Research workbench
Cam-P458 complex (crystal form 1)
Analyse Cam-P458 complex (crystal form 1) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6YNU
- Type
- protein
- Length
- 340 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Calmodulin-1; Bifunctional adenylate cyclase TOXIN/HEMOLYSIN cyaa
- UniProt
- P0DP23, A0A380ZZA1
- Ligands
- CA
- Pockets
- 1 · best druggability 0.34
Structure
x-ray diffraction · 2 distinct chains · 66% helix, 4% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Calmodulin-1 | protein | 146 | 63% helix, 4% strand | P0DP23 |
| B, D | Bifunctional adenylate cyclase TOXIN/HEMOLYSIN cyaa | protein | 24 | 88% helix, 0% strand | A0A380ZZA1 |
Ligands and binding sites
- CA · Calcium ion · metal · 9 copies · chains A, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 58 | 0.34 | 0.77 | 14 | empty |
Interfaces
2 interfaces between chains.
- A–B · 629 Ų buried · 3 hydrogen bonds · protein-protein
- C–D · 609 Ų buried · 1 hydrogen bond · 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
- Every structure of UniProt A0A380ZZA1
- Elsewhere: RCSB PDB 6YNU · PDBe 6YNU · UniProt P0DP23 · UniProt A0A380ZZA1
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