Binding Sites are compared using Shaper.
For more information, please see the following publication:
Desaphy J. et al. Comparison and Druggability Prediction of protein-Ligand Binding sites from pharmacophore-annotated cavity shapes J. Chem. Inf. Model., 2012, 52(8), pp2287-2299
Binding Sites are considered as similar when the similarity value is greater than 0.44
| PDB ID | HET | Uniprot Name | EC Number |
|---|---|---|---|
| 3fpd | SAH | Histone-lysine N-methyltransferase EHMT1 |
| PDB ID | HET | Uniprot Name | EC Number | Binding Site Similarity |
Align |
|---|---|---|---|---|---|
| 3fpd | SAH | Histone-lysine N-methyltransferase EHMT1 | / | 1.000 | |
| 2o8j | SAH | Histone-lysine N-methyltransferase EHMT2 | / | 0.630 | |
| 3mo0 | SAH | Histone-lysine N-methyltransferase EHMT1 | / | 0.619 | |
| 2igq | SAH | Histone-lysine N-methyltransferase EHMT1 | / | 0.604 | |
| 3hna | SAH | Histone-lysine N-methyltransferase EHMT1 | / | 0.563 | |
| 5jin | SAM | Histone-lysine N-methyltransferase EHMT2 | / | 0.562 | |
| 5czy | SAM | Eukaryotic huntingtin interacting protein B | / | 0.515 | |
| 2rfi | SAH | Histone-lysine N-methyltransferase EHMT1 | / | 0.505 | |
| 3swc | SAH | Histone-lysine N-methyltransferase EHMT1 | / | 0.491 | |
| 3kmt | SAH | Histone H3K27 methylase | / | 0.463 | |
| 1kbo | 340 | NAD(P)H dehydrogenase [quinone] 1 | 1.6.5.2 | 0.457 | |
| 3u9f | CLM | Chloramphenicol acetyltransferase | 2.3.1.28 | 0.453 | |
| 3ooi | SAM | Histone-lysine N-methyltransferase, H3 lysine-36 and H4 lysine-20 specific | 2.1.1.43 | 0.448 | |
| 2h21 | SAM | Ribulose-1,5 bisphosphate carboxylase/oxygenase large subunit N-methyltransferase, chloroplastic | 2.1.1.127 | 0.446 | |
| 4ype | SAM | Histone-lysine N-methyltransferase ASH1L | 2.1.1.43 | 0.444 | |
| 4cf6 | CBD | NAD(P)H dehydrogenase [quinone] 1 | 1.6.5.2 | 0.443 | |
| 2gv8 | NDP | Thiol-specific monooxygenase | 1.14.13 | 0.442 | |
| 2qim | ZEA | Class 10 plant pathogenesis-related protein | / | 0.442 | |
| 3ru0 | SFG | Histone-lysine N-methyltransferase SMYD3 | 2.1.1.43 | 0.441 |