Research workbench
2.5 ångström crystal structure of the N97S cam mutant
Analyse 2.5 ångström crystal structure of the N97S cam mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6DAH
- Type
- protein
- Length
- 579 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Calmodulin-1
- UniProt
- P0DP23
- Ligands
- CA
- Pockets
- 5 · best druggability 0.45
Structure
x-ray diffraction · 4 distinct chains · 60% helix, 4% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Calmodulin-1 | protein | 148 | 59% helix, 5% strand | P0DP23 |
| B | Calmodulin-1 | protein | 135 | 59% helix, 4% strand | P0DP23 |
| C | Calmodulin-1 | protein | 149 | 62% helix, 3% strand | P0DP23 |
| D | Calmodulin-1 | protein | 147 | 63% helix, 4% strand | P0DP23 |
Ligands and binding sites
- CA · Calcium ion · metal · 16 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 | 80 | 0.45 | 0.79 | 13 | empty |
| 2 | 181 | 0.44 | 0.74 | 29 | empty |
| 3 | 68 | 0.43 | 0.80 | 11 | empty |
| 4 | 54 | 0.40 | 0.80 | 11 | empty |
| 5 | 69 | 0.38 | 0.78 | 12 | empty |
Interfaces
5 interfaces between chains.
- C–D · 390 Ų buried · 6 hydrogen bonds · protein-protein
- B–D · 251 Ų buried · 3 hydrogen bonds · protein-protein
- A–C · 203 Ų buried · 5 hydrogen bonds · protein-protein
- A–B · 152 Ų buried · 1 hydrogen bond · protein-protein
- A–D · 139 Ų buried · 3 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 P0DP23
- Elsewhere: RCSB PDB 6DAH · PDBe 6DAH · UniProt P0DP23
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