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Nickel 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

Nickel Binding Sites:

The binding sites of Nickel 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 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 Co-Crystallization, PDB code: 3mic:

Nickel binding site 1 out of 1 in 3mic

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

b:39.0
occ:1.00
O A:HOH539 1.9 46.8 1.0
NE2 A:HIS235 2.1 39.3 1.0
O A:HOH536 2.4 50.8 1.0
O A:HOH543 2.5 45.7 1.0
O A:HOH542 2.6 38.3 1.0
CD2 A:HIS235 3.0 39.0 1.0
CE1 A:HIS235 3.1 38.5 1.0
CB A:ASP282 4.0 48.4 1.0
CG A:HIS235 4.1 39.8 1.0
ND1 A:HIS235 4.1 38.7 1.0
OD1 A:ASP282 4.2 49.6 1.0
CG A:ASP282 4.4 48.5 1.0
O A:HOH540 4.4 57.5 1.0
O A:HOH544 4.7 48.7 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 25 08:27:49 2020
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