3dpc

X-ray diffraction
2.3Å resolution

Structure of E.coli Alkaline Phosphatase Mutant in Complex with a Phosphorylated Peptide

Released:

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 trimer (preferred)
PDBe Complex ID:
PDB-CPX-132774 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Alkaline phosphatase Chains: A, B
Molecule details ›
Chains: A, B
Length: 455 amino acids
Theoretical weight: 47.95 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
  • Canonical: P00634 (Residues: 23-471; Coverage: 100%)
Gene names: JW0374, b0383, phoA
Sequence domains: Alkaline phosphatase
Structure domains: Alkaline Phosphatase, subunit A
Phosphorylated Peptide Chain: C
Molecule details ›
Chain: C
Length: 10 amino acids
Theoretical weight: 1.18 KDa
Source organism: Escherichia coli K-12
Expression system: Not provided

Ligands and Environments

2 bound ligands:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU FR-E DW
Spacegroup: P212121
Unit cell:
a: 64.862Å b: 107.74Å c: 148.389Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.234 0.234 0.271
Expression systems:
  • Escherichia coli
  • Not provided