Magnesium in PDB 1zun: Crystal Structure of A Gtp-Regulated Atp Sulfurylase Heterodimer From Pseudomonas Syringae

Enzymatic activity of Crystal Structure of A Gtp-Regulated Atp Sulfurylase Heterodimer From Pseudomonas Syringae

All present enzymatic activity of Crystal Structure of A Gtp-Regulated Atp Sulfurylase Heterodimer From Pseudomonas Syringae:
2.7.7.4;

Protein crystallography data

The structure of Crystal Structure of A Gtp-Regulated Atp Sulfurylase Heterodimer From Pseudomonas Syringae, PDB code: 1zun was solved by J.D.Mougous, D.H.Lee, S.C.Hubbard, M.W.Schelle, D.J.Vocadlo, J.M.Berger, C.R.Bertozzi, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

*Resolution Low / High (Å)*	20.00 / 2.70
*Space group*	H 3
*Cell size a, b, c (Å), α, β, γ (°)*	110.072, 110.072, 171.002, 90.00, 90.00, 120.00
*R / R_free (%)*	22.2 / 27.6

Other elements in 1zun:

The structure of Crystal Structure of A Gtp-Regulated Atp Sulfurylase Heterodimer From Pseudomonas Syringae also contains other interesting chemical elements:

Sodium

(Na)

1 atom

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of A Gtp-Regulated Atp Sulfurylase Heterodimer From Pseudomonas Syringae (pdb code 1zun). 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 Crystal Structure of A Gtp-Regulated Atp Sulfurylase Heterodimer From Pseudomonas Syringae, PDB code: 1zun:

Magnesium binding site 1 out of 1 in 1zun

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Magnesium Binding Sites List in 1zun

Magnesium binding site 1 out of 1 in the Crystal Structure of A Gtp-Regulated Atp Sulfurylase Heterodimer From Pseudomonas Syringae

Mono view

Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of A Gtp-Regulated Atp Sulfurylase Heterodimer From Pseudomonas Syringae within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:Mg598 b:37.0 occ:1.00	O3G	A:AGS600	1.9	57.8	1.0
	O	A:HOH714	2.1	40.3	1.0
	O	A:HOH708	2.4	39.5	1.0
	O1B	A:AGS600	2.4	58.6	1.0
	O	A:ALA211	2.5	59.3	1.0
	O2A	A:AGS600	2.5	59.1	1.0
	PG	A:AGS600	3.4	57.8	1.0
	O	A:HOH713	3.5	41.0	1.0
	C	A:ALA211	3.5	59.2	1.0
	PB	A:AGS600	3.6	58.1	1.0
	CB	A:ALA211	3.8	59.2	1.0
	PA	A:AGS600	3.8	58.6	1.0
	O3B	A:AGS600	3.9	58.5	1.0
	CA	A:ALA211	4.1	59.2	1.0
	O3A	A:AGS600	4.1	58.4	1.0
	O2G	A:AGS600	4.1	58.4	1.0
	N	A:ALA211	4.4	59.1	1.0
	O5'	A:AGS600	4.5	59.5	1.0
	OG	A:SER34	4.8	52.6	1.0
	S1G	A:AGS600	4.8	58.5	1.0
	O2B	A:AGS600	5.0	59.0	1.0

Reference:

J.D.Mougous, D.H.Lee, S.C.Hubbard, M.W.Schelle, D.J.Vocadlo, J.M.Berger, C.R.Bertozzi. Molecular Basis For G Protein Control of the Prokaryotic Atp Sulfurylase. Mol.Cell V. 21 109 2006.
ISSN: ISSN 1097-2765
PubMed: 16387658
DOI: 10.1016/J.MOLCEL.2005.10.034

Page generated: Tue Aug 13 20:14:00 2024

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