Research workbench
Structure of calmodulin bound to a calcineurin peptide: a new way of making an old binding mode
Analyse Structure of calmodulin bound to a calcineurin peptide: a new way of making an… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2F2O
- Type
- protein
- Length
- 315 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Calmodulin fused with calmodulin-binding domain of calcineurin
- UniProt
- P62157, Q309F2
- Ligands
- CA
- Pockets
- 4 · best druggability 0.62
Structure
x-ray diffraction · 2 distinct chains · 66% helix, 4% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Calmodulin fused with calmodulin-binding domain of calcineurin | protein | 156 | 65% helix, 4% strand | P62157, Q309F2 |
| B | Calmodulin fused with calmodulin-binding domain of calcineurin | protein | 159 | 67% helix, 4% strand | P62157, Q309F2 |
Ligands and binding sites
- CA · Calcium ion · metal · 8 copies · 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, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 392 | 0.62 | 0.77 | 48 | empty |
| 2 | 74 | 0.36 | 0.76 | 13 | empty |
| 3 | 51 | 0.31 | 0.76 | 7 | empty |
| 4 | 57 | 0.28 | 0.74 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 1744 Ų buried · 21 hydrogen bonds · protein-protein
Compared structures
- 2F2O · Structure of calmodulin bound to a calcineurin peptide: a new way of making an old… · the same entry in another collection · chain A against A, TM-score 1.00
- P62157 · AlphaFold monomer V2.0 prediction for calmodulin (P62157) · a predicted model of the same protein · chain B against A, TM-score 0.55
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 P62157
- Every structure of UniProt Q309F2
- Elsewhere: RCSB PDB 2F2O · PDBe 2F2O · UniProt P62157 · UniProt Q309F2
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