Research workbench
Structure of the C-terminal brct domain of human XRCC1
Analyse Structure of the C-terminal brct domain of human XRCC1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6WH2
- Type
- protein
- Length
- 191 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- X-ray repair cross complementing protein 1 variant
- UniProt
- Q59HH7
- Pockets
- 1 · best druggability 0.37
Structure
x-ray diffraction · 2 distinct chains · 35% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | X-ray repair cross complementing protein 1 variant | protein | 95 | 36% helix, 16% strand | Q59HH7 |
| B | X-ray repair cross complementing protein 1 variant | protein | 96 | 34% helix, 14% strand | Q59HH7 |
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 | 83 | 0.37 | 0.77 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 623 Ų buried · 12 hydrogen bonds · protein-protein
Compared structures
- 6WH2 · Structure of the C-terminal BRCT domain of human XRCC1 · the same entry in another collection · chain A against A, TM-score 1.00
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 Q59HH7
- Elsewhere: RCSB PDB 6WH2 · PDBe 6WH2 · UniProt Q59HH7
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