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Crystal structure of RAD53 1-466
Analyse Crystal structure of RAD53 1-466 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5XZW
- Type
- protein
- Length
- 757 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- SERINE/THREONINE-protein kinase RAD53
- EC
- 2.7.12.1
- UniProt
- P22216
- Pockets
- 7 · best druggability 0.79
Structure
x-ray diffraction · 2 distinct chains · 30% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | SERINE/THREONINE-protein kinase RAD53 (EC 2.7.12.1) | protein | 378 | 31% helix, 26% strand | P22216 |
| B | SERINE/THREONINE-protein kinase RAD53 (EC 2.7.12.1) | protein | 379 | 30% helix, 25% strand | P22216 |
Pockets
7 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 851 | 0.79 | 0.82 | 97 | empty |
| 2 | 546 | 0.74 | 0.82 | 50 | empty |
| 3 | 539 | 0.70 | 0.79 | 61 | empty |
| 4 | 300 | 0.54 | 0.75 | 36 | empty |
| 5 | 83 | 0.45 | 0.81 | 17 | empty |
Interfaces
1 interface between chains.
- A–B · 1084 Ų buried · 9 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 P22216
- Elsewhere: RCSB PDB 5XZW · PDBe 5XZW · UniProt P22216
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