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Magnesium in PDB 2rio: Structure of the Dual Enzyme IRE1 Reveals the Basis For Catalysis and Regulation of Non-Conventional Splicing

Enzymatic activity of Structure of the Dual Enzyme IRE1 Reveals the Basis For Catalysis and Regulation of Non-Conventional Splicing

All present enzymatic activity of Structure of the Dual Enzyme IRE1 Reveals the Basis For Catalysis and Regulation of Non-Conventional Splicing:
2.7.11.1;

Protein crystallography data

The structure of Structure of the Dual Enzyme IRE1 Reveals the Basis For Catalysis and Regulation of Non-Conventional Splicing, PDB code: 2rio was solved by K.P.Lee, M.Dey, D.Neculai, C.Cao, T.E.Dever, F.Sicheri, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.83 / 2.40
Space group P 65
Cell size a, b, c (Å), α, β, γ (°) 130.307, 130.307, 175.011, 90.00, 90.00, 120.00
R / Rfree (%) 22.2 / 26.6

Other elements in 2rio:

The structure of Structure of the Dual Enzyme IRE1 Reveals the Basis For Catalysis and Regulation of Non-Conventional Splicing also contains other interesting chemical elements:

Strontium (Sr) 2 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Structure of the Dual Enzyme IRE1 Reveals the Basis For Catalysis and Regulation of Non-Conventional Splicing (pdb code 2rio). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Structure of the Dual Enzyme IRE1 Reveals the Basis For Catalysis and Regulation of Non-Conventional Splicing, PDB code: 2rio:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 2rio

Go back to Magnesium Binding Sites List in 2rio
Magnesium binding site 1 out of 2 in the Structure of the Dual Enzyme IRE1 Reveals the Basis For Catalysis and Regulation of Non-Conventional Splicing


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of the Dual Enzyme IRE1 Reveals the Basis For Catalysis and Regulation of Non-Conventional Splicing within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1102

b:29.0
occ:1.00
O1A A:ADP1101 2.0 18.4 1.0
OD2 A:ASP171 2.0 23.2 1.0
O3B A:ADP1101 2.0 25.7 1.0
OD1 A:ASN145 2.2 18.5 1.0
CG A:ASP171 3.2 29.0 1.0
CG A:ASN145 3.2 25.2 1.0
PB A:ADP1101 3.3 25.0 1.0
PA A:ADP1101 3.4 19.9 1.0
ND2 A:ASN145 3.6 24.9 1.0
O3A A:ADP1101 3.7 20.5 1.0
O2B A:ADP1101 3.7 24.6 1.0
CB A:ASP171 3.9 27.1 1.0
SR A:SR1103 4.2 34.5 1.0
O5' A:ADP1101 4.2 23.6 1.0
OD1 A:ASP171 4.2 25.1 1.0
O2A A:ADP1101 4.5 20.9 1.0
CB A:ASN145 4.5 19.5 1.0
O1B A:ADP1101 4.5 27.4 1.0
O A:GLN144 4.7 23.9 1.0
C5' A:ADP1101 4.7 22.1 1.0
CA A:ASN145 4.8 21.5 1.0
OD2 A:ASP140 4.9 26.5 1.0
C A:GLN144 5.0 23.6 1.0

Magnesium binding site 2 out of 2 in 2rio

Go back to Magnesium Binding Sites List in 2rio
Magnesium binding site 2 out of 2 in the Structure of the Dual Enzyme IRE1 Reveals the Basis For Catalysis and Regulation of Non-Conventional Splicing


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Structure of the Dual Enzyme IRE1 Reveals the Basis For Catalysis and Regulation of Non-Conventional Splicing within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg2102

b:26.8
occ:1.00
O1A B:ADP2101 2.1 18.6 1.0
O3B B:ADP2101 2.1 21.7 1.0
OD2 B:ASP171 2.2 18.9 1.0
OD1 B:ASN145 2.2 20.7 1.0
CG B:ASN145 3.1 24.3 1.0
CG B:ASP171 3.2 26.1 1.0
ND2 B:ASN145 3.3 19.2 1.0
PB B:ADP2101 3.4 20.7 1.0
PA B:ADP2101 3.4 18.6 1.0
O3A B:ADP2101 3.8 19.3 1.0
O2B B:ADP2101 3.9 22.4 1.0
CB B:ASP171 3.9 24.8 1.0
SR B:SR2103 4.1 37.0 1.0
OD1 B:ASP171 4.2 20.2 1.0
O5' B:ADP2101 4.2 18.7 1.0
CB B:ASN145 4.5 21.9 1.0
O2A B:ADP2101 4.6 18.4 1.0
O1B B:ADP2101 4.6 25.7 1.0
C5' B:ADP2101 4.8 19.6 1.0
O B:GLN144 4.9 25.1 1.0
CA B:ASN145 4.9 23.0 1.0
OD2 B:ASP140 4.9 38.0 1.0
N B:ASN145 5.0 24.1 1.0

Reference:

K.P.Lee, M.Dey, D.Neculai, C.Cao, T.E.Dever, F.Sicheri. Structure of the Dual Enzyme IRE1 Reveals the Basis For Catalysis and Regulation in Nonconventional Rna Splicing. Cell(Cambridge,Mass.) V. 132 89 2008.
ISSN: ISSN 0092-8674
PubMed: 18191223
DOI: 10.1016/J.CELL.2007.10.057
Page generated: Mon Dec 14 07:38:38 2020

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