› 1yjl

X-ray diffraction
2.4Å resolution

Reduced Peptidylglycine alpha-Hydroxylating Monooxygenase in a new crystal form

Released:
DOI: 10.2210/pdb1yjl/pdb
PDB entry 1yjl coloured by chain, front view.
PDB entry 1yjl coloured by chain, side view.
PDB entry 1yjl coloured by chain, top view.
Source organism: Rattus norvegicus
Primary publication:
The catalytic copper of peptidylglycine alpha-hydroxylating monooxygenase also plays a critical structural role.
Siebert X, Eipper BA, Mains RE, Prigge ST, Blackburn NJ, Amzel LM
Biophys J 89 3312-9 (2005)
PMID: 16100265

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:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-147156 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peptidylglycine alpha-amidating monooxygenase Chain: A
Molecule details ›
Chain: A
Length: 306 amino acids
Theoretical weight: 34.14 KDa
Source organism: Rattus norvegicus
Expression system: Cricetulus griseus
UniProt:
  • Canonical: P14925 (Residues: 50-355; Coverage: 32%)
Gene name: Pam
Sequence domains:
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X25
Spacegroup: P212121
Unit cell:
a: 59.764Å b: 66.019Å c: 69.526Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.209 0.206 0.274
Expression system: Cricetulus griseus

Quick links

Citations

2 review citations

60 YEARS OF POMC: From POMC and α-MSH to PAM, molecular oxygen, copper, and vitamin C.
Kumar et al. (2016)
1 more

2 mentions without citation

Copper active sites in biology.
Solomon et al. (2014)
1 more