Bromine 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:

Magnesium (Mg) 1 atom

Bromine Binding Sites:

The binding sites of Bromine 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 Bromine atom.
In total only one binding site of Bromine was determined in the The Structure of A Beta-Glucuronidase From Glycoside Hydrolase Family 2, PDB code: 6hpd:

Bromine binding site 1 out of 1 in 6hpd

Go back to Bromine Binding Sites List in 6hpd
Bromine 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 Bromine with other atoms in the Br 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:Br1001

b:18.2
occ:0.74
 OG1 A:THR351 3.0 16.9 1.0
O A:HOH1461 3.3 14.1 1.0
N A:ALA353 3.4 11.2 1.0
CG A:PRO188 3.6 18.5 1.0
CB A:ALA353 3.7 12.3 1.0
CD A:PRO577 3.7 15.9 1.0
CB A:THR351 3.7 16.4 1.0
CD2 A:HIS578 3.8 19.2 1.0
N A:ASN352 3.9 13.4 1.0
CD A:PRO188 4.0 17.9 1.0
CA A:GLY576 4.0 17.2 1.0
CA A:ALA353 4.2 12.5 1.0
C A:THR351 4.2 14.0 1.0
CB A:LYS349 4.3 13.1 1.0
N A:PRO577 4.4 17.3 1.0
O A:HOH1156 4.4 8.7 1.0
C A:ASN352 4.4 12.3 1.0
CA A:ASN352 4.5 12.5 1.0
C A:GLY576 4.5 18.0 1.0
CB A:PRO188 4.5 18.1 1.0
NE2 A:HIS578 4.5 19.2 1.0
CA A:THR351 4.6 14.2 1.0
CG A:LYS349 4.8 12.9 1.0
O A:THR351 4.8 14.5 1.0
CG A:PRO577 4.9 16.0 1.0
CG A:HIS578 4.9 19.8 1.0
CG2 A:THR351 4.9 17.2 1.0
O A:ALA353 5.0 15.3 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: Sat Dec 12 02:34:06 2020

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