› 1yip

X-ray diffraction
2.2Å resolution

Oxidized Peptidylglycine Alpha-Hydroxylating Monooxygenase (PHM) in a New Crystal Form

Released:
DOI: 10.2210/pdb1yip/pdb
PDB entry 1yip coloured by chain, front view.
PDB entry 1yip coloured by chain, side view.
PDB entry 1yip 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: 311 amino acids
Theoretical weight: 34.67 KDa
Source organism: Rattus norvegicus
Expression system: Cricetulus griseus
UniProt:
  • Canonical: P14925 (Residues: 45-355; Coverage: 33%)
Gene name: Pam
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand CU 2 x CU
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P212121
Unit cell:
a: 58.523Å b: 65.683Å c: 69.871Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.192 0.19 0.239
Expression system: Cricetulus griseus

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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

3 mentions without citation

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