Research workbench
Structure of RIP2K(D146N) with bound staurosporine
Analyse Structure of RIP2K(D146N) with bound staurosporine in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5NG2
- Type
- protein
- Length
- 552 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Receptor-interacting SERINE/THREONINE-protein kinase 2
- EC
- 2.7.11.1, 2.7.10.2
- UniProt
- O43353
- Ligands
- STU, PO4
- Pockets
- 8 · best druggability 0.79
Structure
x-ray diffraction · 2 distinct chains · 37% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Receptor-interacting SERINE/THREONINE-protein kinase 2 (EC 2.7.11.1, 2.7.10.2) | protein | 274 | 36% helix, 18% strand | O43353 |
| B | Receptor-interacting SERINE/THREONINE-protein kinase 2 (EC 2.7.11.1, 2.7.10.2) | protein | 278 | 38% helix, 18% strand | O43353 |
Ligands and binding sites
- STU · Staurosporine · ligand · 2 copies · chains A, B
- PO4 · Phosphate ion · ion · 6 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 921 | 0.79 | 0.81 | 85 | PO4 |
| 2 | 366 | 0.66 | 0.80 | 37 | STU |
| 3 | 333 | 0.65 | 0.81 | 37 | STU |
| 4 | 120 | 0.46 | 0.78 | 18 | empty |
| 5 | 139 | 0.45 | 0.77 | 18 | PO4 |
Interfaces
1 interface between chains.
- A–B · 1543 Ų buried · 14 hydrogen bonds · protein-protein
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 O43353
- Elsewhere: RCSB PDB 5NG2 · PDBe 5NG2 · UniProt O43353
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