MolNFT v1 · #38195 · protein
Crystal structure of putative O-methyltransferase from bacillus halodurans
2GPY: “Crystal structure of putative O-methyltransferase from bacillus halodurans”. X-ray diffraction, 2 ligands (ZN, MG), 9 pockets (best druggability 0.60). MolNFT v1 #38195 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 2GPY
- Type
- protein
- Length
- 377 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- O-methyltransferase
- Ligands
- ZN, MG
- Pockets
- 9 · best druggability 0.60
Structure
x-ray diffraction · 2 distinct chains · 42% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | O-methyltransferase | protein | 185 | 42% helix, 23% strand | — |
| B | O-methyltransferase | protein | 192 | 42% helix, 23% strand | — |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
9 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 56 | 0.60 | 0.92 | 18 | empty |
| 2 | 280 | 0.59 | 0.78 | 36 | empty |
| 3 | 96 | 0.55 | 0.85 | 26 | empty |
| 4 | 79 | 0.46 | 0.82 | 18 | empty |
| 5 | 91 | 0.45 | 0.80 | 21 | empty |
Interfaces
1 interface between chains.
- A–B · 1356 Ų buried · 9 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 14 modified (engineered).
Compared structures
- 2GPY · Crystal structure of putative O-methyltransferase from Bacillus halodurans · the same entry in another collection · chain B against B, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Elsewhere: RCSB PDB 2GPY · PDBe 2GPY
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