Research workbench
Structure of MG2+ bound N-terminal domain of calmodulin
Analyse Structure of MG2+ bound N-terminal domain of calmodulin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3UCW
- Type
- protein
- Length
- 305 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Calmodulin
- UniProt
- P62158
- Ligands
- MG
- Pockets
- 5 · best druggability 0.50
Structure
x-ray diffraction · 4 distinct chains · 61% helix, 8% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Calmodulin | protein | 74 | 61% helix, 8% strand | P62158 |
| B | Calmodulin | protein | 77 | 61% helix, 8% strand | P62158 |
| C | Calmodulin | protein | 76 | 61% helix, 8% strand | P62158 |
| D | Calmodulin | protein | 78 | 60% helix, 8% strand | P62158 |
Ligands and binding sites
- MG · Magnesium ion · metal · 10 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 66 | 0.50 | 0.85 | 18 | empty |
| 2 | 73 | 0.36 | 0.77 | 13 | empty |
| 3 | 81 | 0.36 | 0.76 | 13 | empty |
| 4 | 67 | 0.34 | 0.77 | 10 | empty |
| 5 | 70 | 0.30 | 0.74 | 21 | empty |
Interfaces
3 interfaces between chains.
- A–B · 709 Ų buried · 7 hydrogen bonds · protein-protein
- C–D · 386 Ų buried · 2 hydrogen bonds · protein-protein
- A–D · 285 Ų buried · 5 hydrogen bonds · protein-protein
Compared structures
- 3UCW · Structure of MG2+ bound N-Terminal domain of Calmodulin · 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 P62158
- Elsewhere: RCSB PDB 3UCW · PDBe 3UCW · UniProt P62158
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