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Crystal structure of apo-glycine N-methyltransferase (gnmt)
Analyse Crystal structure of apo-glycine N-methyltransferase (gnmt) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1BHJ
- Type
- protein
- Length
- 584 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glycine N-methyltransferase
- EC
- 2.1.1.20
- UniProt
- P13255
- Pockets
- 6 · best druggability 0.84
Structure
x-ray diffraction · 1 distinct chain · 27% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Glycine N-methyltransferase (EC 2.1.1.20) | protein | 292 | 27% helix, 25% strand | P13255 |
Pockets
6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 298 | 0.84 | 0.94 | 43 | empty |
| 2 | 320 | 0.84 | 0.94 | 42 | empty |
| 3 | 574 | 0.77 | 0.83 | 60 | empty |
| 4 | 102 | 0.40 | 0.76 | 25 | empty |
| 5 | 98 | 0.39 | 0.76 | 24 | empty |
Interfaces
1 interface between chains.
- A–B · 2138 Ų buried · 29 hydrogen bonds · protein-protein
Compared structures
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: RCSB PDB 1BHJ · PDBe 1BHJ · UniProt P13255
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