Copper in PDB 1phm: Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) From Rat

All present enzymatic activity of Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) From Rat:
1.14.17.3;

The structure of Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) From Rat, PDB code: 1phm 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)	6.00 / 1.90
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	68.400, 68.660, 81.380, 90.00, 90.00, 90.00
R / Rfree (%)	19.6 / 26.1

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

Copper binding site 1 out of 3 in the Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) From Rat


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 (Phm) From Rat within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu357 b:52.1 occ:1.00 ND1 A:HIS107 1.9 59.6 1.0 ND1 A:HIS108 1.9 40.6 1.0 ND1 A:HIS172 2.3 59.4 1.0 CG A:HIS108 2.9 35.6 1.0 CG A:HIS107 2.9 57.7 1.0 CE1 A:HIS108 2.9 36.5 1.0 CE1 A:HIS107 2.9 60.6 1.0 CE1 A:HIS172 3.2 59.2 1.0 CB A:HIS107 3.3 50.5 1.0 CB A:HIS108 3.3 38.6 1.0 CG A:HIS172 3.4 58.9 1.0 N A:HIS108 3.5 42.4 1.0 C A:HIS107 3.7 46.4 1.0 CB A:HIS172 3.8 49.8 1.0 CA A:HIS108 4.0 38.9 1.0 O A:HOH438 4.0 53.8 1.0 NE2 A:HIS108 4.1 39.3 1.0 CD2 A:HIS108 4.1 35.8 1.0 NE2 A:HIS107 4.1 62.3 1.0 CD2 A:HIS107 4.1 58.9 1.0 CA A:HIS107 4.1 47.8 1.0 O A:HIS107 4.1 46.5 1.0 NE2 A:HIS172 4.4 62.8 1.0 CD2 A:HIS172 4.5 60.7 1.0 OH A:TYR79 4.7 55.3 1.0 C A:HIS108 4.9 38.7 1.0 O A:HOH588 4.9 72.1 1.0 O A:HIS108 4.9 39.5 1.0

Copper binding site 2 out of 3 in the Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) From Rat


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 (Phm) From Rat within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu358 b:35.2 occ:1.00 NE2 A:HIS242 1.9 27.9 1.0 NE2 A:HIS244 2.1 27.1 1.0 O A:HOH360 2.3 48.7 1.0 SD A:MET314 2.4 32.9 1.0 CE1 A:HIS242 2.9 26.4 1.0 CD2 A:HIS242 2.9 28.6 1.0 CD2 A:HIS244 3.0 23.8 1.0 CE1 A:HIS244 3.1 24.8 1.0 CG A:MET314 3.3 28.4 1.0 CE A:MET314 3.6 34.7 1.0 CB A:MET314 3.7 27.8 1.0 ND1 A:HIS242 4.1 29.1 1.0 CG A:HIS242 4.1 28.5 1.0 CG A:HIS244 4.2 25.7 1.0 ND1 A:HIS244 4.2 26.5 1.0 O A:HOH594 4.5 53.0 1.0 O A:GLY307 4.9 33.7 1.0

Copper binding site 3 out of 3 in the Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) From Rat


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 (Phm) From Rat within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu359 b:34.1 occ:1.00 N1 A:AZI361 1.8 36.1 1.0 O A:HOH363 2.0 30.2 1.0 NE2 A:HIS235 2.1 30.7 1.0 O1 A:GOL362 2.3 42.4 1.0 O2 A:GOL362 2.3 51.2 1.0 C1 A:GOL362 2.8 50.2 1.0 N2 A:AZI361 2.8 52.3 1.0 C2 A:GOL362 2.9 57.1 1.0 CD2 A:HIS235 2.9 28.6 1.0 CE1 A:HIS235 3.2 31.4 1.0 N3 A:AZI361 4.0 50.4 1.0 CB A:ASP282 4.1 33.1 1.0 CG A:HIS235 4.1 32.8 1.0 ND1 A:HIS235 4.2 31.6 1.0 C3 A:GOL362 4.3 64.2 1.0 OD1 A:ASP282 4.4 33.0 1.0 O A:HOH424 4.5 44.0 1.0 O A:HOH370 4.5 43.6 1.0 CG A:ASP282 4.5 37.4 1.0 O A:HOH525 4.6 65.7 1.0

S.T.Prigge, A.S.Kolhekar, B.A.Eipper, R.E.Mains, L.M.Amzel. Amidation of Bioactive Peptides: the Structure of Peptidylglycine Alpha-Hydroxylating Monooxygenase. Science V. 278 1300 1997.
ISSN: ISSN 0036-8075
PubMed: 9360928
DOI: 10.1126/SCIENCE.278.5341.1300