Copper in PDB 1sdw: Reduced (Cu+) Peptidylglycine Alpha-Hydroxylating Monooxygenase with Bound Peptide and Dioxygen

All present enzymatic activity of Reduced (Cu+) Peptidylglycine Alpha-Hydroxylating Monooxygenase with Bound Peptide and Dioxygen:
1.14.17.3;

The structure of Reduced (Cu+) Peptidylglycine Alpha-Hydroxylating Monooxygenase with Bound Peptide and Dioxygen, PDB code: 1sdw was solved by S.T.Prigge, 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)	19.69 / 1.85
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	69.478, 68.979, 82.108, 90.00, 90.00, 90.00
R / Rfree (%)	19.7 / 22.6

The structure of Reduced (Cu+) Peptidylglycine Alpha-Hydroxylating Monooxygenase with Bound Peptide and Dioxygen also contains other interesting chemical elements:

Nickel	(Ni)	1 atom
Iodine	(I)	8 atoms

The binding sites of Copper atom in the Reduced (Cu+) Peptidylglycine Alpha-Hydroxylating Monooxygenase with Bound Peptide and Dioxygen (pdb code 1sdw). 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 with Bound Peptide and Dioxygen, PDB code: 1sdw:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in the Reduced (Cu+) Peptidylglycine Alpha-Hydroxylating Monooxygenase with Bound Peptide and Dioxygen


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 with Bound Peptide and Dioxygen within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu357 b:52.1 occ:1.00 ND1 A:HIS107 1.8 55.5 1.0 ND1 A:HIS108 2.0 44.8 1.0 ND1 A:HIS172 2.1 53.5 1.0 CE1 A:HIS107 2.8 55.4 1.0 CG A:HIS107 2.9 53.8 1.0 CG A:HIS108 2.9 41.3 1.0 CE1 A:HIS108 3.0 44.4 1.0 CE1 A:HIS172 3.1 53.8 1.0 CG A:HIS172 3.1 54.1 1.0 CB A:HIS108 3.2 41.5 1.0 CB A:HIS107 3.3 51.4 1.0 CB A:HIS172 3.4 48.8 1.0 N A:HIS108 3.5 45.0 1.0 C A:HIS107 3.7 47.3 1.0 NE2 A:HIS107 3.9 57.1 1.0 CA A:HIS108 4.0 42.5 1.0 CD2 A:HIS107 4.0 56.8 1.0 CD2 A:HIS108 4.1 43.4 1.0 O A:HIS107 4.1 47.7 1.0 CA A:HIS107 4.1 49.2 1.0 NE2 A:HIS108 4.1 49.2 1.0 NE2 A:HIS172 4.2 55.0 1.0 CD2 A:HIS172 4.3 52.9 1.0 O A:HOH515 4.3 54.9 1.0 O A:HOH499 4.6 52.2 1.0 C A:HIS108 4.8 39.7 1.0 OH A:TYR79 4.8 67.9 1.0 O A:HIS108 4.8 42.4 1.0 CA A:HIS172 4.9 48.1 1.0 O A:HIS172 5.0 47.1 1.0

Copper binding site 2 out of 2 in the Reduced (Cu+) Peptidylglycine Alpha-Hydroxylating Monooxygenase with Bound Peptide and Dioxygen


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 with Bound Peptide and Dioxygen within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu358 b:34.0 occ:1.00 O1 A:OXY360 2.1 39.9 1.0 NE2 A:HIS242 2.1 28.7 1.0 NE2 A:HIS244 2.1 35.3 1.0 SD A:MET314 2.3 32.7 1.0 O2 A:OXY360 2.8 45.9 1.0 CD2 A:HIS244 3.1 32.0 1.0 CD2 A:HIS242 3.1 30.7 1.0 CE1 A:HIS242 3.1 29.3 1.0 CE1 A:HIS244 3.2 33.9 1.0 CE A:MET314 3.3 37.2 1.0 CG A:MET314 3.4 28.8 1.0 CB A:MET314 3.8 26.8 1.0 CG A:HIS244 4.2 33.6 1.0 ND1 A:HIS244 4.3 33.5 1.0 ND1 A:HIS242 4.3 27.9 1.0 CG A:HIS242 4.3 28.1 1.0 CAT A:IYT701 4.3 40.0 1.0 NT A:IYT701 4.4 38.3 1.0 C A:IYT701 4.6 40.1 1.0 O A:IYT701 4.8 42.1 1.0 CT A:IYT701 4.9 36.2 1.0

S.T.Prigge, B.A.Eipper, R.E.Mains, L.M.Amzel. Dioxygen Binds End-on to Mononuclear Copper in A Precatalytic Enzyme Complex. Science V. 304 864 2004.
ISSN: ISSN 0036-8075
PubMed: 15131304
DOI: 10.1126/SCIENCE.1094583