Copper in PDB 8dsl: Peptidylglycine Alpha Hydroxylating Monooxygenase, Q272E

All present enzymatic activity of Peptidylglycine Alpha Hydroxylating Monooxygenase, Q272E:
1.14.17.3; 4.3.2.5;

The structure of Peptidylglycine Alpha Hydroxylating Monooxygenase, Q272E, PDB code: 8dsl was solved by R.J.Arias, N.J.Blackburn, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	38.25 / 2.05
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	39.166, 53.535, 86.139, 85.03, 89.79, 77.62
R / Rfree (%)	19.6 / 23.9

The binding sites of Copper atom in the Peptidylglycine Alpha Hydroxylating Monooxygenase, Q272E (pdb code 8dsl). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 4 binding sites of Copper where determined in the Peptidylglycine Alpha Hydroxylating Monooxygenase, Q272E, PDB code: 8dsl:
Jump to Copper binding site number: 1; 2; 3; 4;

Copper binding site 1 out of 4 in the Peptidylglycine Alpha Hydroxylating Monooxygenase, Q272E


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Peptidylglycine Alpha Hydroxylating Monooxygenase, Q272E within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu401 b:71.1 occ:1.00 NE2 A:HIS242 1.9 71.5 1.0 NE2 A:HIS244 2.2 69.1 1.0 SD A:MET314 2.3 78.7 1.0 CE1 A:HIS242 2.8 69.6 1.0 CE1 A:HIS244 3.0 67.2 1.0 CD2 A:HIS242 3.0 65.0 1.0 O A:HOH569 3.1 69.7 1.0 CD2 A:HIS244 3.2 66.5 1.0 CG A:MET314 3.4 65.9 1.0 CB A:MET314 3.8 58.8 1.0 ND1 A:HIS242 4.0 63.8 1.0 CE A:MET314 4.0 82.2 1.0 CG A:HIS242 4.1 58.9 1.0 ND1 A:HIS244 4.1 69.9 1.0 CG A:HIS244 4.3 58.4 1.0 O A:GLY308 4.9 103.0 1.0

Copper binding site 2 out of 4 in the Peptidylglycine Alpha Hydroxylating Monooxygenase, Q272E


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Peptidylglycine Alpha Hydroxylating Monooxygenase, Q272E within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu402 b:94.6 occ:1.00 ND1 A:HIS108 2.0 68.7 1.0 ND1 A:HIS107 2.0 81.1 1.0 ND1 A:HIS172 2.1 68.1 1.0 CE1 A:HIS108 2.8 66.2 1.0 CE1 A:HIS172 3.0 61.1 1.0 CG A:HIS107 3.0 69.0 1.0 CE1 A:HIS107 3.0 79.1 1.0 CG A:HIS108 3.1 53.0 1.0 CG A:HIS172 3.1 53.2 1.0 CB A:HIS107 3.3 47.2 1.0 CB A:HIS172 3.5 43.2 1.0 N A:HIS108 3.6 36.6 1.0 CB A:HIS108 3.6 42.0 1.0 C A:HIS107 3.7 37.2 1.0 NE2 A:HIS108 4.0 65.3 1.0 CD2 A:HIS107 4.1 74.2 1.0 CA A:HIS107 4.1 39.3 1.0 NE2 A:HIS107 4.1 76.9 1.0 CD2 A:HIS108 4.1 59.1 1.0 NE2 A:HIS172 4.1 58.2 1.0 CA A:HIS108 4.1 38.6 1.0 CD2 A:HIS172 4.2 57.1 1.0 O A:HIS107 4.3 36.9 1.0 O A:HIS172 4.8 32.7 1.0 CA A:HIS172 4.9 35.8 1.0 OH A:TYR79 5.0 63.3 1.0

Copper binding site 3 out of 4 in the Peptidylglycine Alpha Hydroxylating Monooxygenase, Q272E


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 3 of Peptidylglycine Alpha Hydroxylating Monooxygenase, Q272E within 5.0Å range: probe atom residue distance (Å) B Occ B:Cu401 b:86.8 occ:1.00 ND1 B:HIS108 2.0 59.0 1.0 ND1 B:HIS107 2.0 85.4 1.0 ND1 B:HIS172 2.1 60.5 1.0 CE1 B:HIS108 2.8 58.4 1.0 CG B:HIS107 2.9 68.9 1.0 CE1 B:HIS172 2.9 60.8 1.0 CB B:HIS107 3.1 55.3 1.0 CG B:HIS108 3.1 48.6 1.0 CE1 B:HIS107 3.1 78.6 1.0 CG B:HIS172 3.2 47.0 1.0 N B:HIS108 3.5 40.3 1.0 CB B:HIS108 3.6 41.9 1.0 C B:HIS107 3.6 49.0 1.0 CB B:HIS172 3.6 39.5 1.0 NE2 B:HIS108 3.9 55.7 1.0 CA B:HIS107 3.9 47.1 1.0 CD2 B:HIS107 4.1 73.5 1.0 CD2 B:HIS108 4.1 55.5 1.0 NE2 B:HIS172 4.1 56.3 1.0 CA B:HIS108 4.1 39.1 1.0 O B:HIS107 4.1 44.5 1.0 NE2 B:HIS107 4.2 79.7 1.0 CD2 B:HIS172 4.2 53.3 1.0 O B:HIS172 4.7 38.8 1.0 N B:HIS107 5.0 38.6 1.0 CA B:HIS172 5.0 36.1 1.0 OH B:TYR79 5.0 55.9 1.0

Copper binding site 4 out of 4 in the Peptidylglycine Alpha Hydroxylating Monooxygenase, Q272E


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 4 of Peptidylglycine Alpha Hydroxylating Monooxygenase, Q272E within 5.0Å range: probe atom residue distance (Å) B Occ B:Cu402 b:77.0 occ:1.00 NE2 B:HIS242 2.0 72.4 1.0 NE2 B:HIS244 2.0 72.5 1.0 SD B:MET314 2.3 76.3 1.0 CE1 B:HIS244 2.8 70.5 1.0 CD2 B:HIS242 3.0 64.0 1.0 CD2 B:HIS244 3.1 68.3 1.0 CE1 B:HIS242 3.1 67.2 1.0 O B:HOH551 3.3 58.8 1.0 CG B:MET314 3.5 67.4 1.0 CB B:MET314 3.8 63.1 1.0 CE B:MET314 3.9 70.9 1.0 ND1 B:HIS244 3.9 67.3 1.0 CG B:HIS244 4.0 66.2 1.0 CG B:HIS242 4.1 61.1 1.0 ND1 B:HIS242 4.1 64.3 1.0 O B:GLY308 4.6 117.1 1.0 O B:THR243 4.9 66.0 1.0

R.J.Arias, E.F.Welch, N.J.Blackburn. New Structures Reveal Flexible Dynamics Between the Subdomains of Peptidylglycine Monooxygenase. Implications For An Open to Closed Mechanism. Protein Sci. E4615 2023.
ISSN: ESSN 1469-896X
PubMed: 36880254
DOI: 10.1002/PRO.4615