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 / R_free (%)*	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

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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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