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Nickel in PDB 5v2v: Ethylene Forming Enzyme in Complex with Nickel

Enzymatic activity of Ethylene Forming Enzyme in Complex with Nickel

All present enzymatic activity of Ethylene Forming Enzyme in Complex with Nickel:
1.13.12.19; 1.14.11.34;

Protein crystallography data

The structure of Ethylene Forming Enzyme in Complex with Nickel, PDB code: 5v2v was solved by M.Fellner, S.Martinez, J.Hu, R.P.Hausinger, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 43.88 / 3.04
Space group P 2 21 21
Cell size a, b, c (Å), α, β, γ (°) 41.790, 79.310, 87.750, 90.00, 90.00, 90.00
R / Rfree (%) 19.9 / 26.8

Nickel Binding Sites:

The binding sites of Nickel atom in the Ethylene Forming Enzyme in Complex with Nickel (pdb code 5v2v). 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 Ethylene Forming Enzyme in Complex with Nickel, PDB code: 5v2v:

Nickel binding site 1 out of 1 in 5v2v

Go back to Nickel Binding Sites List in 5v2v
Nickel binding site 1 out of 1 in the Ethylene Forming Enzyme in Complex with Nickel


Mono view


Stereo pair view

A full contact list of Nickel with other atoms in the Ni binding site number 1 of Ethylene Forming Enzyme in Complex with Nickel within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ni401

b:52.0
occ:0.97
NE2 A:HIS189 2.0 51.1 1.0
OD1 A:ASP191 2.0 33.1 1.0
NE2 A:HIS268 2.0 46.9 1.0
O A:HOH501 2.3 40.8 1.0
O A:HOH502 2.4 47.5 1.0
CE1 A:HIS268 2.9 43.7 1.0
CG A:ASP191 2.9 41.6 1.0
CE1 A:HIS189 2.9 57.3 1.0
CD2 A:HIS189 3.0 51.2 1.0
OD2 A:ASP191 3.1 40.4 1.0
CD2 A:HIS268 3.1 45.5 1.0
ND1 A:HIS268 4.0 38.3 1.0
ND1 A:HIS189 4.0 48.7 1.0
CG A:HIS189 4.1 47.7 1.0
CG A:HIS268 4.2 37.7 1.0
CB A:ASP191 4.3 38.9 1.0
N A:ASP191 4.7 49.3 1.0
CA A:ASP191 4.7 42.4 1.0

Reference:

S.Martinez, M.Fellner, C.Q.Herr, A.Ritchie, J.Hu, R.P.Hausinger. Structures and Mechanisms of the Non-Heme Fe(II)- and 2-Oxoglutarate-Dependent Ethylene-Forming Enzyme: Substrate Binding Creates A Twist. J. Am. Chem. Soc. V. 139 11980 2017.
ISSN: ESSN 1520-5126
PubMed: 28780854
DOI: 10.1021/JACS.7B06186
Page generated: Wed Dec 16 01:49:14 2020

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