Magnesium in PDB 5hqb: A Glycoside Hydrolase Family 97 Enzyme (E480Q) in Complex with Panose From Pseudoalteromonas Sp. Strain K8

Protein crystallography data

The structure of A Glycoside Hydrolase Family 97 Enzyme (E480Q) in Complex with Panose From Pseudoalteromonas Sp. Strain K8, PDB code: 5hqb was solved by J.Li, C.He, Y.Xiao, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 39.29 / 1.80
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 119.167, 119.167, 181.832, 90.00, 90.00, 120.00
R / Rfree (%) 13.7 / 15.5

Other elements in 5hqb:

The structure of A Glycoside Hydrolase Family 97 Enzyme (E480Q) in Complex with Panose From Pseudoalteromonas Sp. Strain K8 also contains other interesting chemical elements:

Calcium (Ca) 1 atom
Chlorine (Cl) 2 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the A Glycoside Hydrolase Family 97 Enzyme (E480Q) in Complex with Panose From Pseudoalteromonas Sp. Strain K8 (pdb code 5hqb). 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 A Glycoside Hydrolase Family 97 Enzyme (E480Q) in Complex with Panose From Pseudoalteromonas Sp. Strain K8, PDB code: 5hqb:

Magnesium binding site 1 out of 1 in 5hqb

Go back to Magnesium Binding Sites List in 5hqb
Magnesium binding site 1 out of 1 in the A Glycoside Hydrolase Family 97 Enzyme (E480Q) in Complex with Panose From Pseudoalteromonas Sp. Strain K8


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of A Glycoside Hydrolase Family 97 Enzyme (E480Q) in Complex with Panose From Pseudoalteromonas Sp. Strain K8 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg704

b:14.8
occ:1.00
OD2 A:ASP611 2.0 14.8 1.0
O A:HOH893 2.0 12.1 1.0
O A:GLY584 2.0 15.3 1.0
OD2 A:ASP585 2.1 16.2 1.0
O A:HOH1148 2.1 15.7 1.0
O A:HOH1303 2.2 16.0 1.0
C A:GLY584 3.1 17.6 1.0
CG A:ASP611 3.2 15.5 1.0
CG A:ASP585 3.3 23.7 1.0
CA A:ASP585 3.6 12.8 1.0
N A:ASP585 3.7 13.9 1.0
CB A:ASP611 3.7 14.7 1.0
CB A:ASP585 4.0 13.2 1.0
OE2 A:GLU612 4.0 19.7 1.0
O A:HOH1650 4.0 39.5 1.0
NH2 A:ARG615 4.1 25.9 1.0
OE1 A:GLU612 4.1 16.3 1.0
CA A:GLY584 4.2 16.1 1.0
OD1 A:ASP611 4.2 16.5 1.0
OE1 A:GLU492 4.3 16.8 1.0
OD1 A:ASP585 4.3 20.9 1.0
O A:HOH843 4.3 52.9 1.0
O A:HOH1156 4.4 34.9 1.0
O A:HOH1048 4.5 20.0 1.0
CD A:GLU612 4.5 22.1 1.0
CB A:GLU492 4.7 13.1 1.0
O A:HOH831 4.7 38.7 1.0
C A:ASP585 4.9 17.1 1.0

Reference:

C.He, J.Li, W.Li, Y.Xue, Z.Fang, W.Fang, X.Zhang, X.Wang, Y.Xiao. Structures of PSPAG97A Alpha-Glucoside Hydrolase Reveal A Novel Mechanism For Chloride Induced Activation. J. Struct. Biol. V. 196 426 2016.
ISSN: ESSN 1095-8657
PubMed: 27645700
DOI: 10.1016/J.JSB.2016.09.009
Page generated: Mon Dec 14 20:28:34 2020

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