X-ray diffraction
3.1Å resolution

Reduced (Cu+) peptidylglycine alpha-hydroxylating monooxygenase (PHM) with bound nitrite


Function and Biology Details

Reactions catalysed:
[Peptide]-glycine + 2 ascorbate + O(2) = [peptide]-(2S)-2-hydroxyglycine + 2 monodehydroascorbate + H(2)O
[Peptide]-(2S)-2-hydroxyglycine = [peptide]-amide + glyoxylate
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Peptidylglycine alpha-amidating monooxygenase Chain: A
Molecule details ›
Chain: A
Length: 314 amino acids
Theoretical weight: 35.01 KDa
Source organism: Rattus norvegicus
Expression system: Cricetulus griseus
  • Canonical: P14925 (Residues: 43-356; Coverage: 33%)
Gene name: Pam
Sequence domains:
Structure domains:

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X4C
Spacegroup: P212121
Unit cell:
a: 68.973Å b: 69.317Å c: 81.114Å
α: 90° β: 90° γ: 90°
R R work R free
0.219 0.216 0.282
Expression system: Cricetulus griseus