Copper in PDB 3mlj: Reduced (Cu+) Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) with Bound Carbon Monooxide (Co)

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

The structure of Reduced (Cu+) Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) with Bound Carbon Monooxide (Co), PDB code: 3mlj was solved by S.T.Prigge, E.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)	53.00 / 2.15
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	69.226, 68.860, 81.744, 90.00, 90.00, 90.00
R / Rfree (%)	21 / 26

The structure of Reduced (Cu+) 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 Reduced (Cu+) Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) with Bound Carbon Monooxide (Co) (pdb code 3mlj). 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 (Cu+) Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) with Bound Carbon Monooxide (Co), PDB code: 3mlj:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in the Reduced (Cu+) 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 Reduced (Cu+) Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) with Bound Carbon Monooxide (Co) within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu357 b:55.5 occ:0.70 ND1 A:HIS107 2.0 53.0 1.0 ND1 A:HIS108 2.0 53.5 1.0 ND1 A:HIS172 2.0 51.5 1.0 CE1 A:HIS107 2.8 53.2 1.0 CE1 A:HIS172 2.9 50.7 1.0 CG A:HIS108 2.9 51.3 1.0 CE1 A:HIS108 3.0 53.5 1.0 CG A:HIS107 3.1 51.9 1.0 CG A:HIS172 3.1 49.8 1.0 CB A:HIS108 3.2 50.2 1.0 O A:HOH414 3.3 65.7 1.0 N A:HIS108 3.5 50.1 1.0 CB A:HIS172 3.5 48.9 1.0 CB A:HIS107 3.6 50.8 1.0 C A:HIS107 3.8 50.4 1.0 NE2 A:HIS107 3.9 53.0 1.0 CA A:HIS108 3.9 49.8 1.0 NE2 A:HIS172 4.0 50.8 1.0 CD2 A:HIS107 4.1 52.6 1.0 CD2 A:HIS108 4.1 52.9 1.0 NE2 A:HIS108 4.1 53.8 1.0 O A:HOH436 4.1 76.0 1.0 CD2 A:HIS172 4.2 50.5 1.0 O A:HIS107 4.3 50.3 1.0 O A:HOH421 4.3 60.2 1.0 CA A:HIS107 4.3 50.7 1.0 OH A:TYR79 4.6 54.0 1.0 C A:HIS108 4.8 49.4 1.0 CA A:HIS172 5.0 48.6 1.0

Copper binding site 2 out of 2 in the Reduced (Cu+) 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 Reduced (Cu+) Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) with Bound Carbon Monooxide (Co) within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu358 b:51.3 occ:1.00 C A:CMO1 1.8 53.2 1.0 NE2 A:HIS242 2.0 48.5 1.0 NE2 A:HIS244 2.0 49.0 1.0 O A:CMO1 2.5 54.2 1.0 SD A:MET314 2.6 53.3 1.0 CD2 A:HIS244 2.9 47.0 1.0 CD2 A:HIS242 3.0 48.1 1.0 CE1 A:HIS242 3.0 46.8 1.0 CE1 A:HIS244 3.1 46.6 1.0 CG A:MET314 3.6 47.6 1.0 CE A:MET314 3.9 52.7 1.0 CB A:MET314 3.9 45.9 1.0 CG A:HIS244 4.1 47.4 1.0 ND1 A:HIS242 4.1 48.2 1.0 ND1 A:HIS244 4.2 46.5 1.0 CG A:HIS242 4.2 47.0 1.0 O A:ACT360 4.8 52.2 1.0 O A:GLY308 4.9 48.6 1.0 O A:GLY307 5.0 46.4 1.0

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