MolNFT v1 · #154761 · protein
AlphaFold monomer V2.0 prediction for glycine N-methyltransferase (P13255)
P13255: “AlphaFold monomer V2.0 prediction for glycine N-methyltransferase (P13255)”. 4 pockets (best druggability 0.79). MolNFT v1 #154761 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- Accession
- P13255
- Type
- protein
- Length
- 293 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xc5799D7f1A93bc7790F029132Fea537c97F07693
- Molecule
- Glycine N-methyltransferase
- UniProt
- P13255
- Pockets
- 4 · best druggability 0.79
Structure
1 distinct chain · 31% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glycine N-methyltransferase | protein | 293 | 31% helix, 29% strand | P13255 |
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 138 | 0.79 | 0.97 | 30 | empty |
| 2 | 172 | 0.54 | 0.80 | 32 | empty |
| 3 | 103 | 0.37 | 0.75 | 20 | empty |
| 4 | 70 | 0.35 | 0.77 | 18 | empty |
Compared structures
- 1NBH · Structure of glycine N-methyltransferase complexed with S-adenosylmethionine and acetate… · an experimental structure of the same protein · chain A against D, TM-score 0.93
- 1NBH · Structure of glycine N-methyltransferase complexed with S- adenosylmethionine and… · an experimental structure of the same protein · chain A against D, TM-score 0.93
- 1KIA · Crystal structure of glycine N-methyltransferase complexed with S-adenosylmethionine and… · an experimental structure of the same protein · chain A against B, TM-score 0.92
- 1KIA · Crystal structure of glycine N-methyltransferase complexed with S- adenosylmethionine and… · an experimental structure of the same protein · chain A against B, TM-score 0.92
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P13255
- Elsewhere: UniProt P13255 · AlphaFold DB P13255
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