Research workbench
Crystal structure of calcium binding domain of CPCDPK3, CGD5_820
Analyse Crystal structure of calcium binding domain of CPCDPK3, CGD5_820 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3L19
- Type
- protein
- Length
- 363 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- CALCIUM/CALMODULIN dependent protein kinase with a kinase domain and 4 calmodulin like ef…
- EC
- 2.7.1.-
- UniProt
- Q5CS01
- Ligands
- CA
- Pockets
- 4 · best druggability 0.49
Structure
x-ray diffraction · 2 distinct chains · 64% helix, 4% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | CALCIUM/CALMODULIN dependent protein kinase with a kinase domain and 4 calmodulin like ef hands (EC 2.7.1.-) | protein | 184 | 64% helix, 4% strand | Q5CS01 |
| B | CALCIUM/CALMODULIN dependent protein kinase with a kinase domain and 4 calmodulin like ef hands (EC 2.7.1.-) | protein | 179 | 64% helix, 4% strand | Q5CS01 |
Ligands and binding sites
- CA · Calcium ion · metal · 8 copies · chains A, B
- GOL · Glycerol · additive · 4 copies · chains A, B
- 1PE · Pentaethylene glycol · additive · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 190 | 0.49 | 0.76 | 31 | GOL, 1PE |
| 2 | 143 | 0.41 | 0.74 | 23 | empty |
| 3 | 91 | 0.33 | 0.73 | 16 | empty |
| 4 | 63 | 0.29 | 0.74 | 17 | empty |
Interfaces
1 interface between chains.
- A–B · 410 Ų buried · 14 hydrogen bonds · protein-protein
Compared structures
- 3L19 · Crystal structure of calcium binding domain of CpCDPK3, cgd5_820 · the same entry in another collection · chain A against A, TM-score 1.00
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 Q5CS01
- Elsewhere: RCSB PDB 3L19 · PDBe 3L19 · UniProt Q5CS01
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