MolNFT v1 · #148661 · protein
Thiophosphorylated PAK3 kinase domain
6FD3 · SERINE/THREONINE-protein kinase pak 3: “Thiophosphorylated PAK3 kinase domain”. X-ray diffraction, 2 ligands (ADP, MG), 1 pocket (best druggability 0.68). MolNFT v1 #148661 on GenesisL1: 3D structure, binding sites and pockets in…
- PDB
- 6FD3
- Type
- protein
- Length
- 297 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- SERINE/THREONINE-protein kinase pak 3
- EC
- 2.7.11.1
- UniProt
- O75914
- Ligands
- ADP, MG
- Pockets
- 1 · best druggability 0.68
Structure
x-ray diffraction · 1 distinct chain · 43% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | SERINE/THREONINE-protein kinase pak 3 (EC 2.7.11.1) | protein | 297 | 43% helix, 18% strand | O75914 |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · chains A
- MG · Magnesium ion · metal · 2 copies · chains A
- EDO · 1,2-ethanediol · additive · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 274 | 0.68 | 0.84 | 38 | MG, ADP |
Modifications
Observed in the structure: 1 modified (nonstandard).
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 O75914
- Elsewhere: RCSB PDB 6FD3 · PDBe 6FD3 · UniProt O75914
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