1yrt

X-ray diffraction
2.1Å resolution

Crystal Structure analysis of the adenylyl cyclaes catalytic domain of adenylyl cyclase toxin of Bordetella pertussis in presence of c-terminal calmodulin

Released:

Function and Biology Details

Reaction catalysed:
ATP = 3',5'-cyclic AMP + diphosphate
Biochemical function:
Biological process:
  • not assigned
Cellular component:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
PDBe Complex ID:
PDB-CPX-143620 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Calmodulin-sensitive adenylate cyclase Chain: A
Molecule details ›
Chain: A
Length: 364 amino acids
Theoretical weight: 39.43 KDa
Source organism: Bordetella pertussis
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P0DKX7 (Residues: 1-364; Coverage: 21%)
Gene names: BP0760, cya, cyaA
Sequence domains: Anthrax toxin LF subunit
Structure domains:
Calmodulin-1 Chain: B
Molecule details ›
Chain: B
Length: 74 amino acids
Theoretical weight: 8.55 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P0DP23 (Residues: 76-149; Coverage: 50%)
Gene names: CALM, CALM1, CAM, CAM1
Sequence domains: EF-hand domain pair
Structure domains: EF-hand

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 14-ID-B
Spacegroup: P41212
Unit cell:
a: 79.362Å b: 79.362Å c: 139.211Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.24 0.22 0.27
Expression systems:
  • Escherichia coli BL21(DE3)
  • Escherichia coli