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Nickel 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:

Copper (Cu) 2 atoms

Nickel Binding Sites:

The binding sites of Nickel 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 Nickel atom.
In total only one binding site of Nickel was determined in the Oxidized (CU2+) Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) with Bound Azide Obtained By Soaking (100MM NAN3), PDB code: 3mid:

Nickel binding site 1 out of 1 in 3mid

Go back to Nickel Binding Sites List in 3mid
Nickel binding site 1 out of 1 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 Nickel with other atoms in the Ni 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:Ni359

b:60.2
occ:1.00
 N1 A:AZI2 1.9 62.4 1.0
NE2 A:HIS235 2.1 56.8 1.0
O A:HOH6 2.2 63.1 1.0
O A:HOH8 2.4 50.9 1.0
N2 A:AZI2 2.7 64.0 1.0
CD2 A:HIS235 2.8 55.4 1.0
CE1 A:HIS235 3.3 56.4 1.0
O A:HOH9 3.3 53.8 1.0
N3 A:AZI2 3.7 64.7 1.0
CB A:ASP282 3.7 55.1 1.0
CG A:HIS235 4.1 54.6 1.0
CG A:ASP282 4.1 55.8 1.0
ND1 A:HIS235 4.2 55.7 1.0
OD2 A:ASP282 4.4 58.1 1.0
OD1 A:ASP282 4.6 56.7 1.0
CA A:ASP282 4.7 55.1 1.0
N A:ASP282 4.8 55.9 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: Mon Aug 18 18:47:12 2025

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