KpKP13 Protein target profile

2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase

Accession: KP13_02514

Gene: AHE42980.1 ispD 3D evidence: AlphaFold DB model + ColabFold model UniProt A0A0H3GWT7

Export view

Length 236

Pocket druggability (P2Rank · AlphaFold DB model) 0.37

Direct ligand evidence 0 63 total records

Functional annotation 1 EC 5 GO

Target summary

Target candidate with partial support; inspect missing evidence before prioritizing.

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

Main supporting evidence

Core gene across strains Marked as conserved by both pan-genome tools: Roary and CoreCruncher. Structure available AlphaFold DB model + ColabFold model Ligand evidence via structure/bioactivity 7 structural and 6 bioactivity records.

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 (%): 26.984 Lower values reduce human off-target concern.
Human E-value: 3.14e-16
Gut microbiome similarity: 3.0% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 86.864 Higher values support similarity to known essential genes.
DEG E-value: 3.33e-152 Smaller values mean stronger essential-gene similarity.

Structure confidence

ColabFold pLDDT: 93.17 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) 0.37

Structure A0A0H3GWT7

Pocket Pocket 1

Druggability (FPocket) 0.114

Structure A0A0H3GWT7

Pocket Pocket 12

ColabFold model

P2Rank 0.363 · Pocket 1

FPocket 0.377 · Pocket 5

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 144 / 4744 genomes with a hit

Prevalence 3.0%

Sequence

Primary amino-acid sequence viewer.

MAATFPGVCAVVPAAGFGRRMQTECPKQYLSIGNKTILEHAVAALLADARVQRVVIAVSPGDRRFSQLPLAQHPQITVVDGGAERADSVLAGLQALPEAQWVLVHDAARPCLHQDDLSRLLSLCETSRVGGILAAPVRDTMKRAEPGKTAIAHTVDRNDLWHALTPQFFPRELLVDCLTRALNEGATITDEASALEYCGFHPQLVAGRADNIKVTRPEDLALAEFYLTRSRHQEKA

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 5 GO

Subcellular localization

Localization: Cytoplasmic

Enzyme Commission (EC)

2.7.7.60

Gene Ontology (GO)

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:0003824 Catalysis of a biochemical reaction at physiological temperatures. In biologically catalyzed reactions, the reactants are known as substrates, and the catalysts are naturally occurring macromolecular substances known as enzymes. Enzymes possess specific binding sites for substrates, and are usually composed wholly or largely of protein, but RNA that has catalytic activity (ribozyme) is often also regarded as enzymatic.
GO:0070567 Catalysis of the transfer of a cytidylyl group to an acceptor.
GO:0050518 Catalysis of the reaction: 2-C-methyl-D-erythritol 4-phosphate + CTP = 4-CDP-2-C-methyl-D-erythritol + diphosphate.
GO:0019288 The chemical reactions and pathways resulting in the formation of isopentenyl diphosphate by the mevalonate-independent pathway. 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.

21 records

Show feature table

Start	End	DB	Term	Name
4	235	Gene3D	G3DSA:3.90.550.10	Spore Coat Polysaccharide Biosynthesis Protein SpsA; Chain A
4	235	InterPro	IPR029044	Nucleotide-diphospho-sugar transferases
7	227	Hamap	MF_00108	2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [ispD].
7	227	InterPro	IPR001228	2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase
8	233	PANTHER	PTHR32125	2-C-METHYL-D-ERYTHRITOL 4-PHOSPHATE CYTIDYLYLTRANSFERASE, CHLOROPLASTIC
8	229	Pfam	PF01128	2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase
8	229	InterPro	IPR034683	Cytidylyltransferase IspD/TarI
15	236	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
9	227	NCBIfam	TIGR00453	2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase
9	227	InterPro	IPR001228	2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase
102	109	ProSitePatterns	PS01295	4-diphosphocytidyl-2C-methyl-D-erythritol synthase signature.
102	109	InterPro	IPR018294	4-diphosphocytidyl-2C-methyl-D-erythritol synthase, conserved site
10	14	Phobius	SIGNAL_PEPTIDE_C_REGION	C-terminal region of a signal peptide.
8	227	SUPERFAMILY	SSF53448	Nucleotide-diphospho-sugar transferases
8	227	InterPro	IPR029044	Nucleotide-diphospho-sugar transferases
8	223	CDD	cd02516	CDP-ME_synthetase
8	223	InterPro	IPR034683	Cytidylyltransferase IspD/TarI
1	14	Phobius	SIGNAL_PEPTIDE	Signal peptide region
3	232	FunFam	G3DSA:3.90.550.10:FF:000003	2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase
1	1	Phobius	SIGNAL_PEPTIDE_N_REGION	N-terminal region of a signal peptide.
2	9	Phobius	SIGNAL_PEPTIDE_H_REGION	Hydrophobic region of a signal peptide.

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.

Download VMD script Full viewer

Loading 3D structure...

Drag to rotate — click the view, then scroll to zoom.

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

0.37

Show in viewer

Surrounding area

Pocket 2 P2Rank #2

0.095

Show in viewer

Surrounding area

Pocket 3 P2Rank #3

0.062

Show in viewer

Surrounding area

Pocket 4 P2Rank #4

0.047

Show in viewer

Surrounding area

Residue sets

UniProt: Site:157-157 Positions MEP for the nucleophilic attack

UniProt: Site:20-20 Transition state stabilizer

UniProt: Site:213-213 Positions MEP for the nucleophilic attack

UniProt: Site:27-27 Transition state stabilizer

Binding pockets · P2Rank

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

Pocket 1 P2Rank #1

0.363

Show in viewer

Surrounding area

Pocket 2 P2Rank #2

0.072

Show in viewer

Surrounding area

Pocket 3 P2Rank #3

0.068

Show in viewer

Surrounding area

Pocket 4 P2Rank #4

0.05

Show in viewer

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_A0A0H3GWT7	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold KP13_02514	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 and bioactivity evidence are both available for this target.

Direct evidence 0 same-protein records

Transferred evidence 13 records from similar proteins

Structural ligands 7 0 loaded crystals

Measured bioactivity 6 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

30A PDB via homolog 303.7 Da · LogP 2.38 · TPSA 87.7 Open detail RCSB PDB

CAD PDB via homolog Detail RCSB PDB

CDM PDB via homolog Detail RCSB PDB

DTT PDB via homolog Detail RCSB PDB

H70 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
30A RCSB PDB	2YCM	P69834	303.7 Da LogP 2.38 TPSA 87.7	✓ Ro5	✓ Clean	`c1ccc(cc1)Cc2c(nc3c(cnn3c2O)C(=O)O)Cl`
CAD RCSB PDB	4ZDQ	Q2SWT6	138.0 Da LogP 0.11 TPSA 37.3	✓ Ro5	✓ Clean	`C[As](=O)(C)O`
CDM RCSB PDB	3Q80	P9WKG9	521.3 Da LogP -3.20 TPSA 273.6	3 viol.	✓ Clean	`C[C@](CO)([C@@H](CO[P@](=O)(O)O[P@](=O)(O)OC[C@…`
DTT RCSB PDB	4NAL	P69834	154.3 Da LogP -0.43 TPSA 40.5	✓ Ro5	✓ Clean	`C([C@@H]([C@H](CS)O)O)S`
H70 RCSB PDB	4NAL	P69834	464.8 Da LogP 5.98 TPSA 36.0	1 viol.	✓ Clean	`c1c(cc(c(c1c2c(c(c([nH]2)Br)Br)Br)O)Cl)Cl`
MW5 RCSB PDB	2YC3	P69834	260.7 Da LogP 1.66 TPSA 63.1	✓ Ro5	✓ Clean	`c1ccc(cc1)CC2=C(N=C3NC=NN3C2=O)Cl`
V2V RCSB PDB	6XHQ	Q2G1C0	537.3 Da LogP -4.23 TPSA 293.8	3 viol.	✓ Clean	`C1=CN(C(=O)N=C1N)[C@H]2[C@@H]([C@@H](C(O2)COP(=…`

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
CHEMBL2289489 ChEMBL	P69834	7.46 ~34.7 nM	284.7 Da LogP 2.55 TPSA 74.2	✓ Ro5	✓ Clean	`N#Cc1cnn2c(O)c(Cc3ccccc3)c(Cl)nc12`
CHEMBL2289491 ChEMBL	P69834	6.85 ~141.3 nM	260.7 Da LogP 2.07 TPSA 63.3	✓ Ro5	✓ Clean	`Oc1c(Cc2ccccc2)c(Cl)nc2ncnn12`
CHEMBL1592555 ChEMBL	Q2SWT6	—	273.7 Da LogP 2.63 TPSA 55.6	✓ Ro5	✓ Clean	`Cn1ncc2c(NCc3ccc(Cl)cc3)ncnc21`
CHEMBL3735118 ChEMBL	Q2SWT6	—	308.2 Da LogP 3.28 TPSA 55.6	✓ Ro5	✓ Clean	`Cn1ncc2c(NCc3ccc(Cl)c(Cl)c3)ncnc21`
CHEMBL3735997 ChEMBL	Q2SWT6	—	269.3 Da LogP 1.72 TPSA 75.9	✓ Ro5	✓ Clean	`Cn1ncc2c(NCCc3ccc(O)cc3)ncnc21`
CHEMBL3736022 ChEMBL	Q2SWT6	—	322.2 Da LogP 3.32 TPSA 55.6	✓ Ro5	✓ Clean	`Cn1ncc2c(NCCc3ccc(Cl)cc3Cl)ncnc21`

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
ZINC1577353 ZINC	1.000	273.7 Da LogP 2.63 TPSA 55.6	✓ Ro5	✓ Clean	`Cn1ncc2c(NCc3ccc(Cl)cc3)ncnc21`
ZINC4338812 ZINC	0.792	308.2 Da LogP 3.28 TPSA 55.6	✓ Ro5	✓ Clean	`Cn1ncc2c(NCc3ccc(Cl)cc3Cl)ncnc21`
ZINC3356779 ZINC	0.786	253.3 Da LogP 2.28 TPSA 55.6	✓ Ro5	✓ Clean	`Cc1ccc(CNc2ncnc3c2cnn3C)cc1`
ZINC5730157 ZINC	0.778	264.3 Da LogP 2.21 TPSA 74.2	✓ Ro5	✓ Clean	`Cc1nc2c(C#N)cnn2c(O)c1Cc1ccccc1`
ZINC9532131 ZINC	0.778	287.8 Da LogP 2.67 TPSA 55.6	✓ Ro5	✓ Clean	`Cn1ncc2c(NCCc3ccc(Cl)cc3)ncnc21`
ZINC1577357 ZINC	0.773	253.3 Da LogP 2.02 TPSA 55.6	✓ Ro5	✓ Clean	`Cn1ncc2c(NCCc3ccccc3)ncnc21`
ZINC40493231 ZINC	0.773	255.3 Da LogP 1.68 TPSA 75.9	✓ Ro5	✓ Clean	`Cn1ncc2c(NCc3ccc(O)cc3)ncnc21`
ZINC8584776 ZINC	0.767	257.3 Da LogP 2.11 TPSA 55.6	✓ Ro5	✓ Clean	`Cn1ncc2c(NCc3ccc(F)cc3)ncnc21`
ZINC97020230 ZINC	0.765	366.7 Da LogP 3.43 TPSA 55.6	✓ Ro5	✓ Clean	`Cn1ncc2c(NCCc3cc(Cl)ccc3Br)ncnc21`
ZINC838233 ZINC	0.762	239.3 Da LogP 1.98 TPSA 55.6	✓ Ro5	✓ Clean	`Cn1ncc2c(NCc3ccccc3)ncnc21`
ZINC8216074 ZINC	0.754	477.3 Da LogP -2.95 TPSA 253.3	2 viol.	✓ Clean	`Nc1ccn([C@@H]2O[C@H](CO[P@@](=O)(O)O[P@](=O)(O)…`
ZINC8551188 ZINC	0.754	477.3 Da LogP -2.95 TPSA 253.3	2 viol.	✓ Clean	`Nc1ccn([C@@H]2O[C@H](CO[P@](=O)(O)O[P@](=O)(O)O…`
ZINC12502055 ZINC	0.746	483.2 Da LogP -2.21 TPSA 270.4	2 viol.	✓ Clean	`Nc1ccn([C@@H]2O[C@@H](CO[P@@](=O)(O)O[P@@](=O)(…`
ZINC13431059 ZINC	0.746	483.2 Da LogP -2.21 TPSA 270.4	2 viol.	✓ Clean	`Nc1ccn([C@@H]2O[C@@H](CO[P@@](=O)(O)O[P@@](=O)(…`
ZINC53683723 ZINC	0.746	483.2 Da LogP -2.21 TPSA 270.4	2 viol.	✓ Clean	`Nc1ccn([C@@H]2O[C@@H](CO[P@@](=O)(O)O[P@@](=O)(…`
ZINC82142140 ZINC	0.746	483.2 Da LogP -2.21 TPSA 270.4	2 viol.	✓ Clean	`Nc1ccn([C@@H]2O[C@H](CO[P@@](=O)(O)O[P@@](=O)(O…`
ZINC8582968 ZINC	0.745	273.7 Da LogP 2.63 TPSA 55.6	✓ Ro5	✓ Clean	`Cn1ncc2c(NCc3cccc(Cl)c3)ncnc21`
ZINC9532026 ZINC	0.745	283.3 Da LogP 2.03 TPSA 64.9	✓ Ro5	✓ Clean	`COc1ccc(CCNc2ncnc3c2cnn3C)cc1`
ZINC9532170 ZINC	0.744	240.3 Da LogP 1.37 TPSA 68.5	✓ Ro5	✓ Clean	`Cn1ncc2c(NCc3ccncc3)ncnc21`
ZINC104864216 ZINC	0.741	403.2 Da LogP -2.33 TPSA 223.9	2 viol.	✓ Clean	`Nc1ccn([C@H]2O[C@@H](CO[P@](=O)(O)OP(=O)(O)O)[C…`
ZINC12504412 ZINC	0.741	403.2 Da LogP -2.33 TPSA 223.9	2 viol.	✓ Clean	`Nc1ccn([C@@H]2O[C@@H](CO[P@@](=O)(O)OP(=O)(O)O)…`
ZINC12504413 ZINC	0.741	403.2 Da LogP -2.33 TPSA 223.9	2 viol.	✓ Clean	`Nc1ccn([C@H]2O[C@@H](CO[P@@](=O)(O)OP(=O)(O)O)[…`
ZINC12504414 ZINC	0.741	403.2 Da LogP -2.33 TPSA 223.9	2 viol.	✓ Clean	`Nc1ccn([C@@H]2O[C@H](CO[P@@](=O)(O)OP(=O)(O)O)[…`
ZINC13431045 ZINC	0.741	403.2 Da LogP -2.33 TPSA 223.9	2 viol.	✓ Clean	`Nc1ccn([C@H]2O[C@@H](CO[P@@](=O)(O)OP(=O)(O)O)[…`
ZINC13431047 ZINC	0.741	403.2 Da LogP -2.33 TPSA 223.9	2 viol.	✓ Clean	`Nc1ccn([C@@H]2O[C@@H](CO[P@@](=O)(O)OP(=O)(O)O)…`
ZINC13548733 ZINC	0.741	403.2 Da LogP -2.33 TPSA 223.9	2 viol.	✓ Clean	`Nc1ccn([C@@H]2O[C@H](CO[P@@](=O)(O)OP(=O)(O)O)[…`
ZINC33913782 ZINC	0.741	403.2 Da LogP -2.33 TPSA 223.9	2 viol.	✓ Clean	`Nc1ccn([C@@H]2O[C@H](CO[P@@](=O)(O)OP(=O)(O)O)[…`
ZINC8215624 ZINC	0.741	403.2 Da LogP -2.33 TPSA 223.9	2 viol.	✓ Clean	`Nc1ccn([C@@H]2O[C@H](CO[P@@](=O)(O)OP(=O)(O)O)[…`
ZINC1577358 ZINC	0.733	269.3 Da LogP 1.98 TPSA 64.9	✓ Ro5	✓ Clean	`COc1ccc(CNc2ncnc3c2cnn3C)cc1`
ZINC8216134 ZINC	0.721	446.2 Da LogP -2.35 TPSA 238.9	2 viol.	✓ Clean	`NCCO[P@@](=O)(O)O[P@](=O)(O)OC[C@H]1O[C@@H](n2c…`
ZINC12372230 ZINC	0.714	240.3 Da LogP 1.73 TPSA 63.3	✓ Ro5	✓ Clean	`Cc1nc2ncnn2c(O)c1Cc1ccccc1`
ZINC42240352 ZINC	0.708	259.3 Da LogP 2.08 TPSA 55.6	✓ Ro5	✓ Clean	`Cn1ncc2c(NCCc3ccsc3)ncnc21`
ZINC337881621 ZINC	0.706	307.3 Da LogP 2.44 TPSA 55.6	✓ Ro5	✓ Clean	`Cn1ncc2c(NCCc3ccc(F)c(F)c3F)ncnc21`
ZINC26775664 ZINC	0.702	297.4 Da LogP 2.51 TPSA 64.9	✓ Ro5	✓ Clean	`CCOCc1ccc(CNc2ncnc3c2cnn3C)cc1`
ZINC52100767 ZINC	0.702	317.4 Da LogP 1.38 TPSA 89.8	✓ Ro5	✓ Clean	`Cn1ncc2c(NCc3ccc(S(C)(=O)=O)cc3)ncnc21`
ZINC12876870 ZINC	0.700	297.3 Da LogP 1.75 TPSA 74.1	✓ Ro5	✓ Clean	`Cn1ncc2c(NCc3ccc4c(c3)OCCO4)ncnc21`
ZINC9058175 ZINC	0.700	332.4 Da LogP 0.67 TPSA 115.8	✓ Ro5	✓ Clean	`Cn1ncc2c(NCCc3ccc(S(N)(=O)=O)cc3)ncnc21`
ZINC14167932 ZINC	0.694	271.3 Da LogP 2.42 TPSA 55.6	✓ Ro5	✓ Clean	`Cc1ccc(CNc2ncnc3c2cnn3C)cc1F`
ZINC14206747 ZINC	0.694	299.3 Da LogP 1.99 TPSA 74.1	✓ Ro5	✓ Clean	`COc1ccc(CNc2ncnc3c2cnn3C)cc1OC`
ZINC1718454 ZINC	0.689	308.2 Da LogP 3.28 TPSA 55.6	✓ Ro5	✓ Clean	`Cn1ncc2c(NCc3ccc(Cl)cc3)nc(Cl)nc21`
ZINC12502057 ZINC	0.688	483.2 Da LogP -2.21 TPSA 270.4	2 viol.	✓ Clean	`Nc1ccn([C@H]2O[C@@H](CO[P@@](=O)(O)O[P@@](=O)(O…`
ZINC12502058 ZINC	0.688	483.2 Da LogP -2.21 TPSA 270.4	2 viol.	✓ Clean	`Nc1ccn([C@@H]2O[C@H](CO[P@@](=O)(O)O[P@@](=O)(O…`
ZINC12933201 ZINC	0.688	332.4 Da LogP 0.76 TPSA 115.8	✓ Ro5	✓ Clean	`Cn1ncc2c(NCc3ccc(CS(N)(=O)=O)cc3)ncnc21`
ZINC12941874 ZINC	0.688	318.4 Da LogP 0.62 TPSA 115.8	✓ Ro5	✓ Clean	`Cn1ncc2c(NCc3ccc(S(N)(=O)=O)cc3)ncnc21`
ZINC13431057 ZINC	0.688	483.2 Da LogP -2.21 TPSA 270.4	2 viol.	✓ Clean	`Nc1ccn([C@H]2O[C@@H](CO[P@@](=O)(O)O[P@@](=O)(O…`
ZINC25726736 ZINC	0.688	483.2 Da LogP -2.21 TPSA 270.4	2 viol.	✓ Clean	`Nc1ccn([C@H]2O[C@@H](CO[P@@](=O)(O)O[P@@](=O)(O…`
ZINC3861746 ZINC	0.688	483.2 Da LogP -2.21 TPSA 270.4	2 viol.	✓ Clean	`Nc1ccn([C@@H]2O[C@H](CO[P@](=O)(O)O[P@@](=O)(O)…`
ZINC4354950 ZINC	0.688	349.8 Da LogP 4.39 TPSA 55.6	✓ Ro5	✓ Clean	`Cc1ccc(-n2ncc3c(NCc4ccc(Cl)cc4)ncnc32)cc1`
ZINC52359382 ZINC	0.688	311.4 Da LogP 2.90 TPSA 64.9	✓ Ro5	✓ Clean	`CC(C)OCc1ccc(CNc2ncnc3c2cnn3C)cc1`
ZINC82142138 ZINC	0.688	483.2 Da LogP -2.21 TPSA 270.4	2 viol.	✓ Clean	`Nc1ccn([C@@H]2O[C@H](CO[P@@](=O)(O)O[P@@](=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 A0A0H3GWT7

Chemistry

ChEMBL CHEMBL2289489 ChEMBL CHEMBL2289491 ChEMBL CHEMBL1592555 ChEMBL CHEMBL3735118 ChEMBL CHEMBL3735997 ChEMBL CHEMBL3736022

2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase

Target candidate with partial support; inspect missing evidence before prioritizing.

Main supporting evidence

Risks to review

Evidence gaps

Prioritization evidence

Off-target risk

Essentiality

Structure confidence

Binding-site evidence

Sequence

Functional annotations

Subcellular localization

Enzyme Commission (EC)

Gene Ontology (GO)

Sequence domains and features

3D structure

Binding pockets · P2Rank

Binding pockets · P2Rank

Binding pockets · FPocket

Structural evidence

Ligand evidence

Cross-references

Sequence

Chemistry