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

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

The structure of Reduced Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) in A New Crystal Form, PDB code: 1yjk 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)	48.22 / 2.00
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	59.146, 66.335, 69.917, 90.00, 90.00, 90.00
R / Rfree (%)	19.6 / 26

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

Copper binding site 1 out of 2 in the Reduced 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 Reduced Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) in A New Crystal Form within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu357 b:51.3 occ:1.00 ND1 A:HIS108 2.0 42.9 1.0 ND1 A:HIS172 2.0 40.1 1.0 ND1 A:HIS107 2.0 43.0 1.0 CE1 A:HIS107 2.8 43.6 1.0 CE1 A:HIS172 2.9 35.9 1.0 CE1 A:HIS108 2.9 42.0 1.0 CG A:HIS108 3.0 36.8 1.0 CG A:HIS107 3.1 39.9 1.0 CG A:HIS172 3.1 31.2 1.0 O A:HOH879 3.4 49.0 1.0 CB A:HIS108 3.4 31.2 1.0 CB A:HIS107 3.6 32.8 1.0 CB A:HIS172 3.6 28.9 1.0 N A:HIS108 3.7 30.5 1.0 NE2 A:HIS107 3.9 46.2 1.0 C A:HIS107 4.0 31.9 1.0 NE2 A:HIS172 4.0 35.6 1.0 NE2 A:HIS108 4.1 41.9 1.0 CD2 A:HIS107 4.1 44.7 1.0 CA A:HIS108 4.1 29.5 1.0 CD2 A:HIS108 4.1 40.6 1.0 CD2 A:HIS172 4.2 34.6 1.0 O A:HIS107 4.4 30.7 1.0 CA A:HIS107 4.4 32.6 1.0 OH A:TYR79 4.6 41.0 1.0 O A:HIS172 4.8 27.4 1.0 CA A:HIS172 5.0 26.2 1.0 C A:HIS108 5.0 28.6 1.0

Copper binding site 2 out of 2 in the Reduced 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 Reduced Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) in A New Crystal Form within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu358 b:49.8 occ:1.00 O A:HOH885 2.0 49.7 1.0 NE2 A:HIS244 2.0 41.6 1.0 NE2 A:HIS242 2.1 33.3 1.0 SD A:MET314 2.2 40.9 1.0 CD2 A:HIS244 2.9 37.8 1.0 CD2 A:HIS242 3.0 31.9 1.0 CE1 A:HIS244 3.0 38.6 1.0 CE1 A:HIS242 3.1 34.2 1.0 CG A:MET314 3.2 38.6 1.0 O A:HOH882 3.6 58.1 1.0 CB A:MET314 3.9 34.1 1.0 CE A:MET314 3.9 44.8 1.0 CG A:HIS244 4.1 36.0 1.0 ND1 A:HIS244 4.1 39.3 1.0 CG A:HIS242 4.2 32.2 1.0 ND1 A:HIS242 4.2 30.1 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