Copper in PDB 3phm: Reduced (Cu+) Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm)

All present enzymatic activity of Reduced (Cu+) Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm):
1.14.17.3;

The structure of Reduced (Cu+) Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm), PDB code: 3phm was solved by S.T.Prigge, L.M.Amzel, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	10.00 / 2.10
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	69.519, 68.770, 82.417, 90.00, 90.00, 90.00
R / Rfree (%)	20 / 25.7

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

Copper binding site 1 out of 2 in the Reduced (Cu+) Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm)


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) within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu357 b:55.5 occ:1.00 ND1 A:HIS108 2.0 47.6 1.0 ND1 A:HIS172 2.1 48.9 1.0 ND1 A:HIS107 2.2 58.7 1.0 CG A:HIS108 2.9 38.3 1.0 CE1 A:HIS107 3.0 57.8 1.0 CG A:HIS172 3.1 48.5 1.0 CG A:HIS107 3.1 54.9 1.0 CE1 A:HIS108 3.1 42.8 1.0 CE1 A:HIS172 3.1 45.6 1.0 CB A:HIS108 3.2 41.6 1.0 CB A:HIS172 3.4 45.3 1.0 CB A:HIS107 3.5 49.3 1.0 N A:HIS108 3.5 44.2 1.0 C A:HIS107 3.9 46.6 1.0 CA A:HIS108 3.9 41.7 1.0 NE2 A:HIS107 4.1 58.1 1.0 CD2 A:HIS108 4.1 42.7 1.0 CD2 A:HIS107 4.2 56.9 1.0 NE2 A:HIS108 4.2 45.9 1.0 CD2 A:HIS172 4.3 49.2 1.0 NE2 A:HIS172 4.3 45.2 1.0 CA A:HIS107 4.3 47.4 1.0 OH A:TYR79 4.4 61.9 1.0 O A:HOH618 4.4 42.4 1.0 O A:HIS107 4.4 46.0 1.0 O A:HOH438 4.7 56.1 1.0 C A:HIS108 4.7 40.0 1.0 CA A:HIS172 4.8 43.6 1.0 O A:HIS108 4.8 41.4 1.0 O A:HIS172 4.9 42.9 1.0 CZ A:TYR79 4.9 57.6 1.0

Copper binding site 2 out of 2 in the Reduced (Cu+) Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm)


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) within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu358 b:41.9 occ:1.00 O A:HOH705 1.9 47.1 1.0 NE2 A:HIS242 2.1 26.8 1.0 NE2 A:HIS244 2.2 30.5 1.0 SD A:MET314 2.5 36.4 1.0 CE1 A:HIS242 3.0 20.9 1.0 CD2 A:HIS242 3.1 24.2 1.0 CD2 A:HIS244 3.1 25.5 1.0 CE1 A:HIS244 3.3 22.8 1.0 CE A:MET314 3.5 32.0 1.0 CG A:MET314 3.6 31.3 1.0 CB A:MET314 3.9 30.4 1.0 ND1 A:HIS242 4.2 25.3 1.0 CG A:HIS242 4.2 25.8 1.0 CG A:HIS244 4.3 28.3 1.0 ND1 A:HIS244 4.4 27.8 1.0 O A:GLY307 4.9 32.9 1.0 O A:GLY308 4.9 45.5 1.0

S.T.Prigge, A.S.Kolhekar, B.A.Eipper, R.E.Mains, L.M.Amzel. Substrate-Mediated Electron Transfer in Peptidylglycine Alpha-Hydroxylating Monooxygenase. Nat.Struct.Biol. V. 6 976 1999.
ISSN: ISSN 1072-8368
PubMed: 10504734
DOI: 10.1038/13351