253