Magnesium in PDB 6ane: Crystal Structure of Ideonella Sakaiensis Pet Hydrolase

Enzymatic activity of Crystal Structure of Ideonella Sakaiensis Pet Hydrolase

All present enzymatic activity of Crystal Structure of Ideonella Sakaiensis Pet Hydrolase:
3.1.1.101;

Protein crystallography data

The structure of Crystal Structure of Ideonella Sakaiensis Pet Hydrolase, PDB code: 6ane was solved by P.Galaz-Davison, M.Sotomayor, L.P.Parra, C.A.Ramirez-Sarmiento, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 116.93 / 2.02
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 52.868, 233.852, 165.076, 90.00, 90.00, 90.00
R / Rfree (%) 17.7 / 21.7

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Ideonella Sakaiensis Pet Hydrolase (pdb code 6ane). 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 Ideonella Sakaiensis Pet Hydrolase, PDB code: 6ane:

Magnesium binding site 1 out of 1 in 6ane

Go back to Magnesium Binding Sites List in 6ane
Magnesium binding site 1 out of 1 in the Crystal Structure of Ideonella Sakaiensis Pet Hydrolase


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 Ideonella Sakaiensis Pet Hydrolase within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mg301

b:24.0
occ:0.50
O C:HOH425 1.9 14.4 1.0
O C:HOH541 2.0 27.4 1.0
O C:HOH464 2.0 16.4 1.0
OD2 C:ASP123 3.8 17.4 1.0
OD1 C:ASP123 3.9 18.0 1.0
CG C:ASP123 4.2 17.6 1.0
OH C:TYR5 4.2 24.8 1.0
O C:HOH548 4.3 31.5 1.0
CB C:ALA125 4.7 17.4 1.0
O C:HOH433 4.8 34.2 1.0
CE1 C:TYR5 4.9 21.8 1.0

Reference:

T.Fecker, P.Galaz-Davison, F.Engelberger, Y.Narui, M.Sotomayor, L.P.Parra, C.A.Ramirez-Sarmiento. Active Site Flexibility As A Hallmark For Efficient Pet Degradation By I. Sakaiensis Petase. Biophys. J. V. 114 1302 2018.
ISSN: ESSN 1542-0086
PubMed: 29590588
DOI: 10.1016/J.BPJ.2018.02.005
Page generated: Mon Dec 14 22:20:48 2020

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