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Copper in PDB 3mig: Oxidized (CU2+) Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) with Bound Nitrite, Obtained in the Presence of Substrate

Enzymatic activity of Oxidized (CU2+) Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) with Bound Nitrite, Obtained in the Presence of Substrate

All present enzymatic activity of Oxidized (CU2+) Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) with Bound Nitrite, 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 Nitrite, Obtained in the Presence of Substrate, PDB code: 3mig 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 / 2.70
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 68.356, 68.783, 79.979, 90.00, 90.00, 90.00
R / Rfree (%) 22.1 / 27.2

Copper Binding Sites:

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

Copper binding site 1 out of 2 in 3mig

Go back to Copper Binding Sites List in 3mig
Copper binding site 1 out of 2 in the Oxidized (CU2+) Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) with Bound Nitrite, 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 Nitrite, Obtained in the Presence of Substrate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu357

b:81.9
occ:1.00
ND1 A:HIS108 2.0 56.4 1.0
ND1 A:HIS107 2.1 55.9 1.0
ND1 A:HIS172 2.3 58.8 1.0
CG A:HIS108 2.9 56.0 1.0
CE1 A:HIS108 3.0 56.5 1.0
CE1 A:HIS107 3.0 55.7 1.0
CG A:HIS107 3.0 56.2 1.0
CE1 A:HIS172 3.1 58.7 1.0
CB A:HIS108 3.2 55.5 1.0
CG A:HIS172 3.4 58.3 1.0
CB A:HIS107 3.4 56.1 1.0
N A:HIS108 3.4 55.6 1.0
CB A:HIS172 3.7 58.1 1.0
C A:HIS107 3.8 55.8 1.0
CA A:HIS108 3.9 55.5 1.0
NE2 A:HIS107 4.1 55.4 1.0
CD2 A:HIS108 4.1 56.1 1.0
NE2 A:HIS108 4.1 56.8 1.0
CD2 A:HIS107 4.1 55.6 1.0
CA A:HIS107 4.2 56.1 1.0
O A:HIS107 4.3 55.7 1.0
NE2 A:HIS172 4.3 58.6 1.0
CD2 A:HIS172 4.4 58.1 1.0
C A:HIS108 4.8 55.3 1.0
O A:HIS108 4.9 55.1 1.0
OH A:TYR79 5.0 60.0 1.0
O A:HIS172 5.0 58.7 1.0

Copper binding site 2 out of 2 in 3mig

Go back to Copper Binding Sites List in 3mig
Copper binding site 2 out of 2 in the Oxidized (CU2+) Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) with Bound Nitrite, 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 Nitrite, Obtained in the Presence of Substrate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu358

b:60.5
occ:1.00
NE2 A:HIS242 2.1 55.3 1.0
NE2 A:HIS244 2.2 58.8 1.0
O1 A:NO2360 2.3 79.6 1.0
O2 A:NO2360 2.4 79.9 1.0
SD A:MET314 2.5 59.4 1.0
N A:NO2360 2.8 79.8 1.0
CD2 A:HIS242 2.9 53.0 1.0
CD2 A:HIS244 3.1 58.1 1.0
CE1 A:HIS242 3.2 55.0 1.0
CE1 A:HIS244 3.2 58.2 1.0
CE A:MET314 3.7 59.0 1.0
CG A:MET314 3.8 59.0 1.0
CB A:MET314 4.0 58.9 1.0
CG A:HIS242 4.1 54.9 1.0
ND1 A:HIS242 4.2 54.5 1.0
CG A:HIS244 4.3 57.3 1.0
ND1 A:HIS244 4.3 57.7 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: Fri Sep 4 08:08:50 2020
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