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Magnesium in PDB 6qgr: The F420-Reducing [Nife] Hydrogenase Complex From Methanosarcina Barkeri at the Nia-S State

Enzymatic activity of The F420-Reducing [Nife] Hydrogenase Complex From Methanosarcina Barkeri at the Nia-S State

All present enzymatic activity of The F420-Reducing [Nife] Hydrogenase Complex From Methanosarcina Barkeri at the Nia-S State:
1.12.98.1;

Protein crystallography data

The structure of The F420-Reducing [Nife] Hydrogenase Complex From Methanosarcina Barkeri at the Nia-S State, PDB code: 6qgr 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) 48.14 / 1.84
Space group F 2 3
Cell size a, b, c (Å), α, β, γ (°) 235.826, 235.826, 235.826, 90.00, 90.00, 90.00
R / Rfree (%) 17.5 / 22.1

Other elements in 6qgr:

The structure of The F420-Reducing [Nife] Hydrogenase Complex From Methanosarcina Barkeri at the Nia-S State also contains other interesting chemical elements:

Nickel (Ni) 1 atom
Iron (Fe) 19 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the The F420-Reducing [Nife] Hydrogenase Complex From Methanosarcina Barkeri at the Nia-S State (pdb code 6qgr). 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 The F420-Reducing [Nife] Hydrogenase Complex From Methanosarcina Barkeri at the Nia-S State, PDB code: 6qgr:

Magnesium binding site 1 out of 1 in 6qgr

Go back to Magnesium Binding Sites List in 6qgr
Magnesium binding site 1 out of 1 in the The F420-Reducing [Nife] Hydrogenase Complex From Methanosarcina Barkeri at the Nia-S State


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of The F420-Reducing [Nife] Hydrogenase Complex From Methanosarcina Barkeri at the Nia-S State within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg503

b:35.0
occ:0.29
OD1 A:ASN322 2.4 39.0 1.0
O A:HOH720 2.5 34.6 1.0
CG A:ASN322 3.3 39.6 1.0
ND2 A:ASN322 3.5 32.2 1.0
C1 A:144505 3.7 38.2 0.2
CB A:ASN322 4.7 29.7 1.0
O A:ALA318 4.7 31.4 1.0
N A:144505 4.9 41.1 0.2
O A:THR319 5.0 31.3 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: Tue Oct 1 15:28:14 2024

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