Research workbench
Crystal structure of the methyltransferase BC_2162 in complex with S- adenosyl-L-homocysteine from bacillus cereus, northeast structural genomics consortium target BCR20
Analyse Crystal structure of the methyltransferase BC_2162 in complex with S… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3GU3
- Type
- protein
- Length
- 552 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Methyltransferase
- EC
- 2.1.1.-
- UniProt
- Q81E32
- Ligands
- SAH
- Pockets
- 7 · best druggability 0.60
Structure
x-ray diffraction · 1 distinct chain · 41% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Methyltransferase (EC 2.1.1.-) | protein | 276 | 41% helix, 21% strand | Q81E32 |
Ligands and binding sites
- SAH · S-adenosyl-L-homocysteine · ligand · 2 copies · chains A, B
- ACT · Acetate ion · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 391 | 0.60 | 0.76 | 53 | SAH |
| 2 | 345 | 0.59 | 0.76 | 36 | empty |
| 3 | 128 | 0.56 | 0.83 | 22 | empty |
| 4 | 137 | 0.54 | 0.81 | 26 | empty |
| 5 | 210 | 0.49 | 0.75 | 27 | empty |
Interfaces
1 interface between chains.
- A–B · 2001 Ų buried · 46 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 16 modified (engineered).
Compared structures
- 3GU3 · Crystal Structure of the methyltransferase BC_2162 in complex with… · 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
- Every structure of UniProt Q81E32
- Elsewhere: RCSB PDB 3GU3 · PDBe 3GU3 · UniProt Q81E32
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