MolNFT v1 · #137117 · protein
PAK4 kinase domain in complex with fasudil
5VEF · SERINE/THREONINE-protein kinase pak 4: “PAK4 kinase domain in complex with fasudil”. X-ray diffraction, 1 ligand (M77), 2 pockets (best druggability 0.66). MolNFT v1 #137117 on GenesisL1: 3D structure, binding sites and pockets in…
- PDB
- 5VEF
- Type
- protein
- Length
- 290 residues
- Chains
- 1
- 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
- Ligands
- M77
- Pockets
- 2 · best druggability 0.66
Structure
x-ray diffraction · 1 distinct chain · 42% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | SERINE/THREONINE-protein kinase pak 4 (EC 2.7.11.1) | protein | 290 | 42% helix, 18% strand | O96013 |
Ligands and binding sites
- M77 · 5-(1,4-diazepan-1-sulfonyl)isoquinoline · ligand · chains A
- ACT · Acetate ion · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 263 | 0.66 | 0.83 | 35 | M77 |
| 2 | 62 | 0.36 | 0.78 | 15 | empty |
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 5VEF · PDBe 5VEF · UniProt O96013
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