Research workbench
Structure of the glycoslyase domain of MBD4 bound to a 5HMU containing DNA
Analyse Structure of the glycoslyase domain of MBD4 bound to a 5HMU containing DNA in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4EA5
- Type
- protein + DNA
- Length
- 156 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- O95243
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 136 | — | O95243 |
| C | — | dna | 10 | — | — |
| D | — | dna | 10 | — | — |
Compared structures
- 4EA5 · Structure of the glycoslyase domain of MBD4 bound to a 5hmU containing DNA · the same entry in another collection · chain A against A, TM-score 1.00
- O95243 · AlphaFold monomer V2.0 prediction for methyl-cpg-binding domain protein 4 (O95243) · a predicted model of the same protein · chain A against A, TM-score 0.98
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 O95243
- Elsewhere: RCSB PDB 4EA5 · PDBe 4EA5 · UniProt O95243
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