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 / R_free (%)*	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

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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: Mon Jul 7 10:00:48 2025

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