Atomistry » Copper » PDB 3iea-3mn0 » 3mic
Atomistry »
  Copper »
    PDB 3iea-3mn0 »
      3mic »

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

Other elements in 3mic:

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

Nickel (Ni) 1 atom
Sodium (Na) 2 atoms

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: Wed Jul 31 01:19:05 2024

Last articles

Zn in 9MJ5
Zn in 9HNW
Zn in 9G0L
Zn in 9FNE
Zn in 9DZN
Zn in 9E0I
Zn in 9D32
Zn in 9DAK
Zn in 8ZXC
Zn in 8ZUF
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy