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Copper in PDB 3mid: Oxidized (CU2+) Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) with Bound Azide Obtained By Soaking (100MM NAN3)

Enzymatic activity of Oxidized (CU2+) Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) with Bound Azide Obtained By Soaking (100MM NAN3)

All present enzymatic activity of Oxidized (CU2+) Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) with Bound Azide Obtained By Soaking (100MM NAN3):
1.14.17.3;

Protein crystallography data

The structure of Oxidized (CU2+) Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) with Bound Azide Obtained By Soaking (100MM NAN3), PDB code: 3mid 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) 52.78 / 3.06
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 68.882, 69.258, 81.494, 90.00, 90.00, 90.00
R / Rfree (%) 19.8 / 24.5

Other elements in 3mid:

The structure of Oxidized (CU2+) Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) with Bound Azide Obtained By Soaking (100MM NAN3) also contains other interesting chemical elements:

Nickel (Ni) 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 (100MM NAN3) (pdb code 3mid). 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 (100MM NAN3), PDB code: 3mid:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in 3mid

Go back to Copper Binding Sites List in 3mid
Copper binding site 1 out of 2 in the Oxidized (CU2+) Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) with Bound Azide Obtained By Soaking (100MM 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 (100MM NAN3) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu357

b:67.4
occ:1.00
 ND1 A:HIS108 1.9 60.4 1.0
ND1 A:HIS172 2.1 59.7 1.0
ND1 A:HIS107 2.1 61.3 1.0
CE1 A:HIS107 2.8 60.6 1.0
CE1 A:HIS108 2.8 59.4 1.0
CG A:HIS107 2.9 58.7 1.0
CG A:HIS108 2.9 58.0 1.0
CE1 A:HIS172 3.0 58.1 1.0
CG A:HIS172 3.2 56.7 1.0
CB A:HIS108 3.4 56.8 1.0
CB A:HIS107 3.5 57.3 1.0
N A:HIS108 3.6 56.5 1.0
CB A:HIS172 3.6 55.2 1.0
NE2 A:HIS107 3.7 60.3 1.0
CD2 A:HIS107 3.7 59.5 1.0
NE2 A:HIS108 3.9 59.3 1.0
C A:HIS107 4.0 56.7 1.0
CD2 A:HIS108 4.0 59.2 1.0
CA A:HIS108 4.0 56.4 1.0
NE2 A:HIS172 4.1 57.9 1.0
CD2 A:HIS172 4.2 57.5 1.0
OH A:TYR79 4.4 54.7 1.0
CA A:HIS107 4.4 57.0 1.0
O A:HIS107 4.6 56.7 1.0
C A:HIS108 4.9 56.0 1.0
CA A:HIS172 5.0 54.9 1.0

Copper binding site 2 out of 2 in 3mid

Go back to Copper Binding Sites List in 3mid
Copper binding site 2 out of 2 in the Oxidized (CU2+) Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) with Bound Azide Obtained By Soaking (100MM 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 (100MM NAN3) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu358

b:55.8
occ:1.00
 N3 A:AZI3 2.0 60.2 1.0
NE2 A:HIS244 2.1 55.7 1.0
NE2 A:HIS242 2.2 53.3 1.0
SD A:MET314 2.6 54.6 1.0
CD2 A:HIS244 2.9 54.7 1.0
CD2 A:HIS242 3.1 52.3 1.0
N2 A:AZI3 3.1 62.3 1.0
CE1 A:HIS244 3.2 55.5 1.0
CE1 A:HIS242 3.2 51.8 1.0
CB A:MET314 3.9 54.0 1.0
CG A:MET314 3.9 54.3 1.0
CE A:MET314 4.0 55.1 1.0
CG A:HIS244 4.1 53.5 1.0
ND1 A:HIS244 4.2 55.2 1.0
N1 A:AZI3 4.3 62.8 1.0
CG A:HIS242 4.3 52.0 1.0
ND1 A:HIS242 4.3 51.7 1.0
O A:HOH10 4.9 49.2 1.0
O A:GLY308 4.9 55.7 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 01:19:20 2024

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