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Crystal structure of ppra W183R mutant form 1
Analyse Crystal structure of ppra W183R mutant form 1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6A27
- Type
- protein
- Length
- 402 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- DNA repair protein ppra
- UniProt
- O32504
- Ligands
- SO4
- Pockets
- 4 · best druggability 0.50
Structure
x-ray diffraction · 2 distinct chains · 42% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | DNA repair protein ppra | protein | 202 | 41% helix, 22% strand | O32504 |
| B | DNA repair protein ppra | protein | 200 | 43% helix, 22% strand | O32504 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 202 | 0.50 | 0.76 | 23 | empty |
| 2 | 117 | 0.48 | 0.79 | 21 | empty |
| 3 | 139 | 0.45 | 0.76 | 21 | empty |
| 4 | 66 | 0.36 | 0.77 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 798 Ų buried · 13 hydrogen bonds · protein-protein
Compared structures
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 O32504
- Elsewhere: RCSB PDB 6A27 · PDBe 6A27 · UniProt O32504
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