Research workbench
Crystal structure of S. pombe DNMT2 methyltransferase
Analyse Crystal structure of S. pombe DNMT2 methyltransferase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6FDF
- Type
- protein
- Length
- 1,273 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P40999
Structure
x-ray diffraction · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 326 | — | P40999 |
| B | — | protein | 319 | — | P40999 |
| C | — | protein | 314 | — | P40999 |
| D | — | protein | 314 | — | P40999 |
Ligands and binding sites
- GOL · Glycerol · additive · 11 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6FDF · Crystal structure of S. pombe Dnmt2 methyltransferase · the same entry in another collection · chain A against A, TM-score 1.00
- P40999 · AlphaFold monomer V2.0 prediction for tRNA (CYTOSINE(38)-C(5))-methyltransferase (P40999) · a predicted model of the same protein · chain D against A, TM-score 0.96
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 P40999
- Elsewhere: RCSB PDB 6FDF · PDBe 6FDF · UniProt P40999
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