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Copper in PDB 3mic: Oxidized (CU2+) Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) with Bound Azide Obtained By Co-Crystallization

Enzymatic activity of Oxidized (CU2+) Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) with Bound Azide Obtained By Co-Crystallization

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

Protein crystallography data

The structure of Oxidized (CU2+) Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) with Bound Azide Obtained By Co-Crystallization, PDB code: 3mic 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 / 2.42
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 68.454, 68.579, 81.409, 90.00, 90.00, 90.00
R / Rfree (%) 19.6 / 26.4

Copper Binding Sites:

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

Copper binding site 1 out of 2 in 3mic

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


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 Co-Crystallization within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu357

b:52.8
occ:1.00
ND1 A:HIS172 2.1 46.5 1.0
ND1 A:HIS107 2.1 47.7 1.0
ND1 A:HIS108 2.1 47.1 1.0
CE1 A:HIS172 2.9 44.8 1.0
CG A:HIS107 3.0 45.9 1.0
CG A:HIS108 3.1 44.8 1.0
CE1 A:HIS108 3.1 46.1 1.0
CE1 A:HIS107 3.1 47.0 1.0
CG A:HIS172 3.2 44.2 1.0
CB A:HIS107 3.2 45.1 1.0
CB A:HIS108 3.3 44.3 1.0
N A:HIS108 3.3 44.4 1.0
CB A:HIS172 3.6 43.2 1.0
C A:HIS107 3.6 44.7 1.0
O A:HOH459 3.8 49.3 1.0
CA A:HIS108 3.9 44.1 1.0
CA A:HIS107 4.0 44.9 1.0
NE2 A:HIS172 4.1 44.7 1.0
CD2 A:HIS107 4.1 46.4 1.0
O A:HIS107 4.2 44.6 1.0
NE2 A:HIS108 4.2 45.9 1.0
CD2 A:HIS108 4.2 45.1 1.0
NE2 A:HIS107 4.2 46.6 1.0
O A:HOH421 4.2 36.9 1.0
CD2 A:HIS172 4.2 44.6 1.0
O A:HIS172 4.7 42.7 1.0
OH A:TYR79 4.8 41.1 1.0
C A:HIS108 4.8 43.8 1.0
O A:HIS108 4.9 43.6 1.0
CA A:HIS172 4.9 42.9 1.0

Copper binding site 2 out of 2 in 3mic

Go back to Copper Binding Sites List in 3mic
Copper binding site 2 out of 2 in the Oxidized (CU2+) Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) with Bound Azide Obtained By Co-Crystallization


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 Co-Crystallization within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu358

b:42.0
occ:1.00
N1 A:AZI1 2.0 47.8 1.0
NE2 A:HIS242 2.1 41.5 1.0
NE2 A:HIS244 2.1 41.3 1.0
SD A:MET314 2.5 41.7 1.0
N2 A:AZI1 2.7 51.7 1.0
CD2 A:HIS244 3.0 40.5 1.0
CE1 A:HIS242 3.0 40.3 1.0
CD2 A:HIS242 3.1 39.8 1.0
CE1 A:HIS244 3.2 39.8 1.0
CG A:MET314 3.6 41.3 1.0
N3 A:AZI1 3.6 51.1 1.0
CE A:MET314 3.8 40.2 1.0
CB A:MET314 3.8 41.7 1.0
NA A:NA360 3.8 55.2 1.0
ND1 A:HIS242 4.2 40.2 1.0
CG A:HIS244 4.2 40.8 1.0
CG A:HIS242 4.2 40.6 1.0
ND1 A:HIS244 4.2 40.8 1.0
O A:HOH465 4.4 54.4 1.0
OE2 A:GLU128 4.8 53.4 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 08:08:40 2020
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