Research workbench
Binary complex structure of human tau protein kinase I with ADP
Analyse Binary complex structure of human tau protein kinase I with ADP in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1J1C
- Type
- protein
- Length
- 718 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glycogen synthase kinase-3 beta
- EC
- 2.7.1.37
- UniProt
- P49841
- Ligands
- ADP, MG
- Pockets
- 10 · best druggability 0.79
Structure
x-ray diffraction · 2 distinct chains · 34% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glycogen synthase kinase-3 beta (EC 2.7.1.37) | protein | 354 | 34% helix, 19% strand | P49841 |
| B | Glycogen synthase kinase-3 beta (EC 2.7.1.37) | protein | 364 | 34% helix, 21% strand | P49841 |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · 2 copies · chains A, B
- MG · Magnesium ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
10 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 789 | 0.79 | 0.82 | 73 | MG, ADP |
| 2 | 819 | 0.78 | 0.81 | 70 | MG, ADP |
| 3 | 106 | 0.77 | 0.98 | 29 | empty |
| 4 | 115 | 0.48 | 0.79 | 25 | empty |
| 5 | 97 | 0.46 | 0.80 | 24 | empty |
Interfaces
1 interface between chains.
- A–B · 1667 Ų buried · 21 hydrogen bonds · protein-protein
Compared structures
- 1J1C · Binary complex structure of human tau protein kinase I with ADP · the same entry in another collection · chain A against A, TM-score 1.00
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
- Elsewhere: RCSB PDB 1J1C · PDBe 1J1C · UniProt P49841
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