Research workbench
Crystal structure of gsk-3/AXIN complex bound to phosphorylated N- terminal auto-inhibitory PS9 peptide
Analyse Crystal structure of gsk-3/AXIN complex bound to phosphorylated N- terminal… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4NM3
- Type
- protein
- Length
- 377 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glycogen synthase kinase-3 beta; Axin-1
- EC
- 2.7.11.26, 2.7.11.1
- UniProt
- P49841, O15169
- Ligands
- ADP, MG, CL
- Pockets
- 4 · best druggability 0.67
Structure
x-ray diffraction · 2 distinct chains · 36% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glycogen synthase kinase-3 beta (EC 2.7.11.26, 2.7.11.1) | protein | 358 | 33% helix, 20% strand | P49841 |
| B | Axin-1 | protein | 19 | 84% helix, 0% strand | O15169 |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · chains A
- MG · Magnesium ion · metal · 2 copies · chains A
- CL · Chloride ion · ion · chains A
- GOL · Glycerol · additive · 4 copies · chains A
- DTT · 2,3-dihydroxy-1,4-dithiobutane · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 478 | 0.67 | 0.78 | 46 | MG, ADP |
| 2 | 61 | 0.41 | 0.81 | 20 | empty |
| 3 | 111 | 0.41 | 0.76 | 26 | empty |
| 4 | 57 | 0.29 | 0.75 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 716 Ų buried · 2 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 P49841
- Every structure of UniProt O15169
- Elsewhere: RCSB PDB 4NM3 · PDBe 4NM3 · UniProt P49841 · UniProt O15169
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