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Copper in PDB 3mie: Oxidized (CU2+) Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) with Bound Azide Obtained By Soaking (50MM NAN3)

Enzymatic activity of Oxidized (CU2+) Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) with Bound Azide Obtained By Soaking (50MM NAN3)

All present enzymatic activity of Oxidized (CU2+) Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) with Bound Azide Obtained By Soaking (50MM NAN3):
1.14.17.3;

Protein crystallography data

The structure of Oxidized (CU2+) Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) with Bound Azide Obtained By Soaking (50MM NAN3), PDB code: 3mie 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) 52.56 / 3.26
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 68.719, 68.991, 81.259, 90.00, 90.00, 90.00
R / Rfree (%) 19.1 / 24

Other elements in 3mie:

The structure of Oxidized (CU2+) Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) with Bound Azide Obtained By Soaking (50MM NAN3) also contains other interesting chemical elements:

Nickel (Ni) 1 atom
Sodium (Na) 1 atom

Copper Binding Sites:

The binding sites of Copper atom in the Oxidized (CU2+) Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) with Bound Azide Obtained By Soaking (50MM NAN3) (pdb code 3mie). 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 By Soaking (50MM NAN3), PDB code: 3mie:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in 3mie

Go back to Copper Binding Sites List in 3mie
Copper binding site 1 out of 2 in the Oxidized (CU2+) Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) with Bound Azide Obtained By Soaking (50MM NAN3)


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 By Soaking (50MM NAN3) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu357

b:84.6
occ:1.00
 ND1 A:HIS108 2.0 71.5 1.0
ND1 A:HIS107 2.5 62.2 1.0
ND1 A:HIS172 2.5 57.6 1.0
CG A:HIS107 2.9 62.3 1.0
CG A:HIS108 2.9 66.6 1.0
CE1 A:HIS108 3.1 69.5 1.0
CE1 A:HIS107 3.2 62.3 1.0
CB A:HIS108 3.2 64.0 1.0
CB A:HIS107 3.3 62.1 1.0
N A:HIS108 3.3 62.7 1.0
CG A:HIS172 3.4 58.2 1.0
CE1 A:HIS172 3.5 57.8 1.0
CB A:HIS172 3.6 58.2 1.0
CD2 A:HIS107 3.7 62.6 1.0
C A:HIS107 3.8 62.4 1.0
NE2 A:HIS107 3.8 62.6 1.0
CA A:HIS108 3.8 63.3 1.0
CD2 A:HIS108 4.1 68.6 1.0
NE2 A:HIS108 4.1 69.7 1.0
CA A:HIS107 4.2 62.2 1.0
O A:HIS107 4.4 62.4 1.0
OH A:TYR79 4.6 61.8 1.0
CD2 A:HIS172 4.6 58.2 1.0
NE2 A:HIS172 4.6 57.9 1.0
C A:HIS108 4.7 62.8 1.0
O A:HIS172 4.8 58.5 1.0
O A:HIS108 4.9 62.7 1.0
CA A:HIS172 4.9 58.2 1.0

Copper binding site 2 out of 2 in 3mie

Go back to Copper Binding Sites List in 3mie
Copper binding site 2 out of 2 in the Oxidized (CU2+) Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) with Bound Azide Obtained By Soaking (50MM NAN3)


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 By Soaking (50MM NAN3) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu358

b:66.0
occ:1.00
 N1 A:AZI1 2.0 71.6 1.0
NE2 A:HIS242 2.1 61.2 1.0
NE2 A:HIS244 2.3 64.1 1.0
SD A:MET314 2.6 65.8 1.0
CD2 A:HIS242 2.9 59.7 1.0
N2 A:AZI1 2.9 74.2 1.0
CD2 A:HIS244 3.0 62.5 1.0
CE1 A:HIS242 3.1 59.1 1.0
CE1 A:HIS244 3.3 63.4 1.0
CE A:MET314 3.9 66.4 1.0
CG A:MET314 4.0 62.6 1.0
N3 A:AZI1 4.0 73.7 1.0
CB A:MET314 4.1 61.6 1.0
CG A:HIS242 4.1 58.9 1.0
ND1 A:HIS242 4.2 58.4 1.0
CG A:HIS244 4.2 61.2 1.0
ND1 A:HIS244 4.3 62.4 1.0
O A:GLY308 4.9 62.7 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: Wed Jul 31 01:19:21 2024

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