Magnesium in PDB 1i9s: Crystal Structure of the Rna Triphosphatase Domain of Mouse Mrna Capping Enzyme

Enzymatic activity of Crystal Structure of the Rna Triphosphatase Domain of Mouse Mrna Capping Enzyme

All present enzymatic activity of Crystal Structure of the Rna Triphosphatase Domain of Mouse Mrna Capping Enzyme:
3.1.3.33;

Protein crystallography data

The structure of Crystal Structure of the Rna Triphosphatase Domain of Mouse Mrna Capping Enzyme, PDB code: 1i9s was solved by A.Changela, C.K.Ho, A.Martins, S.Shuman, A.Mondragon, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

*Resolution Low / High (Å)*	27.00 / 1.65
*Space group*	C 2 2 2₁
*Cell size a, b, c (Å), α, β, γ (°)*	62.228, 98.856, 71.818, 90.00, 90.00, 90.00
*R / R_free (%)*	19.4 / 22.5

Other elements in 1i9s:

The structure of Crystal Structure of the Rna Triphosphatase Domain of Mouse Mrna Capping Enzyme also contains other interesting chemical elements:

Arsenic

(As)

1 atom

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of the Rna Triphosphatase Domain of Mouse Mrna Capping Enzyme (pdb code 1i9s). 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 the Rna Triphosphatase Domain of Mouse Mrna Capping Enzyme, PDB code: 1i9s:

Magnesium binding site 1 out of 1 in 1i9s

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Magnesium Binding Sites List in 1i9s

Magnesium binding site 1 out of 1 in the Crystal Structure of the Rna Triphosphatase Domain of Mouse Mrna Capping Enzyme

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 the Rna Triphosphatase Domain of Mouse Mrna Capping Enzyme within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:Mg500 b:11.7 occ:0.50	O	A:HOH814	2.0	14.1	0.5
	O	A:HOH817	2.0	12.9	0.5
	O	A:HOH812	2.0	13.6	0.5
	O	A:HOH813	2.0	14.1	0.5
	O	A:HOH816	2.0	15.2	0.5
	O	A:HOH815	2.1	12.9	0.5
	O	A:HOH656	3.9	23.5	1.0
	O2	A:SO4300	4.1	19.4	1.0
	O	A:HOH688	4.1	24.1	1.0
	OD1	A:ASP78	4.2	15.8	1.0
	O4	A:SO4300	4.3	19.8	1.0
	OD2	A:ASP78	4.4	16.1	1.0
	CG	A:PRO33	4.5	15.0	1.0
	CG	A:ASP78	4.8	14.8	1.0
	S	A:SO4300	4.9	17.1	1.0
	CD	A:PRO33	4.9	14.4	1.0
	O	A:HOH621	4.9	20.3	1.0

Reference:

A.Changela, C.K.Ho, A.Martins, S.Shuman, A.Mondragon. Structure and Mechanism of the Rna Triphosphatase Component of Mammalian Mrna Capping Enzyme. Embo J. V. 20 2575 2001.
ISSN: ISSN 0261-4189
PubMed: 11350947
DOI: 10.1093/EMBOJ/20.10.2575

Page generated: Tue Aug 13 04:36:46 2024

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