Magnesium in PDB 6hpd: The Structure of A Beta-Glucuronidase From Glycoside Hydrolase Family 2

Enzymatic activity of The Structure of A Beta-Glucuronidase From Glycoside Hydrolase Family 2

All present enzymatic activity of The Structure of A Beta-Glucuronidase From Glycoside Hydrolase Family 2:
3.2.1.23;

Protein crystallography data

The structure of The Structure of A Beta-Glucuronidase From Glycoside Hydrolase Family 2, PDB code: 6hpd was solved by C.S.Robb, N.Gerlach, L.Reisky, U.Bornshoeru, J.H.Hehemann, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 96.20 / 2.43
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 157.929, 67.170, 96.720, 90.00, 95.93, 90.00
R / Rfree (%) 16.5 / 21.1

Other elements in 6hpd:

The structure of The Structure of A Beta-Glucuronidase From Glycoside Hydrolase Family 2 also contains other interesting chemical elements:

Bromine (Br) 1 atom

Magnesium Binding Sites:

The binding sites of Magnesium atom in the The Structure of A Beta-Glucuronidase From Glycoside Hydrolase Family 2 (pdb code 6hpd). 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 The Structure of A Beta-Glucuronidase From Glycoside Hydrolase Family 2, PDB code: 6hpd:

Magnesium binding site 1 out of 1 in 6hpd

Go back to Magnesium Binding Sites List in 6hpd
Magnesium binding site 1 out of 1 in the The Structure of A Beta-Glucuronidase From Glycoside Hydrolase Family 2


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of The Structure of A Beta-Glucuronidase From Glycoside Hydrolase Family 2 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1002

b:4.0
occ:1.00
 O A:SER590 2.3 13.0 1.0
O A:TRP571 2.3 17.3 1.0
OD1 A:ASN570 2.3 20.0 1.0
O A:HOH1403 2.4 17.3 1.0
O A:ILE572 2.4 16.4 1.0
OE1 A:GLU592 2.5 24.0 1.0
OE2 A:GLU592 2.8 22.4 1.0
CD A:GLU592 3.0 23.2 1.0
C A:TRP571 3.3 16.8 1.0
C A:SER590 3.5 14.4 1.0
C A:ILE572 3.5 15.3 1.0
CG A:ASN570 3.5 19.8 1.0
CA A:GLY591 4.0 16.0 1.0
N A:ILE572 4.0 14.5 1.0
CA A:ILE572 4.1 14.8 1.0
CB A:ILE572 4.1 13.5 1.0
ND2 A:ASN570 4.1 21.0 1.0
N A:GLY591 4.2 14.7 1.0
C A:GLY591 4.2 18.3 1.0
N A:TRP571 4.3 18.6 1.0
N A:GLU592 4.3 18.1 1.0
CA A:TRP571 4.4 16.7 1.0
C A:ASN570 4.5 19.2 1.0
CB A:SER590 4.5 14.4 1.0
CA A:SER590 4.5 14.9 1.0
CD1 A:TRP346 4.5 18.7 1.0
CG A:GLU592 4.6 21.8 1.0
O A:ASN570 4.6 19.8 1.0
N A:PHE573 4.6 14.1 1.0
CB A:ASN570 4.7 19.4 1.0
O A:ASN511 4.7 17.6 1.0
CZ A:PHE547 4.8 12.4 1.0
NE1 A:TRP346 4.8 18.9 1.0
O A:GLY591 4.8 18.9 1.0
CA A:PHE573 4.9 13.5 1.0
CG2 A:ILE572 5.0 10.3 1.0

Reference:

L.Reisky, A.Prechoux, M.K.Zuhlke, M.Baumgen, C.S.Robb, N.Gerlach, T.Roret, C.Stanetty, R.Larocque, G.Michel, T.Song, S.Markert, F.Unfried, M.D.Mihovilovic, A.Trautwein-Schult, D.Becher, T.Schweder, U.T.Bornscheuer, J.H.Hehemann. A Marine Bacterial Enzymatic Cascade Degrades the Algal Polysaccharide Ulvan. Nat.Chem.Biol. V. 15 803 2019.
ISSN: ESSN 1552-4469
PubMed: 31285597
DOI: 10.1038/S41589-019-0311-9
Page generated: Mon Dec 14 22:50:16 2020

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