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Nickel 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

Nickel Binding Sites:

The binding sites of Nickel 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 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 in the Presence of Substrate, PDB code: 3mih:

Nickel binding site 1 out of 1 in 3mih

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

b:97.0
occ:1.00
O A:HOH368 1.9 84.3 1.0
N3 A:AZI4 1.9 0.1 1.0
NE2 A:HIS235 2.2 81.7 1.0
O A:HOH367 2.5 0.6 1.0
O A:HOH370 2.5 0.6 1.0
N2 A:AZI4 2.6 0.5 1.0
CD2 A:HIS235 2.9 82.1 1.0
CE1 A:HIS235 3.3 81.9 1.0
N1 A:AZI4 3.6 0.3 1.0
CB A:ASP282 4.0 88.2 1.0
OD2 A:ASP282 4.1 89.1 1.0
CG A:HIS235 4.1 82.2 1.0
ND1 A:HIS235 4.3 82.1 1.0
CG A:ASP282 4.4 88.5 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 08:28:15 2020
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