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Crystal structure of catalytic domain of PAK4
Analyse Crystal structure of catalytic domain of PAK4 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4L67
- Type
- protein
- Length
- 310 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- SERINE/THREONINE-protein kinase pak 4
- EC
- 2.7.11.1
- UniProt
- O96013
- Pockets
- 3 · best druggability 0.79
Structure
x-ray diffraction · 2 distinct chains · 35% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | SERINE/THREONINE-protein kinase pak 4 (EC 2.7.11.1) | protein | 290 | 37% helix, 16% strand | O96013 |
| B | SERINE/THREONINE-protein kinase pak 4 (EC 2.7.11.1) | protein | 20 | 20% helix, 0% strand | O96013 |
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 656 | 0.79 | 0.84 | 58 | empty |
| 2 | 60 | 0.52 | 0.87 | 14 | empty |
| 3 | 56 | 0.32 | 0.77 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 851 Ų buried · 5 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 modified (phosphorylation).
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 O96013
- Elsewhere: RCSB PDB 4L67 · PDBe 4L67 · UniProt O96013
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