Research workbench
The structure of a putative type II methyltransferase from anaeromyxobacter dehalogenans.
Analyse The structure of a putative type II methyltransferase from anaeromyxobacter… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4HG2
- Type
- protein
- Length
- 471 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Methyltransferase type 11
- UniProt
- Q2IE03
- Pockets
- 3 · best druggability 0.78
Structure
x-ray diffraction · 2 distinct chains · 35% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Methyltransferase type 11 | protein | 235 | 35% helix, 24% strand | Q2IE03 |
| B | Methyltransferase type 11 | protein | 236 | 35% helix, 24% strand | Q2IE03 |
Ligands and binding sites
- EDO · 1,2-ethanediol · additive · 5 copies · chains A, B
- MES · 2-(N-morpholino)-ethanesulfonic acid · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1033 | 0.78 | 0.80 | 89 | MES |
| 2 | 149 | 0.46 | 0.77 | 19 | empty |
| 3 | 52 | 0.35 | 0.79 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 474 Ų buried · 6 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 modified (engineered).
Compared structures
- 4HG2 · The Structure of a Putative Type II Methyltransferase from Anaeromyxobacter dehalogenans. · the same entry in another collection · chain A against A, 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 Q2IE03
- Elsewhere: RCSB PDB 4HG2 · PDBe 4HG2 · UniProt Q2IE03
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