Research workbench
MRE11 ATLD17/18 mutation retains TEL1/ATM activity but blocks DNA double-strand break repair
Analyse MRE11 ATLD17/18 mutation retains TEL1/ATM activity but blocks DNA double-strand… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4HD0
- Type
- protein
- Length
- 651 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q8U1N9
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 332 | — | Q8U1N9 |
| B | — | protein | 319 | — | Q8U1N9 |
Compared structures
- 4HD0 · Mre11 ATLD17/18 mutation retains Tel1/ATM activity but blocks DNA double-strand break… · the same entry in another collection · chain A against A, TM-score 1.00
- Q8U1N9 · AlphaFold monomer V2.0 prediction for DNA double-strand break repair protein MRE11… · a predicted model of the same protein · chain B against A, TM-score 0.99
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 Q8U1N9
- Elsewhere: RCSB PDB 4HD0 · PDBe 4HD0 · UniProt Q8U1N9
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