Research workbench
The MRE11:RAD50 complex forms an ATP dependent molecular clamp in DNA double-strand break repair
Analyse The MRE11:RAD50 complex forms an ATP dependent molecular clamp in DNA… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3QF7
- Type
- protein
- Length
- 782 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q9X1X1, Q9X1X0
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 357 | — | Q9X1X1 |
| B | — | protein | 355 | — | Q9X1X1 |
| D, C | — | protein | 35 | — | Q9X1X0 |
Compared structures
- 3QF7 · The Mre11:Rad50 complex forms an ATP dependent molecular clamp in DNA double-strand break… · the same entry in another collection · chain A against A, TM-score 1.00
- Q9X1X1 · AlphaFold monomer V2.0 prediction for probable DNA double-strand break repair RAD50… · a predicted model of the same protein · chain A against A, TM-score 0.94
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 Q9X1X1
- Every structure of UniProt Q9X1X0
- Elsewhere: RCSB PDB 3QF7 · PDBe 3QF7 · UniProt Q9X1X1 · UniProt Q9X1X0
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