Research workbench
Crystal structure of plasmodium falciparum CDPK2 complexed with inhibitor staurosporine
Analyse Crystal structure of plasmodium falciparum CDPK2 complexed with inhibitor… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4MVF
- Type
- protein
- Length
- 408 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Calcium-dependent protein kinase 2
- EC
- 2.7.11.1
- UniProt
- O15865
- Ligands
- STU, CA
- Pockets
- 7 · best druggability 0.68
Structure
x-ray diffraction · 1 distinct chain · 48% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Calcium-dependent protein kinase 2 (EC 2.7.11.1) | protein | 408 | 48% helix, 15% strand | O15865 |
Ligands and binding sites
- STU · Staurosporine · ligand · chains A
- CA · Calcium ion · metal · 3 copies · chains A
- GOL · Glycerol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 225 | 0.68 | 0.85 | 39 | empty |
| 2 | 246 | 0.62 | 0.81 | 32 | STU |
| 3 | 310 | 0.56 | 0.76 | 37 | empty |
| 4 | 89 | 0.52 | 0.84 | 20 | empty |
| 5 | 183 | 0.50 | 0.77 | 21 | empty |
Compared structures
- 4MVF · Crystal Structure of Plasmodium falciparum CDPK2 complexed with inhibitor staurosporine · the same entry in another collection · chain A against A, TM-score 1.00
- O15865 · AlphaFold monomer V2.0 prediction for calcium-dependent protein kinase 2 (O15865) · a predicted model of the same protein · chain A against A, TM-score 0.96
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 O15865
- Elsewhere: RCSB PDB 4MVF · PDBe 4MVF · UniProt O15865
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