Research workbench
Structure of mouse DNMT1 (731-1602) bound to hemimethylated cpg DNA
Analyse Structure of mouse DNMT1 (731-1602) bound to hemimethylated cpg DNA in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4DA4
- Type
- protein + DNA
- Length
- 1,716 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P13864
Structure
x-ray diffraction · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 835 | — | P13864 |
| B | — | protein | 833 | — | P13864 |
| C, E | — | dna | 12 | — | — |
| D, F | — | dna | 12 | — | — |
Compared structures
- 4DA4 · Structure of mouse DNMT1 (731-1602) bound to hemimethylated CpG DNA · the same entry in another collection · chain F against F, TM-score 1.00
- P13864 · AlphaFold monomer V2.0 prediction for DNA (cytosine-5)-methyltransferase 1 (P13864) · a predicted model of the same protein · chain B against A, TM-score 0.97
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 P13864
- Elsewhere: RCSB PDB 4DA4 · PDBe 4DA4 · UniProt P13864
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