Atomistry » Nickel » PDB 3l1m-3n6n » 3mib
Atomistry »
  Nickel »
    PDB 3l1m-3n6n »
      3mib »

Nickel in PDB 3mib: Oxidized (CU2+) Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) with Bound Nitrite

Enzymatic activity of Oxidized (CU2+) Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) with Bound Nitrite

All present enzymatic activity of Oxidized (CU2+) Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) with Bound Nitrite:
1.14.17.3;

Protein crystallography data

The structure of Oxidized (CU2+) Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) with Bound Nitrite, PDB code: 3mib 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 / 2.35
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 68.612, 68.617, 80.254, 90.00, 90.00, 90.00
R / Rfree (%) 20 / 24.4

Other elements in 3mib:

The structure of Oxidized (CU2+) Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) with Bound Nitrite 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 Nitrite (pdb code 3mib). 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 Nitrite, PDB code: 3mib:

Nickel binding site 1 out of 1 in 3mib

Go back to Nickel Binding Sites List in 3mib
Nickel binding site 1 out of 1 in the Oxidized (CU2+) Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) with Bound Nitrite


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 Nitrite within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ni359

b:51.0
occ:1.00
 O A:HOH486 1.9 54.8 1.0
O2 A:NO22 1.9 57.9 1.0
O A:HOH463 2.0 49.2 1.0
NE2 A:HIS235 2.0 54.8 1.0
O1 A:NO22 2.6 59.3 1.0
N A:NO22 2.8 59.2 1.0
CD2 A:HIS235 2.9 55.6 1.0
CE1 A:HIS235 3.1 55.0 1.0
CB A:ASP282 4.0 64.9 1.0
CG A:HIS235 4.1 56.9 1.0
ND1 A:HIS235 4.1 55.6 1.0
OD1 A:ASP282 4.2 66.2 1.0
CG A:ASP282 4.3 65.4 1.0
O A:HOH40 4.4 64.6 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: Wed Oct 9 17:31:59 2024

Last articles

Zn in 9MJ5
Zn in 9HNW
Zn in 9G0L
Zn in 9FNE
Zn in 9DZN
Zn in 9E0I
Zn in 9D32
Zn in 9DAK
Zn in 8ZXC
Zn in 8ZUF
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy