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Nickel in PDB 3mll: Reduced (Cu+) Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) with Bound Azide

Enzymatic activity of Reduced (Cu+) Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) with Bound Azide

All present enzymatic activity of Reduced (Cu+) Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) with Bound Azide:
1.14.17.3;

Protein crystallography data

The structure of Reduced (Cu+) Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) with Bound Azide, PDB code: 3mll 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 / 3.25
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 68.131, 69.138, 79.936, 90.00, 90.00, 90.00
R / Rfree (%) 24.2 / 29.8

Other elements in 3mll:

The structure of Reduced (Cu+) Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) with Bound Azide also contains other interesting chemical elements:

Copper (Cu) 1 atom

Nickel Binding Sites:

The binding sites of Nickel atom in the Reduced (Cu+) Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) with Bound Azide (pdb code 3mll). 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 Reduced (Cu+) Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) with Bound Azide, PDB code: 3mll:

Nickel binding site 1 out of 1 in 3mll

Go back to Nickel Binding Sites List in 3mll
Nickel binding site 1 out of 1 in the Reduced (Cu+) Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) with Bound Azide


Mono view


Stereo pair view

A full contact list of Nickel with other atoms in the Ni binding site number 1 of Reduced (Cu+) Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) with Bound Azide within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ni359

b:87.5
occ:1.00
NE2 A:HIS235 2.2 88.7 1.0
CD2 A:HIS235 3.0 85.7 1.0
CE1 A:HIS235 3.2 86.8 1.0
CB A:ASP282 3.7 92.5 1.0
OD1 A:ASP282 3.9 0.1 1.0
CG A:ASP282 4.0 98.5 1.0
CG A:HIS235 4.2 81.9 1.0
ND1 A:HIS235 4.3 82.7 1.0
N A:ASP282 4.7 89.9 1.0
CA A:ASP282 4.7 88.8 1.0
OD2 A:ASP282 4.9 0.6 1.0

Reference:

E.E.Chufan, S.T.Prigge, X.Siebert, B.A.Eipper, R.E.Mains, L.M.Amzel. Differential Reactivity Between Two Copper Sites in Peptidylglycine Alpha-Hydroxylating Monooxygenase J.Am.Chem.Soc. V. 132 15565 2010.
ISSN: ISSN 0002-7863
PubMed: 20958070
DOI: 10.1021/JA103117R
Page generated: Thu Oct 29 06:21:03 2020
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