Length
663
Pocket druggability (P2Rank · AlphaFold DB model)
0.869
Metabolic reactions
5
Chokepoint
No
Direct ligand evidence
0
107 total records
Functional annotation
1 EC
5 GO
Target summary
Promising target candidate with multiple supporting evidence streams.
Automated synthesis of the evidence currently loaded. Review the underlying records before prioritizing this protein.
Main supporting evidence
Risks to review
Human similarity
Top human hit identity: 35.915%. This target also has a predicted binding pocket (P2Rank 0.87) — check the ligand evidence before deprioritizing on off-target risk alone.
Microbiome similarity
569 of 4744 screened genomes (12.0%) have a significant similarity hit. This target also has a predicted binding pocket (P2Rank 0.87) — check the ligand evidence before deprioritizing on off-target risk alone.
Mixed conservation
Core/accessory calls are not fully concordant.
Best pocket may be a modeling artifact
FPocket selected-pocket score 0.71, 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
- Hit
- Human identity (%)
- 35.915 Lower values reduce human off-target concern.
- Human E-value
- 1.68e-16
- Gut microbiome similarity
- 12.0% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.
Essentiality
- Essential (DEG)
- Y
- DEG identity (%)
- 95.475 Higher values support similarity to known essential genes.
- DEG E-value
- 0.0 Smaller values mean stronger essential-gene similarity.
Structure confidence
- ColabFold pLDDT
- 98.28 0-100 confidence; >70 supports local structural interpretation.
Binding-site evidence
AlphaFold DB / UniProt modelP2Rank'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)
0.869
Druggability (FPocket)
0.71
ColabFold model
Core conservation
Accessory gene
Gut microbiome
569 / 4744
genomes with a hit
Sequence
Primary amino-acid sequence viewer.
MSSRKELANAIRALSMDAVQKAKSGHPGAPMGMADIAEVLWRDFLNHNPNNPAWADRDRFVLSNGHGSMLIYSLLHLTGYDLPIEELKNFRQLHSKTPGHPEVGYTAGVETTTGPLGQGIANAVGMAIAEKTLAAQFNRPGHDIVDHYTYAFMGDGCMMEGISHEVCSLAGTLKLGKLVAFYDDNGISIDGHVEGWFTDDTAKRFEAYGWHVVRGVDGHDADAIKRAVEEARAVTDKPSLLMCKTIIGFGSPNKAGTHDSHGAPLGDAEIALTREALGWKHAPFDIPSDIYAQWDAKEAGQAKEAAWNEKFAAYAKAFPQEAAEFTRRMKGEMPSDFDAKANEFIAKLQANPAKIASRKASQNAIEAFGPLLPEFLGGSADLAPSNLTLWSGSKPINEDAAGNYIHYGVREFGMTAIANGIALHGGFLPYTSTFLMFVEYARNAVRMAALMKQRQVMVYTHDSIGLGEDGPTHQPVEQVASLRVTPNMSTWRPCDQVESAIAWKYGVERQDGPTALILSRQNLAQQERTAEQLANVARGGYVLKDCAGQPELIFIATGSEVELAVAAWDKLTAEGVKARVVSMPSTDAFDKQDAAYRESVLPKDVTARVAVEAGIADYWFKYVGLNGAIVGMTSFGESAPAEQLFEEFGFTVDNVVAKAKALL
Functional annotations
Enzyme classification and Gene Ontology terms linked to this protein.
1 EC
5 GO
Subcellular localization
- Localization
- Cytoplasmic
Enzyme Commission (EC)
1Gene Ontology (GO)
5- 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:0004802 Catalysis of the reversible transfer of a 2-carbon ketol group (CH2OH-CO-) from a ketose phosphate donor to an aldose phosphate acceptor.
- GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
- GO:0046872 Binding to a metal ion.
- GO:0009052 The branch of the pentose-phosphate shunt which does not involve oxidation reactions. It comprises a series of sugar phosphate interconversions, starting with ribulose 5-P and producing fructose 6-P and glyceraldehyde 3-P.
Sequence domains and features
Domain and signature matches imported from InterPro and related databases.
32 records
Show feature table
| Start | End | DB | Term | Name |
|---|---|---|---|---|
| 5 | 331 | SUPERFAMILY | SSF52518 | Thiamin diphosphate-binding fold (THDP-binding) |
| 5 | 331 | InterPro | IPR029061 | Thiamin diphosphate-binding fold |
| 12 | 32 | ProSitePatterns | PS00801 | Transketolase signature 1. |
| 12 | 32 | InterPro | IPR005474 | Transketolase, N-terminal |
| 354 | 524 | Pfam | PF02779 | Transketolase, pyrimidine binding domain |
| 354 | 524 | InterPro | IPR005475 | Transketolase-like, pyrimidine-binding domain |
| 1 | 662 | PANTHER | PTHR43522 | TRANSKETOLASE |
| 1 | 662 | InterPro | IPR033247 | Transketolase family |
| 5 | 662 | NCBIfam | TIGR00232 | transketolase |
| 5 | 662 | InterPro | IPR005478 | Transketolase, bacterial-like |
| 1 | 326 | Gene3D | G3DSA:3.40.50.970 | - |
| 538 | 663 | FunFam | G3DSA:3.40.50.920:FF:000003 | Transketolase |
| 9 | 274 | CDD | cd02012 | TPP_TK |
| 9 | 274 | InterPro | IPR005474 | Transketolase, N-terminal |
| 355 | 525 | SMART | SM00861 | Transket_pyr_3 |
| 355 | 525 | InterPro | IPR005475 | Transketolase-like, pyrimidine-binding domain |
| 538 | 663 | Gene3D | G3DSA:3.40.50.920 | - |
| 538 | 663 | InterPro | IPR009014 | Transketolase C-terminal/Pyruvate-ferredoxin oxidoreductase domain II |
| 327 | 537 | Gene3D | G3DSA:3.40.50.970 | - |
| 327 | 537 | FunFam | G3DSA:3.40.50.970:FF:000003 | Transketolase |
| 336 | 526 | SUPERFAMILY | SSF52518 | Thiamin diphosphate-binding fold (THDP-binding) |
| 336 | 526 | InterPro | IPR029061 | Thiamin diphosphate-binding fold |
| 467 | 483 | ProSitePatterns | PS00802 | Transketolase signature 2. |
| 467 | 483 | InterPro | IPR020826 | Transketolase binding site |
| 1 | 326 | FunFam | G3DSA:3.40.50.970:FF:000004 | Transketolase |
| 540 | 655 | Pfam | PF02780 | Transketolase, C-terminal domain |
| 540 | 655 | InterPro | IPR033248 | Transketolase, C-terminal domain |
| 4 | 334 | Pfam | PF00456 | Transketolase, thiamine diphosphate binding domain |
| 4 | 334 | InterPro | IPR005474 | Transketolase, N-terminal |
| 359 | 520 | CDD | cd07033 | TPP_PYR_DXS_TK_like |
| 533 | 663 | SUPERFAMILY | SSF52922 | TK C-terminal domain-like |
| 533 | 663 | InterPro | IPR009014 | Transketolase C-terminal/Pyruvate-ferredoxin oxidoreductase domain II |
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 · P2Rank
Druggability (P2Rank): high ≥ 0.5 · medium 0.2–0.49 · low < 0.2
Pocket 1
P2Rank #1
0.869
Likely same site as FPocket 2
2.3 Å
17 shared residues
94% of smaller site
Show in viewer
Surrounding area
Pocket 2
P2Rank #2
0.161
Surrounding area
Pocket 3
P2Rank #3
0.101
Surrounding area
Pocket 4
P2Rank #4
0.074
Surrounding area
Pocket 5
P2Rank #5
0.046
Surrounding area
Binding pockets · FPocket
Druggability (FPocket): high ≥ 0.7 · medium 0.4–0.69 · low < 0.4
Pocket 1
FPocket #2
0.71
Unusual size
Likely same site as P2Rank 1
2.3 Å
17 shared residues
94% of smaller site
Show in viewer
Surrounding area
Residue sets
UniProt: Active site:411-411
Proton donor
UniProt: Binding site:114-116
UniProt: Binding site:155-155
UniProt: Binding site:156-156
UniProt: Binding site:185-185
UniProt: Binding site:187-187
UniProt: Binding site:26-26
UniProt: Binding site:261-261
UniProt: Binding site:358-358
UniProt: Binding site:385-385
UniProt: Binding site:437-437
UniProt: Binding site:461-461
UniProt: Binding site:469-469
UniProt: Binding site:473-473
UniProt: Binding site:520-520
UniProt: Binding site:66-66
UniProt: Site:26-26
Important for catalytic activity
UniProt: Site:261-261
Important for catalytic activity
Binding pockets · P2Rank
Druggability (P2Rank): high ≥ 0.5 · medium 0.2–0.49 · low < 0.2
Pocket 1
P2Rank #1
0.825
Surrounding area
Pocket 2
P2Rank #2
0.114
Surrounding area
Pocket 3
P2Rank #3
0.098
Surrounding area
Pocket 4
P2Rank #4
0.097
Surrounding area
Pocket 5
P2Rank #5
0.043
Likely same site as FPocket 3
3.0 Å
10 shared residues
100% of smaller site
Show in viewer
Surrounding area
Binding pockets · FPocket
Druggability (FPocket): high ≥ 0.7 · medium 0.4–0.69 · low < 0.4
Pocket 1
FPocket #3
0.358
Likely same site as P2Rank 5
3.0 Å
10 shared residues
100% of smaller site
Show in viewer
Surrounding area
Residue sets
UniProt: Active site:411-411
Proton donor
UniProt: Binding site:114-116
UniProt: Binding site:155-155
UniProt: Binding site:156-156
UniProt: Binding site:185-185
UniProt: Binding site:187-187
UniProt: Binding site:26-26
UniProt: Binding site:261-261
UniProt: Binding site:358-358
UniProt: Binding site:385-385
UniProt: Binding site:437-437
UniProt: Binding site:461-461
UniProt: Binding site:469-469
UniProt: Binding site:473-473
UniProt: Binding site:520-520
UniProt: Binding site:66-66
UniProt: Site:26-26
Important for catalytic activity
UniProt: Site:261-261
Important for catalytic activity
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_A0A0H3GY70
|
AlphaFold DB | — | — | full sequence | — | Viewing |
|
ColabFold
VK055_4125
|
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.
107 records
Chemistry signal
Structural and bioactivity evidence are both available for this target.
Direct evidence
0
same-protein records
Transferred evidence
57
records from similar proteins
Structural ligands
28
0 loaded crystals
Measured bioactivity
29
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 |
|---|---|---|---|---|---|---|
| 1U0 RCSB PDB | P29401 | 483.4 Da LogP 1.12 TPSA 205.5 | 1 viol. | ✓ Clean |
Cc1c(sc(c1Cc2cnc(nc2N)C)[C@@H](CO)O)CCOP(=O)(O)…
|
|
| 1Y7 RCSB PDB | P29401 | 292.2 Da LogP -4.11 TPSA 188.1 | 1 viol. | ✓ Clean |
C([C@@H]([C@H]([C@@H]([C@@H]([C@@H](COP(=O)(O)O…
|
|
| 5SP RCSB PDB | P27302 | 230.1 Da LogP -2.62 TPSA 144.5 | ✓ Ro5 | ✓ Clean |
C([C@H]([C@@H](C(=O)CO)O)O)OP(=O)(O)O
|
|
| 8EF RCSB PDB | P34736 | 426.3 Da LogP 1.37 TPSA 168.3 | ✓ Ro5 | ✓ Clean |
Cc1ncc(c(n1)N)CN2CS[C@H](C2=C)CCOP(=O)(O)OP(=O)…
|
|
| 8EL RCSB PDB | P34736 | 426.3 Da LogP 1.72 TPSA 168.3 | ✓ Ro5 | ✓ Clean |
Cc1ncc(c(n1)N)CN2CSC(=C2C)CCOP(=O)(O)OP(=O)(O)O
|
|
| 8EO RCSB PDB | P34736 | 427.3 Da LogP 1.03 TPSA 168.1 | ✓ Ro5 | ✓ Clean |
Cc1ncc(c(n1)N)C[N+]2=C([C@@H](SC2)CCOP(=O)(O)OP…
|
|
| 8FL RCSB PDB | P34736 | 442.3 Da LogP 1.04 TPSA 188.6 | ✓ Ro5 | ✓ Clean |
Cc1ncc(c(n1)N)CN2[C@@H](SC(=C2C)CCOP(=O)(O)OP(=…
|
|
| 8GF RCSB PDB | P34736 | 109.1 Da LogP 0.37 TPSA 51.8 | ✓ Ro5 | ✓ Clean |
Cc1nccc(n1)N
|
|
| 8ML RCSB PDB | P34736 | 686.5 Da LogP -2.34 TPSA 336.2 | 3 viol. | ✓ Clean |
Cc1ncc(c(n1)N)CN2C(SC(C2=C)CCOP(=O)(O)OP(=O)(O)…
|
|
| 8N9 RCSB PDB | P34736 | 484.4 Da LogP 1.48 TPSA 208.8 | 2 viol. | ✓ Clean |
Cc1ncc(c(n1)N)CN\2C(=C(S/C2=C(\CO)/O)CCOP(=O)(O…
|
|
| BTB RCSB PDB | A0A6L7H165 | 209.2 Da LogP -3.01 TPSA 104.4 | ✓ Ro5 | ✓ Clean |
C(CO)N(CCO)C(CO)(CO)CO
|
|
| DX5 RCSB PDB | P29401 | 232.1 Da LogP -2.83 TPSA 147.7 | 1 viol. | ✓ Clean |
C([C@@H]([C@H]([C@@H](COP(=O)(O)O)O)O)O)O
|
|
| E4P RCSB PDB | P34736 | 200.1 Da LogP -1.98 TPSA 124.3 | ✓ Ro5 | ✓ Clean |
C([C@H]([C@H](C=O)O)O)OP(=O)(O)O
|
|
| F6R RCSB PDB | P34736 | 260.1 Da LogP -3.26 TPSA 164.8 | 1 viol. | ✓ Clean |
C([C@H]([C@H]([C@@H](C(=O)CO)O)O)O)OP(=O)(O)O
|
|
| HSX RCSB PDB | P34736 | 230.1 Da LogP -2.47 TPSA 136.7 | ✓ Ro5 | ✓ Clean |
C([C@@H]1[C@H]([C@H]([C@H](O1)O)O)O)OP(=O)(O)O
|
|
| I22 RCSB PDB | P34736 | 290.2 Da LogP -3.90 TPSA 185.0 | 1 viol. | ✓ Clean |
C([C@H]([C@H]([C@H]([C@@H](C(=O)CO)O)O)O)O)OP(=…
|
|
| M6T RCSB PDB | P23254 | 438.3 Da LogP 0.52 TPSA 171.8 | ✓ Ro5 | ✓ Clean |
Cc1c(c(nc(n1)C)N)C[n+]2csc(c2C)CCO[P@](=O)(O)O[…
|
|
| N1T RCSB PDB | P23254 | 423.3 Da LogP 0.81 TPSA 158.9 | ✓ Ro5 | ✓ Clean |
Cc1ccc(c(n1)N)C[n+]2csc(c2C)CCO[P@](=O)(O)O[P@@…
|
|
| N3T RCSB PDB | P23254 | 423.3 Da LogP 0.81 TPSA 158.9 | ✓ Ro5 | ✓ Clean |
Cc1cc(c(cn1)C[n+]2csc(c2C)CCO[P@](=O)(O)O[P@@](…
|
|
| NDQ RCSB PDB | P27302 | 441.3 Da LogP 0.54 TPSA 178.2 | ✓ Ro5 | ✓ Clean |
Cc1c(sc[n+]1Cc2cnc(nc2N)OC)CCOP(=O)(O)OP(=O)(O)O
|
|
| P23 RCSB PDB | P34736 | 220.1 Da LogP 0.62 TPSA 113.3 | ✓ Ro5 | ✓ Clean |
CCCO[P@@](=O)(O)OP(=O)(O)O
|
|
| PG5 RCSB PDB | A0A6L7H165 | 178.2 Da LogP 0.31 TPSA 36.9 | ✓ Ro5 | ✓ Clean |
COCCOCCOCCOC
|
|
| POP RCSB PDB | P34736 | 176.0 Da LogP -2.08 TPSA 129.9 | ✓ Ro5 | ✓ Clean |
O[P@@](=O)([O-])O[P@@](=O)(O)[O-]
|
|
| R5P RCSB PDB | Q0P7Y3 | 230.1 Da LogP -2.62 TPSA 144.5 | ✓ Ro5 | ✓ Clean |
C(C(C(C(C=O)O)O)O)OP(=O)(O)O
|
|
| RP5 RCSB PDB | Q0P7Y3 | 230.1 Da LogP -2.47 TPSA 136.7 | ✓ Ro5 | ✓ Clean |
C([C@@H]1[C@H]([C@H]([C@@H](O1)O)O)O)OP(=O)(O)O
|
|
| S6P RCSB PDB | P29401 | 262.2 Da LogP -3.47 TPSA 167.9 | 1 viol. | ✓ Clean |
C([C@@H]([C@H]([C@@H]([C@@H](COP(=O)(O)O)O)O)O)…
|
|
| T5X RCSB PDB | P27302 | 655.4 Da LogP -2.15 TPSA 316.6 | 3 viol. | ✓ Clean |
Cc1c(sc([n+]1Cc2cnc(nc2N)C)[C@](CO)([C@H]([C@@H…
|
|
| T6F RCSB PDB | P27302 | 685.5 Da LogP -2.79 TPSA 336.9 | 3 viol. | ✓ Clean |
Cc1c(sc([n+]1Cc2cnc(nc2N)C)[C@](CO)([C@H]([C@@H…
|
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 |
|---|---|---|---|---|---|---|
| CHEMBL403691 ChEMBL | P29401 | 8.33 ~4.7 nM | 306.4 Da LogP 1.78 TPSA 69.1 | ✓ Ro5 | ✓ Clean |
CC(=O)OCCc1sc[n+](Cc2ccc(C)nc2N)c1C
|
| CHEMBL255603 ChEMBL | P29401 | 8.15 ~7.1 nM | 250.3 Da LogP 0.90 TPSA 63.0 | ✓ Ro5 | ✓ Clean |
Cc1c(CCO)sc[n+]1Cc1ccc(N)nc1
|
| CHEMBL271044 ChEMBL | P29401 | 8.08 ~8.3 nM | 278.4 Da LogP 1.52 TPSA 63.0 | ✓ Ro5 | ✓ Clean |
Cc1cc(C)c(C[n+]2csc(CCO)c2C)c(N)n1
|
| CHEMBL256627 ChEMBL | P29401 | 8.06 ~8.7 nM | 278.4 Da LogP 1.47 TPSA 63.0 | ✓ Ro5 | ✓ Clean |
CCc1ccc(C[n+]2csc(CCO)c2C)c(N)n1
|
| CHEMBL270613 ChEMBL | P29401 | 8.05 ~8.9 nM | 284.8 Da LogP 1.56 TPSA 63.0 | ✓ Ro5 | ✓ Clean |
Cc1c(CCO)sc[n+]1Cc1ccc(Cl)nc1N
|
| CHEMBL401948 ChEMBL | P29401 | 8.05 ~8.9 nM | 320.2 Da LogP -1.44 TPSA 63.0 | ✓ Ro5 | ✓ Clean |
Cc1c(CCO)sc[n+]1Cc1ccc(Cl)nc1N.[Cl-]
|
| 0YN ChEMBL | P29401 | 7.92 ~12.0 nM | 263.4 Da LogP 1.86 TPSA 72.0 | ✓ Ro5 | ✓ Clean |
Cc1c(csc1CCO)Cc2cnc(nc2N)C
|
| TZD ChEMBL | P29401 | 7.80 ~15.8 nM | 440.3 Da LogP 0.72 TPSA 187.1 | ✓ Ro5 | ✓ Clean |
Cc1ncc(c(n1)N)CN2C(=C(SC2=O)CCO[P@@](=O)(O)OP(=…
|
| CHEMBL252086 ChEMBL | P29401 | 7.75 ~17.8 nM | 299.8 Da LogP -1.78 TPSA 63.0 | ✓ Ro5 | ✓ Clean |
Cc1ccc(C[n+]2csc(CCO)c2C)c(N)n1.[Cl-]
|
| CHEMBL403212 ChEMBL | P29401 | 7.68 ~20.9 nM | 292.4 Da LogP 1.78 TPSA 63.0 | ✓ Ro5 | ✓ Clean |
CCc1sc(CCO)c(C)[n+]1Cc1ccc(C)nc1N
|
| CHEMBL401817 ChEMBL | P29401 | 7.66 ~21.9 nM | 424.3 Da LogP 1.45 TPSA 156.1 | ✓ Ro5 | ✓ Clean |
Cc1ccc(C[n+]2csc(CCOP(=O)(O)OP(=O)(O)O)c2C)c(N)…
|
| CHEMBL256831 ChEMBL | P29401 | 7.64 ~22.9 nM | 307.4 Da LogP 0.86 TPSA 92.1 | ✓ Ro5 | ✓ Clean |
CC(=O)Nc1ccc(C[n+]2csc(CCO)c2C)c(N)n1
|
| CHEMBL402329 ChEMBL | P29401 | 7.60 ~25.1 nM | 278.4 Da LogP 1.52 TPSA 63.0 | ✓ Ro5 | ✓ Clean |
Cc1ccc(C[n+]2c(C)sc(CCO)c2C)c(N)n1
|
| CHEMBL402566 ChEMBL | P29401 | 7.60 ~25.1 nM | 280.4 Da LogP 0.40 TPSA 83.2 | ✓ Ro5 | ✓ Clean |
Cc1ccc(C[n+]2csc(CCO)c2CO)c(N)n1
|
| CHEMBL255340 ChEMBL | P29401 | 7.57 ~26.9 nM | 280.4 Da LogP 0.70 TPSA 83.2 | ✓ Ro5 | ✓ Clean |
Cc1ccc(C[n+]2csc([C@@H](O)CO)c2C)c(N)n1
|
| CHEMBL252441 ChEMBL | P29401 | 7.55 ~28.2 nM | 313.9 Da LogP -1.47 TPSA 63.0 | ✓ Ro5 | ✓ Clean |
Cc1ccc(C[n+]2c(C)sc(CCO)c2C)c(N)n1.[Cl-]
|
| CHEMBL258077 ChEMBL | P29401 | 7.55 ~28.2 nM | 280.4 Da LogP 0.70 TPSA 83.2 | ✓ Ro5 | ✓ Clean |
Cc1ccc(C[n+]2csc([C@H](O)CO)c2C)c(N)n1
|
| CHEMBL256454 ChEMBL | P29401 | 7.54 ~28.8 nM | 250.3 Da LogP 0.90 TPSA 63.0 | ✓ Ro5 | ✓ Clean |
Cc1ccc(C[n+]2csc(CCO)c2)c(N)n1
|
| CHEMBL255339 ChEMBL | P29401 | 7.52 ~30.2 nM | 308.4 Da LogP 1.27 TPSA 83.2 | ✓ Ro5 | ✓ Clean |
Cc1ccc(C[n+]2c(C(C)O)sc(CCO)c2C)c(N)n1
|
| CHEMBL270632 ChEMBL | P29401 | 7.44 ~36.3 nM | 264.4 Da LogP 1.21 TPSA 63.0 | ✓ Ro5 | ✓ Clean |
Cc1ccc(C[n+]2cc(CCO)sc2C)c(N)n1
|
| CHEMBL403365 ChEMBL | P29401 | 7.44 ~36.3 nM | 250.3 Da LogP 0.90 TPSA 63.0 | ✓ Ro5 | ✓ Clean |
Cc1c(CCO)sc[n+]1Cc1cccnc1N
|
| CHEMBL255541 ChEMBL | P29401 | 7.40 ~39.8 nM | 278.4 Da LogP 1.47 TPSA 63.0 | ✓ Ro5 | ✓ Clean |
CCc1c(CCO)sc[n+]1Cc1ccc(C)nc1N
|
| CHEMBL255542 ChEMBL | P29401 | 7.28 ~52.5 nM | 280.4 Da LogP 0.70 TPSA 83.2 | ✓ Ro5 | ✓ Clean |
Cc1ccc(C[n+]2csc(C(O)CO)c2C)c(N)n1
|
| CHEMBL429246 ChEMBL | P29401 | 7.24 ~57.5 nM | 275.4 Da LogP 0.78 TPSA 86.8 | ✓ Ro5 | ✓ Clean |
Cc1c(CCO)sc[n+]1Cc1ccc(C#N)nc1N
|
| CHEMBL271521 ChEMBL | P29401 | 7.19 ~64.6 nM | 250.3 Da LogP 0.90 TPSA 63.0 | ✓ Ro5 | ✓ Clean |
Cc1c(CCO)sc[n+]1Cc1cnccc1N
|
| CHEMBL270168 ChEMBL | P29401 | 6.98 ~104.7 nM | 318.3 Da LogP 1.92 TPSA 63.0 | ✓ Ro5 | ✓ Clean |
Cc1c(CCO)sc[n+]1Cc1ccc(C(F)(F)F)nc1N
|
| CHEMBL252637 ChEMBL | P29401 | 6.96 ~109.6 nM | 285.8 Da LogP -2.09 TPSA 63.0 | ✓ Ro5 | ✓ Clean |
Cc1c(CCO)sc[n+]1Cc1cccnc1N.[Cl-]
|
| CHEMBL270384 ChEMBL | P29401 | 6.96 ~109.6 nM | 376.2 Da LogP 1.51 TPSA 63.0 | ✓ Ro5 | ✓ Clean |
Cc1c(CCO)sc[n+]1Cc1cc(I)cnc1N
|
| CHEMBL430409 ChEMBL | P29401 | 6.77 ~169.8 nM | 423.3 Da LogP 1.56 TPSA 148.7 | ✓ Ro5 | ✓ Clean |
Cc1ncc(C[n+]2csc(CCOP(C)(=O)OP(=O)(O)O)c2C)c(N)…
|
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 |
|---|---|---|---|---|---|
| ZINC12504154 ZINC | 1.000 | 230.1 Da LogP -2.47 TPSA 136.7 | ✓ Ro5 | ✓ Clean |
O=P(O)(O)OC[C@H]1O[C@H](O)[C@@H](O)[C@@H]1O
|
| ZINC1529626 ZINC | 1.000 | 230.1 Da LogP -2.62 TPSA 144.5 | ✓ Ro5 | ✓ Clean |
O=C(CO)[C@H](O)[C@@H](O)COP(=O)(O)O
|
| ZINC1532546 ZINC | 1.000 | 230.1 Da LogP -2.47 TPSA 136.7 | ✓ Ro5 | ✓ Clean |
O=P(O)(O)OC[C@@H]1O[C@H](O)[C@@H](O)[C@H]1O
|
| ZINC1532567 ZINC | 1.000 | 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 | 1.000 | 230.1 Da LogP -2.62 TPSA 144.5 | ✓ Ro5 | ✓ Clean |
O=C(CO)[C@@H](O)[C@@H](O)COP(=O)(O)O
|
| ZINC1615342 ZINC | 1.000 | 209.2 Da LogP -3.01 TPSA 104.4 | ✓ Ro5 | ✓ Clean |
OCCN(CCO)C(CO)(CO)CO
|
| ZINC1692489 ZINC | 1.000 | 222.3 Da LogP 0.33 TPSA 46.2 | ✓ Ro5 | ✓ Clean |
COCCOCCOCCOCCOC
|
| ZINC30320708 ZINC | 1.000 | 230.1 Da LogP -2.62 TPSA 144.5 | ✓ Ro5 | ✓ Clean |
O=C(CO)[C@@H](O)[C@H](O)COP(=O)(O)O
|
| ZINC4096190 ZINC | 1.000 | 230.1 Da LogP -2.47 TPSA 136.7 | ✓ Ro5 | ✓ Clean |
O=P(O)(O)OC[C@H]1O[C@H](O)[C@H](O)[C@@H]1O
|
| ZINC4228241 ZINC | 1.000 | 230.1 Da LogP -2.47 TPSA 136.7 | ✓ Ro5 | ✓ Clean |
O=P(O)(O)OC[C@H]1O[C@@H](O)[C@H](O)[C@@H]1O
|
| ZINC4521831 ZINC | 1.000 | 230.1 Da LogP -2.47 TPSA 136.7 | ✓ Ro5 | ✓ Clean |
O=P(O)(O)OC[C@H]1O[C@@H](O)[C@@H](O)[C@@H]1O
|
| ZINC4530388 ZINC | 1.000 | 266.3 Da LogP 0.35 TPSA 55.4 | ✓ Ro5 | ✓ Clean |
COCCOCCOCCOCCOCCOC
|
| ZINC5701172 ZINC | 1.000 | 310.4 Da LogP 0.36 TPSA 64.6 | ✓ Ro5 | ✓ Clean |
COCCOCCOCCOCCOCCOCCOC
|
| ZINC5997861 ZINC | 1.000 | 398.5 Da LogP 0.40 TPSA 83.1 | ✓ Ro5 | ✓ Clean |
COCCOCCOCCOCCOCCOCCOCCOCCOC
|
| ZINC100351935 ZINC | 0.962 | 260.1 Da LogP -3.10 TPSA 156.9 | 1 viol. | ✓ Clean |
O=P(O)(O)OC[C@@H]1O[C@H](O)[C@H](O)[C@H](O)[C@@…
|
| ZINC1529564 ZINC | 0.962 | 260.1 Da LogP -3.10 TPSA 156.9 | 1 viol. | ✓ Clean |
O=P(O)(O)OC[C@@H]1O[C@@H](O)[C@H](O)[C@H](O)[C@…
|
| ZINC1532533 ZINC | 0.962 | 260.1 Da LogP -3.10 TPSA 156.9 | 1 viol. | ✓ Clean |
O=P(O)(O)OC[C@@H]1O[C@H](O)[C@@H](O)[C@H](O)[C@…
|
| ZINC1532857 ZINC | 0.962 | 260.1 Da LogP -3.10 TPSA 156.9 | 1 viol. | ✓ Clean |
O=P(O)(O)OC[C@@H]1O[C@@H](O)[C@@H](O)[C@H](O)[C…
|
| ZINC3581460 ZINC | 0.962 | 260.1 Da LogP -3.10 TPSA 156.9 | 1 viol. | ✓ Clean |
O=P(O)(O)OC[C@@H]1O[C@@H](O)[C@@H](O)[C@H](O)[C…
|
| ZINC38276879 ZINC | 0.962 | 260.1 Da LogP -3.10 TPSA 156.9 | 1 viol. | ✓ Clean |
O=P(O)(O)OC[C@H]1O[C@@H](O)[C@@H](O)[C@H](O)[C@…
|
| ZINC38276880 ZINC | 0.962 | 260.1 Da LogP -3.10 TPSA 156.9 | 1 viol. | ✓ Clean |
O=P(O)(O)OC[C@H]1O[C@H](O)[C@@H](O)[C@H](O)[C@H…
|
| ZINC3869397 ZINC | 0.962 | 260.1 Da LogP -3.10 TPSA 156.9 | 1 viol. | ✓ Clean |
O=P(O)(O)OC[C@H]1O[C@@H](O)[C@@H](O)[C@@H](O)[C…
|
| ZINC3875374 ZINC | 0.962 | 260.1 Da LogP -3.10 TPSA 156.9 | 1 viol. | ✓ Clean |
O=P(O)(O)OC[C@H]1O[C@@H](O)[C@H](O)[C@@H](O)[C@…
|
| ZINC3875375 ZINC | 0.962 | 260.1 Da LogP -3.10 TPSA 156.9 | 1 viol. | ✓ Clean |
O=P(O)(O)OC[C@H]1O[C@H](O)[C@H](O)[C@@H](O)[C@@…
|
| ZINC4095545 ZINC | 0.962 | 260.1 Da LogP -3.10 TPSA 156.9 | 1 viol. | ✓ Clean |
O=P(O)(O)OC[C@H]1O[C@@H](O)[C@H](O)[C@@H](O)[C@…
|
| ZINC4095546 ZINC | 0.962 | 260.1 Da LogP -3.10 TPSA 156.9 | 1 viol. | ✓ Clean |
O=P(O)(O)OC[C@H]1O[C@H](O)[C@H](O)[C@@H](O)[C@H…
|
| ZINC4096188 ZINC | 0.962 | 260.1 Da LogP -3.10 TPSA 156.9 | 1 viol. | ✓ Clean |
O=P(O)(O)OC[C@H]1O[C@H](O)[C@@H](O)[C@@H](O)[C@…
|
| ZINC8551507 ZINC | 0.962 | 260.1 Da LogP -3.10 TPSA 156.9 | 1 viol. | ✓ Clean |
O=P(O)(O)OC[C@@H]1O[C@H](O)[C@@H](O)[C@H](O)[C@…
|
| ZINC8215517 ZINC | 0.810 | 425.3 Da LogP 0.84 TPSA 169.0 | ✓ Ro5 | ✓ Clean |
Cc1ncc(C[n+]2csc(CCO[P@@](=O)(O)OP(=O)(O)O)c2C)…
|
| ZINC100065511 ZINC | 0.793 | 260.1 Da LogP -3.26 TPSA 164.8 | 1 viol. | ✓ Clean |
O=C(CO)[C@H](O)[C@H](O)[C@@H](O)COP(=O)(O)O
|
| ZINC100085043 ZINC | 0.793 | 260.1 Da LogP -3.26 TPSA 164.8 | 1 viol. | ✓ Clean |
O=C(CO)[C@H](O)[C@H](O)[C@H](O)COP(=O)(O)O
|
| ZINC104869937 ZINC | 0.793 | 260.1 Da LogP -3.26 TPSA 164.8 | 1 viol. | ✓ Clean |
O=C(CO)[C@H](O)[C@@H](O)[C@@H](O)COP(=O)(O)O
|
| ZINC13537943 ZINC | 0.793 | 260.1 Da LogP -3.26 TPSA 164.8 | 1 viol. | ✓ Clean |
O=C(CO)[C@H](O)[C@@H](O)[C@H](O)COP(=O)(O)O
|
| ZINC85994845 ZINC | 0.793 | 260.1 Da LogP -3.26 TPSA 164.8 | 1 viol. | ✓ Clean |
O=C(CO)[C@@H](O)[C@H](O)[C@H](O)COP(=O)(O)O
|
| ZINC5132038 ZINC | 0.767 | 290.2 Da LogP -3.90 TPSA 185.0 | 1 viol. | ✓ Clean |
O=C(CO)[C@@H](O)[C@H](O)[C@H](O)[C@H](O)COP(=O)…
|
| ZINC13516910 ZINC | 0.759 | 244.1 Da LogP -2.42 TPSA 136.7 | ✓ Ro5 | ✓ Clean |
O=P(O)(O)OC[C@@H]1O[C@@H](CO)[C@@H](O)[C@H]1O
|
| ZINC2562340 ZINC | 0.759 | 244.1 Da LogP -2.42 TPSA 136.7 | ✓ Ro5 | ✓ Clean |
O=P(O)(O)OC[C@@H]1O[C@@H](CO)[C@H](O)[C@H]1O
|
| ZINC4097102 ZINC | 0.742 | 259.2 Da LogP -3.14 TPSA 162.7 | 1 viol. | ✓ Clean |
N[C@H]1[C@H](O)O[C@H](COP(=O)(O)O)[C@@H](O)[C@@…
|
| ZINC4097103 ZINC | 0.742 | 259.2 Da LogP -3.14 TPSA 162.7 | 1 viol. | ✓ Clean |
N[C@H]1[C@@H](O)O[C@H](COP(=O)(O)O)[C@@H](O)[C@…
|
| ZINC34764844 ZINC | 0.733 | 206.3 Da LogP 1.09 TPSA 36.9 | ✓ Ro5 | ✓ Clean |
CCCOCCOCCOCCOC
|
| ZINC3870277 ZINC | 0.724 | 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
|
| ZINC1532839 ZINC | 0.700 | 345.3 Da LogP 0.72 TPSA 122.4 | ✓ Ro5 | ✓ Clean |
Cc1ncc(C[n+]2csc(CCOP(=O)(O)O)c2C)c(N)n1
|
| ZINC13520374 ZINC | 0.694 | 426.3 Da LogP 0.97 TPSA 163.2 | ✓ Ro5 | ✓ Clean |
Cc1ncc(C[n+]2csc(CCO[P@@](=O)(O)OP(=O)(O)O)c2C)…
|
| ZINC1694013 ZINC | 0.690 | 281.4 Da LogP 0.31 TPSA 85.1 | ✓ Ro5 | ✓ Clean |
COc1ncc(C[n+]2csc(CCO)c2C)c(N)n1
|
| ZINC16052118 ZINC | 0.688 | 340.4 Da LogP -0.28 TPSA 84.8 | ✓ Ro5 | ✓ Clean |
COCCOCCOCCOCCOCCOCCOCCO
|
| ZINC34317654 ZINC | 0.688 | 472.6 Da LogP -0.23 TPSA 112.5 | 1 viol. | ✓ Clean |
COCCOCCOCCOCCOCCOCCOCCOCCOCCOCCO
|
| ZINC44583772 ZINC | 0.688 | 356.5 Da LogP 0.66 TPSA 64.6 | ✓ Ro5 | ✓ Clean |
COCCOCCOCCOCCOCCOCCOCCS
|
| ZINC575432090 ZINC | 0.688 | 355.4 Da LogP -0.38 TPSA 99.9 | ✓ Ro5 | ✓ Clean |
COCCOCCOCCOCCOCCOCCOCCON
|
| ZINC90556280 ZINC | 0.688 | 339.4 Da LogP -0.31 TPSA 90.6 | ✓ Ro5 | ✓ Clean |
COCCOCCOCCOCCOCCOCCOCCN
|
| ZINC90556286 ZINC | 0.688 | 312.4 Da LogP 0.65 TPSA 55.4 | ✓ Ro5 | ✓ Clean |
COCCOCCOCCOCCOCCOCCS
|
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
Chemistry
ChEMBL
CHEMBL403691
ChEMBL
CHEMBL255603
ChEMBL
CHEMBL271044
ChEMBL
CHEMBL256627
ChEMBL
CHEMBL270613
ChEMBL
CHEMBL401948
ChEMBL
0YN
ChEMBL
TZD
ChEMBL
CHEMBL252086
ChEMBL
CHEMBL403212
ChEMBL
CHEMBL401817
ChEMBL
CHEMBL256831
ChEMBL
CHEMBL402329
ChEMBL
CHEMBL402566
ChEMBL
CHEMBL255340
ChEMBL
CHEMBL252441
ChEMBL
CHEMBL258077
ChEMBL
CHEMBL256454
ChEMBL
CHEMBL255339
ChEMBL
CHEMBL270632
ChEMBL
CHEMBL403365
ChEMBL
CHEMBL255541
ChEMBL
CHEMBL255542
ChEMBL
CHEMBL429246
ChEMBL
CHEMBL271521
ChEMBL
CHEMBL270168
ChEMBL
CHEMBL252637
ChEMBL
CHEMBL270384
ChEMBL
CHEMBL430409
Pathways
BioCyc
1TRANSKETO-RXN-D-SEDOHEPTULOSE-7-P/GAP//CPD-16551/XYLULOSE-5-PHOSPHATE.56.
BioCyc
1TRANSKETO-RXN-D-SEDOHEPTULOSE-7-P/GAP//CPD-15895/XYLULOSE-5-PHOSPHATE.56.
KEGG
R01641
BioCyc
1TRANSKETO-RXN
KEGG
R01830
BioCyc
2TRANSKETO-RXN
BioCyc
1TRANSKETO-RXN-D-SEDOHEPTULOSE-7-P/GAP//CPD-15318/XYLULOSE-5-PHOSPHATE.56.