Research workbench
Crystal structure of the human cyclin G associated kinase (gak)
Analyse Crystal structure of the human cyclin G associated kinase (gak) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4O38
- Type
- protein
- Length
- 543 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cyclin-G-associated kinase
- EC
- 2.7.11.1
- UniProt
- O14976
- Pockets
- 11 · best druggability 0.64
Structure
x-ray diffraction · 2 distinct chains · 35% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cyclin-G-associated kinase (EC 2.7.11.1) | protein | 267 | 36% helix, 21% strand | O14976 |
| B | Cyclin-G-associated kinase (EC 2.7.11.1) | protein | 276 | 34% helix, 21% strand | O14976 |
Ligands and binding sites
- SIN · Succinic acid · additive · 2 copies · chains A, B
- GOL · Glycerol · additive · 2 copies · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
11 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 327 | 0.64 | 0.80 | 41 | SIN |
| 2 | 275 | 0.64 | 0.81 | 35 | SIN |
| 3 | 196 | 0.51 | 0.77 | 28 | empty |
| 4 | 146 | 0.44 | 0.76 | 23 | empty |
| 5 | 51 | 0.44 | 0.84 | 20 | empty |
Interfaces
1 interface between chains.
- A–B · 1947 Ų buried · 27 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 8 modified (engineered).
Compared structures
- 4O38 · Crystal structure of the human cyclin G associated kinase (GAK) · the same entry in another collection · chain A against A, TM-score 1.00
- O14976 · AlphaFold monomer V2.0 prediction for cyclin-G-associated kinase (O14976) · a predicted model of the same protein · chain A against A, TM-score 0.95
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 O14976
- Elsewhere: RCSB PDB 4O38 · PDBe 4O38 · UniProt O14976
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