Research workbench
Structure of calmodulin complexed with the calmodulin binding domain of calcineurin
Analyse Structure of calmodulin complexed with the calmodulin binding domain of… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2JZI
- Type
- protein
- Length
- 172 residues
- Chains
- 2
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Calmodulin; SERINE/THREONINE-protein phosphatase 2B catalytic subunit alpha isoform
- EC
- 3.1.3.16
- UniProt
- P62158, Q08209
- Ligands
- CA
- Pockets
- 3 · best druggability 0.57
Structure
solution nmr · 2 distinct chains · 62% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Calmodulin | protein | 148 | 57% helix, 0% strand | P62158 |
| B | SERINE/THREONINE-protein phosphatase 2B catalytic subunit alpha isoform (EC 3.1.3.16) | protein | 24 | 92% helix, 0% strand | Q08209 |
Ligands and binding sites
- CA · Calcium ion · metal · 4 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 210 | 0.57 | 0.79 | 30 | empty |
| 2 | 168 | 0.54 | 0.80 | 30 | empty |
| 3 | 86 | 0.39 | 0.77 | 22 | empty |
Interfaces
1 interface between chains.
- A–B · 1339 Ų buried · 10 hydrogen bonds · protein-protein
Compared structures
- 2JZI · Structure of Calmodulin complexed with the Calmodulin Binding Domain of Calcineurin · the same entry in another collection · chain A against A, TM-score 1.00
- Q08209 · AlphaFold monomer V2.0 prediction for SERINE/THREONINE-protein phosphatase 2B catalytic… · a predicted model of the same protein · chain B against A, TM-score 0.52
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 P62158
- Every structure of UniProt Q08209
- Elsewhere: RCSB PDB 2JZI · PDBe 2JZI · UniProt P62158 · UniProt Q08209
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