Bromine in PDB 6hsw: A CE15 Glucuronoyl Esterase From Teredinibacter Turnerae T7901

The structure of A CE15 Glucuronoyl Esterase From Teredinibacter Turnerae T7901, PDB code: 6hsw was solved by S.Mazurkewich, L.Lo Leggio, J.C.Navarro Poulsen, J.Larsbrink, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	44.81 / 2.15
Space group	P 31 2 1
Cell size a, b, c (Å), α, β, γ (°)	121.173, 121.173, 198.203, 90.00, 90.00, 120.00
R / Rfree (%)	16.4 / 21.2

The binding sites of Bromine atom in the A CE15 Glucuronoyl Esterase From Teredinibacter Turnerae T7901 (pdb code 6hsw). This binding sites where shown within 5.0 Angstroms radius around Bromine atom.
In total 2 binding sites of Bromine where determined in the A CE15 Glucuronoyl Esterase From Teredinibacter Turnerae T7901, PDB code: 6hsw:
Jump to Bromine binding site number: 1; 2;

Bromine binding site 1 out of 2 in the A CE15 Glucuronoyl Esterase From Teredinibacter Turnerae T7901


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 1 of A CE15 Glucuronoyl Esterase From Teredinibacter Turnerae T7901 within 5.0Å range: probe atom residue distance (Å) B Occ B:Br501 b:94.9 occ:1.00 HD22 B:ASN207 2.8 58.3 1.0 HH22 B:ARG200 2.9 56.0 1.0 HH12 B:ARG200 3.1 52.0 1.0 ND2 B:ASN207 3.6 48.6 1.0 NH2 B:ARG200 3.6 46.7 1.0 HB2 B:ASN207 3.6 50.9 1.0 HA B:GLN204 3.6 42.8 1.0 O B:HOH632 3.7 40.5 1.0 NH1 B:ARG200 3.8 43.3 1.0 HG2 B:GLN204 3.8 42.8 1.0 O B:HOH798 3.8 48.8 1.0 HB3 B:ASN207 3.9 50.9 1.0 CZ B:ARG200 4.1 41.5 1.0 HD21 B:ASN207 4.1 58.3 1.0 CB B:ASN207 4.1 42.4 1.0 HH21 B:ARG200 4.3 56.0 1.0 CG B:ASN207 4.4 43.7 1.0 HH11 B:ARG200 4.4 52.0 1.0 CG B:GLN204 4.6 35.7 1.0 CA B:GLN204 4.6 35.7 1.0 HG3 B:GLN204 4.6 42.8 1.0 HG2 B:GLU203 4.7 58.1 1.0

Bromine binding site 2 out of 2 in the A CE15 Glucuronoyl Esterase From Teredinibacter Turnerae T7901


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 2 of A CE15 Glucuronoyl Esterase From Teredinibacter Turnerae T7901 within 5.0Å range: probe atom residue distance (Å) B Occ C:Br501 b:0.4 occ:1.00 HH22 C:ARG200 2.7 67.9 1.0 HD22 C:ASN207 2.7 83.2 1.0 HH12 C:ARG200 3.3 82.7 1.0 NH2 C:ARG200 3.5 56.6 1.0 ND2 C:ASN207 3.6 69.4 1.0 HB2 C:ASN207 3.7 61.8 1.0 O C:HOH644 3.7 48.6 1.0 HA C:GLN204 3.8 52.0 1.0 HO1 C:EDO508 3.8 79.4 1.0 NH1 C:ARG200 3.9 68.9 1.0 HB3 C:ASN207 3.9 61.8 1.0 HG2 C:GLN204 3.9 59.0 1.0 HH21 C:ARG200 4.0 67.9 1.0 CZ C:ARG200 4.1 59.0 1.0 HD21 C:ASN207 4.1 83.2 1.0 CB C:ASN207 4.1 51.5 1.0 O C:HOH638 4.2 54.4 1.0 CG C:ASN207 4.4 49.3 1.0 H11 C:EDO508 4.5 96.5 1.0 HH11 C:ARG200 4.6 82.7 1.0 CA C:GLN204 4.7 43.3 1.0 O1 C:EDO508 4.7 66.2 1.0 CG C:GLN204 4.8 49.2 1.0 O C:HOH809 4.9 57.8 1.0 H12 C:EDO508 4.9 96.5 1.0 HB3 C:GLN204 4.9 64.9 1.0 HG2 C:GLU203 4.9 90.8 1.0 C1 C:EDO508 5.0 80.4 1.0

J.Arnling Baath, S.Mazurkewich, J.N.Poulsen, L.Olsson, L.Lo Leggio, J.Larsbrink. Structure-Function Analyses Reveal That A Glucuronoyl Esterase Fromteredinibacter Turneraeinteracts with Carbohydrates and Aromatic Compounds. J.Biol.Chem. V. 294 6635 2019.
ISSN: ESSN 1083-351X
PubMed: 30814248
DOI: 10.1074/JBC.RA119.007831