› 1phm

X-ray diffraction
1.9Å resolution

PEPTIDYLGLYCINE ALPHA-HYDROXYLATING MONOOXYGENASE (PHM) FROM RAT

Released:
DOI: 10.2210/pdb1phm/pdb
PDB entry 1phm coloured by chain, front view.
PDB entry 1phm coloured by chain, side view.
PDB entry 1phm coloured by chain, top view.
Source organism: Rattus norvegicus
Primary publication:
Amidation of bioactive peptides: the structure of peptidylglycine alpha-hydroxylating monooxygenase.
Prigge ST, Kolhekar AS, Eipper BA, Mains RE, Amzel LM
Science 278 1300-5 (1997)
PMID: 9360928

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: 310 amino acids
Theoretical weight: 34.58 KDa
Source organism: Rattus norvegicus
Expression system: Cricetulus griseus
UniProt:
  • Canonical: P14925 (Residues: 45-354; Coverage: 33%)
Gene name: Pam
Sequence domains:
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand CU 3 x CU
Ligand AZI 1 x AZI
Ligand GOL 4 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X4A
Spacegroup: P212121
Unit cell:
a: 68.4Å b: 68.66Å c: 81.38Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.196 0.196 0.261
Expression system: Cricetulus griseus

Quick links

Citations

29 review citations

The proprotein convertases.
Steiner DF. (1998)
28 more

24 mentions without citation

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