Research workbench
Crystal structure of CHK1 kinase domain in complex with a claspin phosphopeptide
Analyse Crystal structure of CHK1 kinase domain in complex with a claspin phosphopeptide in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7AKO
- Type
- protein
- Length
- 561 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- SERINE/THREONINE-protein kinase CHK1; Claspin
- EC
- 2.7.11.1
- UniProt
- O14757, Q9HAW4
- Ligands
- STU, ZN
- Pockets
- 5 · best druggability 0.62
Structure
x-ray diffraction · 4 distinct chains · 35% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | SERINE/THREONINE-protein kinase CHK1 (EC 2.7.11.1) | protein | 270 | 35% helix, 22% strand | O14757 |
| B | SERINE/THREONINE-protein kinase CHK1 (EC 2.7.11.1) | protein | 271 | 35% helix, 21% strand | O14757 |
| C | Claspin | protein | 10 | 60% helix, 0% strand | Q9HAW4 |
| D | Claspin | protein | 10 | 0% helix, 0% strand | Q9HAW4 |
Ligands and binding sites
- STU · Staurosporine · ligand · 2 copies · chains A, B
- ZN · Zinc ion · metal · chains A, C
- EDO · 1,2-ethanediol · additive · 7 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 252 | 0.62 | 0.81 | 31 | STU |
| 2 | 257 | 0.61 | 0.80 | 32 | STU |
| 3 | 174 | 0.56 | 0.81 | 26 | empty |
| 4 | 100 | 0.36 | 0.75 | 17 | empty |
| 5 | 61 | 0.31 | 0.75 | 17 | empty |
Interfaces
4 interfaces between chains.
- B–D · 564 Ų buried · 7 hydrogen bonds · protein-protein
- A–B · 505 Ų buried · 6 hydrogen bonds · protein-protein
- A–C · 484 Ų buried · 8 hydrogen bonds · protein-protein
- B–C · 255 Ų buried · 3 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified (phosphorylation).
Compared structures
- 7AKO · Crystal structure of CHK1 kinase domain in complex with a CLASPIN phosphopeptide · the same entry in another collection · chain A against A, TM-score 1.00
- O14757 · AlphaFold monomer V2.0 prediction for SERINE/THREONINE-protein kinase CHK1 (O14757) · a predicted model of the same protein · chain B against A, TM-score 0.96
- 2C3K · Identification of a buried pocket for potent and selective inhibition of CHK1: prediction… · a predicted model of the same protein · chain B against A, TM-score 0.95
- 2C3L · Identification of a buried pocket for potent and selective inhibition of CHK1: prediction… · a predicted model of the same protein · chain B against A, TM-score 0.94
- 2C3J · Identification of a buried pocket for potent and selective inhibition of CHK1: prediction… · a predicted model of the same protein · chain B against A, TM-score 0.94
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 O14757
- Every structure of UniProt Q9HAW4
- Elsewhere: RCSB PDB 7AKO · PDBe 7AKO · UniProt O14757 · UniProt Q9HAW4
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