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Nickel in PDB 3mif: Oxidized (CU2+) Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) with Bound Carbon Monooxide (Co)

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

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

Protein crystallography data

The structure of Oxidized (CU2+) Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) with Bound Carbon Monooxide (Co), PDB code: 3mif was solved by X.Siebert, 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) 34.63 / 2.00
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 69.246, 69.715, 83.121, 90.00, 90.00, 90.00
R / Rfree (%) 20.7 / 23.5

Other elements in 3mif:

The structure of Oxidized (CU2+) Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) with Bound Carbon Monooxide (Co) 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 Carbon Monooxide (Co) (pdb code 3mif). 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 Carbon Monooxide (Co), PDB code: 3mif:

Nickel binding site 1 out of 1 in 3mif

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


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 Carbon Monooxide (Co) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ni359

b:30.8
occ:1.00
 O A:HOH474 2.0 32.0 1.0
NE2 A:HIS235 2.1 34.2 1.0
O A:HOH475 2.2 33.5 1.0
O A:HOH476 2.3 34.4 1.0
O A:HOH477 2.4 32.0 1.0
CD2 A:HIS235 3.0 34.1 1.0
CE1 A:HIS235 3.1 34.7 1.0
O A:HOH483 4.1 34.7 1.0
CG A:HIS235 4.2 35.6 1.0
ND1 A:HIS235 4.2 34.9 1.0
CB A:ASP282 4.2 38.7 1.0
O A:HOH376 4.2 39.2 1.0
OD1 A:ASP282 4.3 36.9 1.0
CG A:ASP282 4.5 38.4 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 17:32:20 2024

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