MolNFT v1 · #168612 · protein
PAK4 kinase domain in complex with beta-catenin SER675 substrate peptide
6WLX · SERINE/THREONINE-protein kinase pak 4: “PAK4 kinase domain in complex with beta-catenin SER675 substrate peptide”. X-ray diffraction, 2 pockets (best druggability 0.59). MolNFT v1 #168612 on GenesisL1: 3D structure, binding sites…
- PDB
- 6WLX
- Type
- protein
- Length
- 297 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- SERINE/THREONINE-protein kinase pak 4; Catenin beta-1
- EC
- 2.7.11.1
- UniProt
- O96013, P35222
- Pockets
- 2 · best druggability 0.59
Structure
x-ray diffraction · 2 distinct chains · 40% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | SERINE/THREONINE-protein kinase pak 4 (EC 2.7.11.1) | protein | 292 | 41% helix, 17% strand | O96013 |
| B | Catenin beta-1 | protein | 5 | 0% helix, 0% strand | P35222 |
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 | 231 | 0.59 | 0.80 | 37 | empty |
| 2 | 70 | 0.36 | 0.77 | 22 | empty |
Interfaces
1 interface between chains.
- A–B · 430 Ų buried · 10 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 modified (phosphorylation).
Compared structures
- 6WLX · PAK4 kinase domain in complex with beta-catenin Ser675 substrate peptide · the same entry in another collection · chain A against A, TM-score 1.00
- O96013 · AlphaFold monomer V2.0 prediction for SERINE/THREONINE-protein kinase pak 4 (O96013) · a predicted model of the same protein · chain A against A, TM-score 0.98
- P35222 · AlphaFold monomer V2.0 prediction for catenin beta-1 (P35222) · a predicted model of the same protein · chain B against A, TM-score 0.77
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
- Every structure of UniProt P35222
- Elsewhere: RCSB PDB 6WLX · PDBe 6WLX · UniProt O96013 · UniProt P35222
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