Research workbench
Crystal structure of CTR1 kinase domain mutant D676N in complex with staurosporine
Analyse Crystal structure of CTR1 kinase domain mutant D676N in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3P86
- Type
- protein
- Length
- 489 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- SERINE/THREONINE-protein kinase CTR1
- EC
- 2.7.11.1
- UniProt
- Q05609
- Ligands
- STU
- Pockets
- 5 · best druggability 0.79
Structure
x-ray diffraction · 2 distinct chains · 41% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | SERINE/THREONINE-protein kinase CTR1 (EC 2.7.11.1) | protein | 250 | 42% helix, 18% strand | Q05609 |
| B | SERINE/THREONINE-protein kinase CTR1 (EC 2.7.11.1) | protein | 239 | 39% helix, 17% strand | Q05609 |
Ligands and binding sites
- STU · Staurosporine · ligand · chains A
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 | 890 | 0.79 | 0.82 | 79 | empty |
| 2 | 249 | 0.65 | 0.82 | 31 | empty |
| 3 | 300 | 0.65 | 0.80 | 31 | STU |
| 4 | 100 | 0.45 | 0.79 | 21 | empty |
| 5 | 52 | 0.31 | 0.76 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 1124 Ų buried · 13 hydrogen bonds · protein-protein
Compared structures
- 3P86 · Crystal structure of CTR1 kinase domain mutant D676N in complex with staurosporine · the same entry in another collection · chain A against A, TM-score 1.00
- Q05609 · AlphaFold monomer V2.0 prediction for SERINE/THREONINE-protein kinase CTR1 (Q05609) · a predicted model of the same protein · chain B against A, TM-score 0.98
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 Q05609
- Elsewhere: RCSB PDB 3P86 · PDBe 3P86 · UniProt Q05609
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