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Crystal structure of apo-pkr kinase domain
Analyse Crystal structure of apo-pkr kinase domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3UIU
- Type
- protein
- Length
- 510 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Interferon-induced, double-stranded RNA-activated protein kinase
- EC
- 2.7.11.1, 2.7.10.2
- UniProt
- P19525
- Pockets
- 7 · best druggability 0.72
Structure
x-ray diffraction · 1 distinct chain · 35% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Interferon-induced, double-stranded RNA-activated protein kinase (EC 2.7.11.1, 2.7.10.2) | protein | 255 | 35% helix, 20% strand | P19525 |
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 | 65 | 0.72 | 0.98 | 21 | empty |
| 2 | 418 | 0.68 | 0.80 | 55 | empty |
| 3 | 252 | 0.61 | 0.80 | 36 | empty |
| 4 | 246 | 0.58 | 0.79 | 35 | empty |
| 5 | 125 | 0.48 | 0.79 | 21 | empty |
Interfaces
1 interface between chains.
- A–B · 947 Ų buried · 8 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 P19525
- Elsewhere: RCSB PDB 3UIU · PDBe 3UIU · UniProt P19525
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