Protein target profile
VK055_2379
1-deoxy-D-xylulose 5-phosphate reductoisomerase
Length
400
Pocket druggability
0.956
Metabolic reactions
1
Chokepoint
Yes
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
Metabolic bottleneck
Catalyzes a reaction that is the only producer or consumer of a metabolite in the imported metabolic model.
Central metabolic position
More central than 95.7% of genes in this genome.
No isoenzyme backup detected
Imported GPR rules do not show an alternative enzyme for the catalyzed reaction set.
No similar human protein detected
The current BLAST sequence screen did not find a significant human match, lowering apparent off-target risk.
Review the complete evidence below
Risks to review
Microbiome similarity
203 of 4744 screened genomes (4.3%) have a significant similarity hit. This target also has a predicted binding pocket (FPocket 0.96) — check the ligand evidence before deprioritizing on off-target risk alone.
Best pocket may be a modeling artifact
FPocket selected-pocket score 0.96, but this pocket's geometry is unusually large/diffuse compared to this protein's other predicted pockets — may reflect a low-confidence or disordered model region rather than a real cavity.
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
- 4.3% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.
Essentiality
- Essential (DEG)
- Y
- DEG identity (%)
- 80.808 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
- 97.08 0-100 confidence; >70 supports local structural interpretation.
Binding-site evidence
AlphaFold DB / UniProt modelThe 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
0.956
P2Rank
0.943
ColabFold model
Core conservation
Conserved core gene
Gut microbiome
203 / 4744
genomes with a hit
Cross-references
External database identifiers for this protein, its structures, ligands, and metabolic reactions.
Sequence
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
Pathways
Sequence
Primary amino-acid sequence viewer.
MKQLTVLGSTGSIGCSTLDVVRHNPGRFSVAALVAGKNVDRMVEQCLEFTPRYAVMDDAQSAERLRTRLHEHGSRTEVLSGQQAAAEVAALDEVDQVMAAIVGAAGLVPTLAAIRAGKTVLLANKESLVTCGRLFMEAVQQSGARLLPVDSEHNAIFQSMPETIQQHLGYADLARNGVSSILLTGSGGPFRETAVAELAAMTPDQACRHPNWSMGRKISVDSATMMNKGLEYIEARWLFNASAQQMEVLIHPQSVIHSMVRYQDGSVLAQLGEPDMRTPIAHTMGWPQRLNSGVKPLDFCQLSNLSFSAPDYTRYPCLKLAMDAFDVGQAATTTLNAANEESVAAFLHGDIRFTDIAAVNLAVLDKMDLQEPQGIDDVLVIDAEARAIAHQQLLRLVAQA
Functional annotations
Enzyme classification and Gene Ontology terms linked to this protein.
1 EC
7 GO
Enzyme Commission (EC)
1Gene Ontology (GO)
7- 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:0046872 Binding to a metal ion.
- GO:0070402 Binding to the reduced form, NADPH, of nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions.
- 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 |
|---|---|---|---|---|
| 1 | 399 | PIRSF | PIRSF006205 | Dxp_reductoisomrs |
| 1 | 399 | InterPro | IPR003821 | 1-deoxy-D-xylulose 5-phosphate reductoisomerase |
| 1 | 150 | Gene3D | G3DSA:3.40.50.720 | - |
| 1 | 15 | ProSiteProfiles | PS51257 | Prokaryotic membrane lipoprotein lipid attachment site profile. |
| 2 | 150 | SUPERFAMILY | SSF51735 | NAD(P)-binding Rossmann-fold domains |
| 2 | 150 | InterPro | IPR036291 | NAD(P)-binding domain superfamily |
| 271 | 387 | Pfam | PF13288 | DXP reductoisomerase C-terminal domain |
| 271 | 387 | InterPro | IPR026877 | DXP reductoisomerase 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 |
| 126 | 274 | SUPERFAMILY | SSF55347 | Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain |
| 312 | 397 | Gene3D | G3DSA:1.10.1740.10 | - |
| 312 | 397 | FunFam | G3DSA:1.10.1740.10:FF:000004 | 1-deoxy-D-xylulose 5-phosphate reductoisomerase |
| 1 | 150 | FunFam | G3DSA:3.40.50.720:FF:000045 | 1-deoxy-D-xylulose 5-phosphate reductoisomerase |
| 4 | 392 | Hamap | MF_00183 | 1-deoxy-D-xylulose 5-phosphate reductoisomerase [dxr]. |
| 4 | 392 | InterPro | IPR003821 | 1-deoxy-D-xylulose 5-phosphate reductoisomerase |
| 301 | 393 | SUPERFAMILY | SSF69055 | 1-deoxy-D-xylulose-5-phosphate reductoisomerase, C-terminal domain |
| 301 | 393 | InterPro | IPR036169 | DXP reductoisomerase, C-terminal domain superfamily |
| 2 | 393 | PANTHER | PTHR30525 | 1-DEOXY-D-XYLULOSE 5-PHOSPHATE REDUCTOISOMERASE |
| 2 | 393 | InterPro | IPR003821 | 1-deoxy-D-xylulose 5-phosphate reductoisomerase |
| 4 | 132 | Pfam | PF02670 | 1-deoxy-D-xylulose 5-phosphate reductoisomerase |
| 4 | 132 | InterPro | IPR013512 | 1-deoxy-D-xylulose 5-phosphate reductoisomerase, 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.
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
Selected pocket
-
- Method
- -
- Score
- -
- Visible layer
- -
- Residues
- -
- Pocket properties
- -
Selecting a pocket opens its details and centers the viewer without clearing other active layers. Use Focus this pocket when you want to hide the rest; use Surface for the wider residue environment.
Binding pockets · FPocket
Druggability: high ≥ 0.7 · medium 0.4–0.69 · low < 0.4
Site 1
FPocket #1
0.956
Likely same site as P2Rank 1
4.1 Å
29 shared residues
97% of smaller site
Unusual size
Show in viewer
Surrounding area
Site 2
FPocket #4
0.488
Surrounding area
Site 3
FPocket #22
0.341
Surrounding area
Binding pockets · P2Rank
Probability: high ≥ 0.5 · medium 0.2–0.49 · low < 0.2
Site 1
P2Rank #1
0.943
Likely same site as FPocket 1
4.1 Å
29 shared residues
97% of smaller site
Show in viewer
Surrounding area
Site 2
P2Rank #2
0.028
Surrounding area
Site 3
P2Rank #3
0.003
Surrounding area
Site 4
P2Rank #4
0.001
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 · FPocket
Druggability: high ≥ 0.7 · medium 0.4–0.69 · low < 0.4
Site 1
FPocket #1
0.918
Likely same site as P2Rank 1
7.9 Å
25 shared residues
93% of smaller site
Show in viewer
Surrounding area
Site 2
FPocket #8
0.231
Surrounding area
Binding pockets · P2Rank
Probability: high ≥ 0.5 · medium 0.2–0.49 · low < 0.2
Site 1
P2Rank #1
0.956
Likely same site as FPocket 1
7.9 Å
25 shared residues
93% of smaller site
Show in viewer
Surrounding area
Site 2
P2Rank #2
0.09
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
All structural evidence
Structural evidence
0 + 2Experimental 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
VK055_2379
|
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
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 | 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 | 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 | 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 | 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 | 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 | P45568 | 173.1 Da LogP 0.76 TPSA 70.4 | ✓ Ro5 | ✓ Clean |
c1ccnc(c1)CP(=O)(O)O
|
|
| SYE RCSB PDB | 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.