Copper in PDB 1yip: Oxidized Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) in A New Crystal Form

All present enzymatic activity of Oxidized Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) in A New Crystal Form:
1.14.17.3;

The structure of Oxidized Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) in A New Crystal Form, PDB code: 1yip was solved by X.Siebert, B.A.Eipper, R.E.Mains, S.T.Prigge, N.J.Blackburn, L.M.Amzel, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.01 / 2.20
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	58.523, 65.683, 69.871, 90.00, 90.00, 90.00
R / Rfree (%)	19 / 23.9

The binding sites of Copper atom in the Oxidized Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) in A New Crystal Form (pdb code 1yip). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 2 binding sites of Copper where determined in the Oxidized Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) in A New Crystal Form, PDB code: 1yip:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in the Oxidized Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) in A New Crystal Form


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Oxidized Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) in A New Crystal Form within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu357 b:60.9 occ:1.00 ND1 A:HIS107 2.2 50.4 1.0 ND1 A:HIS108 2.2 47.2 1.0 ND1 A:HIS172 2.3 39.3 1.0 CE1 A:HIS172 3.0 38.5 1.0 CG A:HIS107 3.0 46.2 1.0 CG A:HIS108 3.1 43.0 1.0 CB A:HIS107 3.2 45.0 1.0 CE1 A:HIS108 3.2 48.5 1.0 CE1 A:HIS107 3.3 51.5 1.0 CG A:HIS172 3.4 36.8 1.0 CB A:HIS108 3.4 41.1 1.0 N A:HIS108 3.5 41.2 1.0 C A:HIS107 3.8 43.3 1.0 CB A:HIS172 3.9 35.0 1.0 CA A:HIS108 4.0 41.0 1.0 O A:HOH500 4.1 40.8 1.0 CA A:HIS107 4.1 43.9 1.0 NE2 A:HIS172 4.2 38.5 1.0 CD2 A:HIS107 4.2 49.9 1.0 NE2 A:HIS107 4.3 50.1 1.0 O A:HIS107 4.3 43.4 1.0 CD2 A:HIS108 4.3 47.6 1.0 NE2 A:HIS108 4.3 47.9 1.0 CD2 A:HIS172 4.4 37.7 1.0 O A:HIS172 4.8 34.4 1.0 OH A:TYR79 5.0 48.2 1.0 C A:HIS108 5.0 39.3 1.0

Copper binding site 2 out of 2 in the Oxidized Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) in A New Crystal Form


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Oxidized Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) in A New Crystal Form within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu358 b:53.3 occ:1.00 NE2 A:HIS242 2.2 38.0 1.0 NE2 A:HIS244 2.3 48.4 1.0 O A:HOH369 2.4 69.1 1.0 SD A:MET314 2.4 47.9 1.0 O A:HOH368 2.5 49.6 1.0 CD2 A:HIS244 3.1 43.5 1.0 CE1 A:HIS242 3.1 40.2 1.0 CD2 A:HIS242 3.2 39.5 1.0 CE1 A:HIS244 3.4 46.8 1.0 CG A:MET314 3.5 46.3 1.0 CE A:MET314 4.0 49.2 1.0 ND1 A:HIS242 4.3 38.2 1.0 CG A:HIS242 4.3 40.3 1.0 CG A:HIS244 4.3 43.2 1.0 ND1 A:HIS244 4.4 44.3 1.0 O A:HOH516 4.5 61.3 1.0 CB A:MET314 4.9 44.9 1.0

X.Siebert, B.A.Eipper, R.E.Mains, S.T.Prigge, N.J.Blackburn, L.M.Amzel. The Catalytic Copper of Peptidylglycine Alpha-Hydroxylating Monooxygenase Also Plays A Critical Structural Role. Biophys.J. V. 89 3312 2005.
ISSN: ISSN 0006-3495
PubMed: 16100265
DOI: 10.1529/BIOPHYSJ.105.066100