Magnesium in PDB 4d3d: Structure of Imine Reductase Bcsired From Bacillus Cereus BAG3X2

Enzymatic activity of Structure of Imine Reductase Bcsired From Bacillus Cereus BAG3X2

All present enzymatic activity of Structure of Imine Reductase Bcsired From Bacillus Cereus BAG3X2:
1.5.1.3;

Protein crystallography data

The structure of Structure of Imine Reductase Bcsired From Bacillus Cereus BAG3X2, PDB code: 4d3d was solved by H.Man, S.Hart, J.P.Turkenburg, G.Grogan, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 107.43 / 1.71
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 55.777, 59.593, 214.867, 90.00, 90.00, 90.00
R / Rfree (%) 17.805 / 20.988

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Structure of Imine Reductase Bcsired From Bacillus Cereus BAG3X2 (pdb code 4d3d). 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 Structure of Imine Reductase Bcsired From Bacillus Cereus BAG3X2, PDB code: 4d3d:

Magnesium binding site 1 out of 1 in 4d3d

Go back to Magnesium Binding Sites List in 4d3d
Magnesium binding site 1 out of 1 in the Structure of Imine Reductase Bcsired From Bacillus Cereus BAG3X2


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of Imine Reductase Bcsired From Bacillus Cereus BAG3X2 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1306

b:20.5
occ:1.00
O A:HOH2008 3.1 18.2 1.0
O A:HOH2064 3.2 35.2 1.0
N A:ARG53 3.3 18.7 1.0
CB A:ASN52 3.6 16.2 1.0
CG A:ARG53 3.7 23.0 1.0
CD2 A:LEU86 3.8 30.8 1.0
CD A:ARG53 3.8 28.6 1.0
CB A:ARG53 3.9 20.5 1.0
CA A:ASN52 4.0 16.3 1.0
CA A:GLY29 4.2 16.9 1.0
C A:ASN52 4.2 19.6 1.0
CA A:ARG53 4.2 20.5 1.0
ND2 A:ASN52 4.6 18.5 1.0
CG A:ASN52 4.6 16.6 1.0
N A:GLY29 4.6 16.5 1.0

Reference:

H.Man, E.Wells, S.Hussain, F.Leipold, S.Hart, J.P.Turkenburg, N.Turner, G.Grogan. Structure, Activity and Stereoselectivity of Nadph- Dependent Oxidoreductases Catalysing the S-Selective Reduction of the Imine Substrate 2-Methylpyrroline Chembiochem 2015.
ISSN: ESSN 1439-7633
DOI: 10.1002/CBIC.201402625
Page generated: Mon Dec 14 11:56:30 2020

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