Research workbench
Crystal structure of ATP-free RAD50 ABC-ATPase
Analyse Crystal structure of ATP-free RAD50 ABC-ATPase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1F2T
- Type
- protein
- Length
- 288 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- RAD50 ABC-ATPase
- UniProt
- P58301
- Pockets
- 1 · best druggability 0.39
Structure
x-ray diffraction · 2 distinct chains · 35% helix, 33% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | RAD50 ABC-ATPase | protein | 145 | 26% helix, 37% strand | P58301 |
| B | RAD50 ABC-ATPase | protein | 143 | 45% helix, 29% strand | P58301 |
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 119 | 0.39 | 0.74 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 2340 Ų buried · 41 hydrogen bonds · protein-protein
Compared structures
- 1F2T · Crystal Structure of ATP-Free RAD50 ABC-ATPase · the same entry in another collection · chain A against A, TM-score 1.00
- P58301 · AlphaFold monomer V2.0 prediction for DNA double-strand break repair RAD50 ATPase (P58301) · a predicted model of the same protein · chain A against A, TM-score 0.88
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 P58301
- Elsewhere: RCSB PDB 1F2T · PDBe 1F2T · UniProt P58301
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