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

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

Other elements in 3mih:

The structure of Oxidized (CU2+) Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) with Bound Azide, Obtained in the Presence of Substrate also contains other interesting chemical elements:

Nickel (Ni) 1 atom
Iodine (I) 1 atom
Sodium (Na) 4 atoms

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: Wed Jul 31 01:19:53 2024

Last articles

Ca in 2V9W
Ca in 2VA3
Ca in 2V5D
Ca in 2V9M
Ca in 2V73
Ca in 2V8B
Ca in 2V72
Ca in 2V5C
Ca in 2UZP
Ca in 2V53
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy