Magnesium in PDB 6qii: Xenon Derivatization of the F420-Reducing [Nife] Hydrogenase Complex From Methanosarcina Barkeri

Enzymatic activity of Xenon Derivatization of the F420-Reducing [Nife] Hydrogenase Complex From Methanosarcina Barkeri

All present enzymatic activity of Xenon Derivatization of the F420-Reducing [Nife] Hydrogenase Complex From Methanosarcina Barkeri:
1.12.98.1;

Protein crystallography data

The structure of Xenon Derivatization of the F420-Reducing [Nife] Hydrogenase Complex From Methanosarcina Barkeri, PDB code: 6qii was solved by Y.Ilina, C.Lorent, S.Katz, J.H.Jeoung, S.Shima, M.Horch, I.Zebger, H.Dobbek, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 45.55 / 2.28
Space group F 2 3
Cell size a, b, c (Å), α, β, γ (°) 236.705, 236.705, 236.705, 90.00, 90.00, 90.00
R / Rfree (%) 17.6 / 22.7

Other elements in 6qii:

The structure of Xenon Derivatization of the F420-Reducing [Nife] Hydrogenase Complex From Methanosarcina Barkeri also contains other interesting chemical elements:

Nickel (Ni) 1 atom
Xenon (Xe) 7 atoms
Iron (Fe) 19 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Xenon Derivatization of the F420-Reducing [Nife] Hydrogenase Complex From Methanosarcina Barkeri (pdb code 6qii). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Xenon Derivatization of the F420-Reducing [Nife] Hydrogenase Complex From Methanosarcina Barkeri, PDB code: 6qii:

Magnesium binding site 1 out of 1 in 6qii

Go back to Magnesium Binding Sites List in 6qii
Magnesium binding site 1 out of 1 in the Xenon Derivatization of the F420-Reducing [Nife] Hydrogenase Complex From Methanosarcina Barkeri


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Xenon Derivatization of the F420-Reducing [Nife] Hydrogenase Complex From Methanosarcina Barkeri within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg504

b:55.3
occ:0.31
OD1 A:ASN322 2.4 58.9 1.0
O A:HOH649 2.5 50.6 1.0
CG A:ASN322 3.2 59.0 1.0
ND2 A:ASN322 3.2 47.8 1.0
H42 A:144505 3.9 77.6 0.3
H32 A:144505 3.9 74.8 0.3
H21 A:144505 4.1 74.8 0.3
CB A:ASN322 4.6 45.8 1.0
O A:ALA318 4.7 46.7 1.0
C4 A:144505 4.8 64.8 0.3
HO3 A:144505 4.9 74.3 0.3
C3 A:144505 4.9 62.5 0.3
O A:THR319 5.0 46.2 1.0

Reference:

Y.Ilina, C.Lorent, S.Katz, J.H.Jeoung, S.Shima, M.Horch, I.Zebger, H.Dobbek. X-Ray Crystallography and Vibrational Spectroscopy Reveal the Key Determinants of Biocatalytic Dihydrogen Cycling By [Nife] Hydrogenases. Angew.Chem.Int.Ed.Engl. 2019.
ISSN: ESSN 1521-3773
PubMed: 31591784
DOI: 10.1002/ANIE.201908258
Page generated: Mon Dec 14 23:52:37 2020

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