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Arsenic 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 / Rfree (%) 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:

Magnesium (Mg) 1 atom

Arsenic Binding Sites:

The binding sites of Arsenic 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 Arsenic atom.
In total only one binding site of Arsenic was determined in the Crystal Structure of the Rna Triphosphatase Domain of Mouse Mrna Capping Enzyme, PDB code: 1i9s:

Arsenic binding site 1 out of 1 in 1i9s

Go back to Arsenic Binding Sites List in 1i9s
Arsenic 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 Arsenic with other atoms in the As 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:As400

b:29.7
occ:0.70
 AS A:CAC400 0.0 29.7 0.7
C2 A:CAC400 2.1 16.2 0.7
C1 A:CAC400 2.1 25.8 0.7
SG A:CYS193 2.4 25.9 1.0
CB A:CYS193 3.2 26.8 1.0
NH1 A:ARG9 3.6 34.5 1.0
CA A:CYS193 3.7 27.0 1.0
CZ3 A:TRP192 3.8 29.2 1.0
CH2 A:TRP192 3.9 27.3 1.0
CD A:ARG9 4.5 27.5 1.0
CE3 A:TRP192 4.5 28.9 1.0
CZ A:ARG9 4.5 32.5 1.0
OH A:TYR165 4.6 22.1 1.0
O A:CYS193 4.6 29.9 1.0
CE2 A:TYR165 4.6 16.2 1.0
CZ A:TYR165 4.6 18.7 1.0
C A:CYS193 4.7 28.5 1.0
N A:CYS193 4.7 27.9 1.0
CZ2 A:TRP192 4.7 28.3 1.0
NE A:ARG9 4.8 30.5 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 Oct 27 16:46:42 2020

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