Research workbench
Solvation effect in conformational changes of ef-hand proteins: X-ray structure of CA2+-saturated double mutant Q41L-K75I of N-domain of calmodulin
Analyse Solvation effect in conformational changes of ef-hand proteins: X-ray structure… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2I08
- Type
- protein
- Length
- 74 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Calmodulin
- UniProt
- P62155
- Ligands
- CA
Structure
x-ray diffraction · 1 distinct chain · 64% helix, 3% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Calmodulin | protein | 74 | 64% helix, 3% strand | P62155 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 2I08 · Solvation effect in conformational changes of EF-hand proteins: X-ray structure of… · 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 P62155
- Elsewhere: RCSB PDB 2I08 · PDBe 2I08 · UniProt P62155
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