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Copper in PDB 3mih: Oxidized (CU2+) Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) with Bound Azide, Obtained in the Presence of Substrate

Enzymatic activity of Oxidized (CU2+) Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) with Bound Azide, Obtained in the Presence of Substrate

All present enzymatic activity of Oxidized (CU2+) Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) with Bound Azide, Obtained in the Presence of Substrate:
1.14.17.3;

Protein crystallography data

The structure of Oxidized (CU2+) Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) with Bound Azide, Obtained in the Presence of Substrate, PDB code: 3mih was solved by 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) 52.00 / 2.74
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 68.110, 68.800, 79.791, 90.00, 90.00, 90.00
R / Rfree (%) 23.7 / 29.6

Copper Binding Sites:

The binding sites of Copper atom in the Oxidized (CU2+) Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) with Bound Azide, Obtained in the Presence of Substrate (pdb code 3mih). 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 Azide, Obtained in the Presence of Substrate, PDB code: 3mih:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in 3mih

Go back to Copper Binding Sites List in 3mih
Copper binding site 1 out of 2 in the Oxidized (CU2+) Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) with Bound Azide, Obtained in the Presence of Substrate


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 Azide, Obtained in the Presence of Substrate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu357

b:0.6
occ:1.00
 ND1 A:HIS108 2.1 82.2 1.0
ND1 A:HIS107 2.3 83.6 1.0
ND1 A:HIS172 2.4 83.0 1.0
CG A:HIS108 3.0 82.4 1.0
CG A:HIS107 3.0 83.3 1.0
CE1 A:HIS107 3.1 83.6 1.0
CE1 A:HIS108 3.1 82.0 1.0
CG A:HIS172 3.1 82.8 1.0
CE1 A:HIS172 3.2 83.2 1.0
CB A:HIS108 3.3 82.5 1.0
CB A:HIS107 3.4 83.1 1.0
CB A:HIS172 3.4 82.5 1.0
N A:HIS108 3.5 82.7 1.0
CA A:HIS108 4.0 82.5 1.0
C A:HIS107 4.0 82.9 1.0
NE2 A:HIS107 4.0 83.7 1.0
CD2 A:HIS107 4.0 83.4 1.0
CD2 A:HIS172 4.1 82.9 1.0
NE2 A:HIS172 4.1 83.1 1.0
CD2 A:HIS108 4.1 82.2 1.0
NE2 A:HIS108 4.1 82.0 1.0
CA A:HIS107 4.3 83.1 1.0
OH A:TYR79 4.4 84.3 1.0
O A:HIS107 4.7 82.8 1.0
CA A:HIS172 4.9 82.5 1.0
C A:HIS108 4.9 82.4 1.0
O A:HIS172 4.9 82.9 1.0
O A:HIS108 4.9 82.4 1.0

Copper binding site 2 out of 2 in 3mih

Go back to Copper Binding Sites List in 3mih
Copper binding site 2 out of 2 in the Oxidized (CU2+) Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) with Bound Azide, Obtained in the Presence of Substrate


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 Azide, Obtained in the Presence of Substrate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu358

b:94.3
occ:1.00
 NE2 A:HIS242 1.9 81.7 1.0
N1 A:AZI3 2.0 0.8 1.0
NE2 A:HIS244 2.2 83.7 1.0
SD A:MET314 2.6 82.9 1.0
CD2 A:HIS242 2.9 82.0 1.0
N2 A:AZI3 2.9 0.9 1.0
CE1 A:HIS242 2.9 81.7 1.0
CD2 A:HIS244 3.1 83.4 1.0
CE1 A:HIS244 3.2 83.5 1.0
CG A:MET314 3.9 82.9 1.0
CE A:MET314 3.9 83.7 1.0
N3 A:AZI3 4.0 0.8 1.0
CB A:MET314 4.0 82.8 1.0
ND1 A:HIS242 4.0 81.6 1.0
CG A:HIS242 4.0 82.0 1.0
CG A:HIS244 4.2 83.2 1.0
ND1 A:HIS244 4.3 83.6 1.0

Reference:

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
Page generated: Fri Sep 4 08:08:54 2020
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