3bdg

X-ray diffraction
1.4Å resolution

Crystal structure of wild-type/T155V mixed dimer of E. coli alkaline phosphatase

Released:
Source organism: Escherichia coli
Entry authors: Grigg JC, Murphy ME

Function and Biology Details

Reaction catalysed:
A phosphate monoester + H(2)O = an alcohol + phosphate
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-132763 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Alkaline phosphatase Chain: A
Molecule details ›
Chain: A
Length: 458 amino acids
Theoretical weight: 48.32 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P00634 (Residues: 22-471; Coverage: 100%)
Gene names: JW0374, b0383, phoA
Sequence domains: Alkaline phosphatase
Structure domains: Alkaline Phosphatase, subunit A
Alkaline phosphatase Chain: B
Molecule details ›
Chain: B
Length: 458 amino acids
Theoretical weight: 48.27 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P00634 (Residues: 22-471; Coverage: 100%)
Gene names: JW0374, b0383, phoA
Sequence domains: Alkaline phosphatase
Structure domains: Alkaline Phosphatase, subunit A

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL9-1
Spacegroup: P21
Unit cell:
a: 55.32Å b: 103.35Å c: 88.286Å
α: 90° β: 105.78° γ: 90°
R-values:
R R work R free
0.161 0.16 0.18
Expression system: Escherichia coli