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Nickel in PDB 3mie: Oxidized (CU2+) Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) with Bound Azide Obtained By Soaking (50MM NAN3)

Enzymatic activity of Oxidized (CU2+) Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) with Bound Azide Obtained By Soaking (50MM NAN3)

All present enzymatic activity of Oxidized (CU2+) Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) with Bound Azide Obtained By Soaking (50MM NAN3):
1.14.17.3;

Protein crystallography data

The structure of Oxidized (CU2+) Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) with Bound Azide Obtained By Soaking (50MM NAN3), PDB code: 3mie 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) 52.56 / 3.26
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 68.719, 68.991, 81.259, 90.00, 90.00, 90.00
R / Rfree (%) 19.1 / 24

Nickel Binding Sites:

The binding sites of Nickel atom in the Oxidized (CU2+) Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) with Bound Azide Obtained By Soaking (50MM NAN3) (pdb code 3mie). 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 (50MM NAN3), PDB code: 3mie:

Nickel binding site 1 out of 1 in 3mie

Go back to Nickel Binding Sites List in 3mie
Nickel binding site 1 out of 1 in the Oxidized (CU2+) Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) with Bound Azide Obtained By Soaking (50MM 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 (50MM NAN3) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ni359

b:63.7
occ:1.00
N3 A:AZI2 2.0 67.5 1.0
O A:HOH7 2.1 70.3 1.0
O A:HOH10 2.2 63.6 1.0
NE2 A:HIS235 2.3 61.7 1.0
O A:HOH11 2.7 51.9 1.0
N2 A:AZI2 2.9 70.4 1.0
CD2 A:HIS235 2.9 60.4 1.0
CE1 A:HIS235 3.5 61.7 1.0
CB A:ASP282 3.9 63.4 1.0
N1 A:AZI2 4.0 71.3 1.0
CG A:HIS235 4.2 60.0 1.0
ND1 A:HIS235 4.4 60.5 1.0
CG A:ASP282 4.4 64.2 1.0
OD2 A:ASP282 4.7 65.6 1.0
CA A:ASP282 4.8 63.3 1.0
N A:ASP282 4.8 63.5 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 25 08:27:57 2020
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