Research workbench
Complex of iqcg and CA2+-bound cam
Analyse Complex of iqcg and CA2+-bound cam in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4M1L
- Type
- protein
- Length
- 168 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Calmodulin; Iq domain-containing protein G
- UniProt
- P62158, Q9H095
- Ligands
- CA, SO4
Structure
x-ray diffraction · 2 distinct chains · 60% helix, 5% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Calmodulin | protein | 145 | 59% helix, 6% strand | P62158 |
| B | Iq domain-containing protein G | protein | 23 | 61% helix, 0% strand | Q9H095 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 1711 Ų buried · 17 hydrogen bonds · protein-protein
Compared structures
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 Q9H095
- Elsewhere: RCSB PDB 4M1L · PDBe 4M1L · UniProt P62158 · UniProt Q9H095
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