Copper in PDB 3mif: Oxidized (CU2+) Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) with Bound Carbon Monooxide (Co)

All present enzymatic activity of Oxidized (CU2+) Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) with Bound Carbon Monooxide (Co):
1.14.17.3;

The structure of Oxidized (CU2+) Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) with Bound Carbon Monooxide (Co), PDB code: 3mif was solved by X.Siebert, E.Chufan, B.A.Eipper, R.E.Mains, L.M.Amzel, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	34.63 / 2.00
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	69.246, 69.715, 83.121, 90.00, 90.00, 90.00
R / Rfree (%)	20.7 / 23.5

The structure of Oxidized (CU2+) Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) with Bound Carbon Monooxide (Co) also contains other interesting chemical elements:

Nickel

(Ni)

1 atom

The binding sites of Copper atom in the Oxidized (CU2+) Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) with Bound Carbon Monooxide (Co) (pdb code 3mif). 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 (CU2+) Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) with Bound Carbon Monooxide (Co), PDB code: 3mif:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in the Oxidized (CU2+) Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) with Bound Carbon Monooxide (Co)


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Oxidized (CU2+) Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) with Bound Carbon Monooxide (Co) within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu357 b:49.1 occ:1.00 ND1 A:HIS107 2.0 44.2 1.0 ND1 A:HIS108 2.0 42.2 1.0 ND1 A:HIS172 2.0 41.6 1.0 CE1 A:HIS172 2.8 40.1 1.0 CE1 A:HIS107 2.9 43.5 1.0 CG A:HIS108 3.0 39.6 1.0 CE1 A:HIS108 3.0 41.0 1.0 CG A:HIS107 3.0 41.6 1.0 CG A:HIS172 3.2 38.6 1.0 CB A:HIS108 3.3 39.0 1.0 CB A:HIS107 3.4 40.4 1.0 N A:HIS108 3.4 39.1 1.0 C A:HIS107 3.7 39.6 1.0 CB A:HIS172 3.7 37.3 1.0 CA A:HIS108 3.9 38.7 1.0 NE2 A:HIS172 4.0 39.6 1.0 NE2 A:HIS107 4.0 43.1 1.0 NE2 A:HIS108 4.1 40.7 1.0 CD2 A:HIS107 4.1 42.6 1.0 O A:HIS107 4.1 39.4 1.0 CD2 A:HIS108 4.1 39.9 1.0 O A:HOH466 4.1 57.0 1.0 CA A:HIS107 4.2 40.1 1.0 O A:HOH386 4.2 45.6 1.0 CD2 A:HIS172 4.2 39.3 1.0 C A:HIS108 4.9 38.3 1.0 O A:HIS172 4.9 37.1 1.0 OH A:TYR79 4.9 44.0 1.0 O A:HOH459 4.9 61.5 1.0 O A:HIS108 5.0 38.2 1.0

Copper binding site 2 out of 2 in the Oxidized (CU2+) Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) with Bound Carbon Monooxide (Co)


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Oxidized (CU2+) Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) with Bound Carbon Monooxide (Co) within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu358 b:35.6 occ:1.00 C A:CMO1 1.8 36.0 0.5 OE2 A:GLU128 1.9 41.9 0.5 NE2 A:HIS242 2.0 38.5 1.0 NE2 A:HIS244 2.0 37.1 1.0 SD A:MET314 2.3 40.0 1.0 O A:CMO1 2.6 36.4 0.5 CD2 A:HIS244 2.9 35.7 1.0 CE1 A:HIS242 3.0 38.2 1.0 CD2 A:HIS242 3.0 37.4 1.0 CE1 A:HIS244 3.1 36.6 1.0 CD A:GLU128 3.1 42.1 0.5 CG A:MET314 3.4 37.4 1.0 CE A:MET314 3.7 40.6 1.0 CB A:MET314 3.7 36.9 1.0 OE1 A:GLU128 3.9 41.9 0.5 CG A:GLU128 4.0 42.1 0.5 CG A:HIS244 4.1 35.6 1.0 ND1 A:HIS242 4.1 38.8 1.0 ND1 A:HIS244 4.1 35.9 1.0 CG A:HIS242 4.2 37.7 1.0 O A:HOH455 4.7 52.9 1.0 O A:GLY307 5.0 37.9 1.0

E.E.Chufan, S.T.Prigge, X.Siebert, B.A.Eipper, R.E.Mains, L.M.Amzel. Differential Reactivity Between the Two Copper Sites of Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) J.Am.Chem.Soc. V. 132 15565 2010.
ISSN: ISSN 0002-7863
PubMed: 20958070
DOI: 10.1021/JA103117R