Research workbench
Crystal structure analysis of the adenylyl cyclaes catalytic domain of adenylyl cyclase toxin of bordetella pertussis in presence of C-terminal calmodulin and 1MM calcium chloride
Analyse Crystal structure analysis of the adenylyl cyclaes catalytic domain of adenylyl… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1YRU
- Type
- protein
- Length
- 420 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Bifunctional hemolysin-adenylate cyclase; Calmodulin
- EC
- 4.6.1.1
- UniProt
- P15318, P62158
- Ligands
- CA
- Pockets
- 3 · best druggability 0.55
Structure
x-ray diffraction · 2 distinct chains · 42% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Bifunctional hemolysin-adenylate cyclase (EC 4.6.1.1) | protein | 351 | 38% helix, 18% strand | P15318 |
| B | Calmodulin | protein | 69 | 59% helix, 3% strand | P62158 |
Ligands and binding sites
- CA · Calcium ion · metal · 2 copies · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 295 | 0.55 | 0.76 | 39 | empty |
| 2 | 97 | 0.38 | 0.76 | 24 | empty |
| 3 | 61 | 0.31 | 0.75 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 1733 Ų buried · 27 hydrogen bonds · protein-protein
Compared structures
- 1YRU · Crystal Structure analysis of the adenylyl cyclaes catalytic domain of adenylyl cyclase… · 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 P15318
- Every structure of UniProt P62158
- Elsewhere: RCSB PDB 1YRU · PDBe 1YRU · UniProt P15318 · UniProt P62158
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