› 3mig

X-ray diffraction
2.7Å resolution

Oxidized (Cu2+) peptidylglycine alpha-hydroxylating monooxygenase (PHM) with bound nitrite, obtained in the presence of substrate

Released:
DOI: 10.2210/pdb3mig/pdb
PDB entry 3mig coloured by chain, front view.
PDB entry 3mig coloured by chain, side view.
PDB entry 3mig coloured by chain, top view.
Source organism: Rattus norvegicus
Primary publication:
Differential reactivity between two copper sites in peptidylglycine α-hydroxylating monooxygenase.
Chufán EE, Prigge ST, Siebert X, Eipper BA, Mains RE, Amzel LM
J Am Chem Soc 132 15565-72 (2010)
PMID: 20958070

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 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: 314 amino acids
Theoretical weight: 35.01 KDa
Source organism: Rattus norvegicus
Expression system: Cricetulus griseus
UniProt:
  • Canonical: P14925 (Residues: 43-356; Coverage: 33%)
Gene name: Pam
Sequence domains:
Structure domains:

Ligands and Environments

4 bound ligands:
Ligand CU 2 x CU
Ligand NI 1 x NI
Ligand NO2 2 x NO2
Ligand GOL 1 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X4C
Spacegroup: P212121
Unit cell:
a: 68.356Å b: 68.783Å c: 79.979Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.224 0.221 0.272
Expression system: Cricetulus griseus

Quick links

Citations

6 review citations

Protein design: toward functional metalloenzymes.
Yu et al. (2014)
5 more

2 mentions without citation

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