Bromine in PDB 5ngw: Glycoside Hydrolase-Like Protein

The structure of Glycoside Hydrolase-Like Protein, PDB code: 5ngw was solved by C.S.Robb, J.-H.Hehemann, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	88.38 / 2.40
Space group	P 31 2 1
Cell size a, b, c (Å), α, β, γ (°)	102.054, 102.054, 80.113, 90.00, 90.00, 120.00
R / Rfree (%)	16.4 / 21.5

The binding sites of Bromine atom in the Glycoside Hydrolase-Like Protein (pdb code 5ngw). This binding sites where shown within 5.0 Angstroms radius around Bromine atom.
In total 5 binding sites of Bromine where determined in the Glycoside Hydrolase-Like Protein, PDB code: 5ngw:
Jump to Bromine binding site number: 1; 2; 3; 4; 5;

Bromine binding site 1 out of 5 in the Glycoside Hydrolase-Like Protein


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 1 of Glycoside Hydrolase-Like Protein within 5.0Å range: probe atom residue distance (Å) B Occ A:Br401 b:54.1 occ:0.59 ND2 A:ASN206 3.5 50.9 1.0 CG A:ASN206 4.7 58.2 1.0

Bromine binding site 2 out of 5 in the Glycoside Hydrolase-Like Protein


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 2 of Glycoside Hydrolase-Like Protein within 5.0Å range: probe atom residue distance (Å) B Occ A:Br402 b:51.4 occ:0.64 N A:PHE11 3.4 83.6 1.0 N A:LEU223 3.5 53.2 1.0 CB A:LEU223 3.6 58.2 1.0 CB A:PRO221 3.7 58.3 1.0 CG A:LEU223 3.7 62.0 1.0 CD A:PRO222 3.7 47.1 1.0 OH A:TYR266 3.9 86.2 1.0 CD1 A:LEU223 3.9 62.5 1.0 N A:PRO222 3.9 45.2 1.0 CE2 A:TYR266 4.0 77.1 1.0 CA A:LEU223 4.1 53.7 1.0 CG A:PRO222 4.1 47.8 1.0 O A:PHE11 4.1 91.3 1.0 C A:PRO221 4.4 49.0 1.0 CA A:PRO221 4.4 55.0 1.0 CZ A:TYR266 4.4 78.5 1.0 CA A:PHE11 4.5 90.4 1.0 C A:PRO222 4.5 52.2 1.0 C A:PHE11 4.6 99.8 1.0 CA A:PRO222 4.7 46.6 1.0 C A:LEU223 4.8 49.2 1.0 N A:ARG224 4.9 44.8 1.0 CB A:PHE11 4.9 88.7 1.0 CG A:PRO221 5.0 57.3 1.0 CB A:PRO222 5.0 48.7 1.0

Bromine binding site 3 out of 5 in the Glycoside Hydrolase-Like Protein


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 3 of Glycoside Hydrolase-Like Protein within 5.0Å range: probe atom residue distance (Å) B Occ A:Br403 b:65.8 occ:0.54 N A:THR60 3.3 49.4 1.0 N A:ASP61 3.4 48.2 1.0 CG A:ASP61 3.6 68.9 1.0 CB A:ASN59 3.7 51.4 1.0 CA A:ASN59 3.8 51.6 1.0 OD1 A:ASP61 3.8 72.5 1.0 OD2 A:ASP61 3.8 72.7 1.0 ND2 A:ASN59 3.8 47.0 1.0 CB A:ASP61 3.9 58.4 1.0 OG1 A:THR60 4.0 51.0 1.0 C A:ASN59 4.0 51.1 1.0 CG A:ASN59 4.1 52.1 1.0 CA A:THR60 4.2 50.7 1.0 CA A:ASP61 4.3 49.4 1.0 C A:THR60 4.3 47.6 1.0 CB A:THR60 4.7 54.6 1.0

Bromine binding site 4 out of 5 in the Glycoside Hydrolase-Like Protein


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 4 of Glycoside Hydrolase-Like Protein within 5.0Å range: probe atom residue distance (Å) B Occ A:Br404 b:64.3 occ:0.55 CE A:LYS364 3.6 67.5 1.0 CD A:LYS368 3.7 44.9 1.0 CE A:LYS368 3.8 43.2 1.0 CG A:LYS368 3.9 42.4 1.0 NZ A:LYS364 4.0 59.7 1.0 CA A:GLY74 4.2 45.5 1.0 CB A:LYS368 4.5 40.7 1.0 O A:HOH569 4.5 44.6 1.0 CD A:LYS364 4.9 61.5 1.0 O A:HOH556 4.9 47.0 1.0

Bromine binding site 5 out of 5 in the Glycoside Hydrolase-Like Protein


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 5 of Glycoside Hydrolase-Like Protein within 5.0Å range: probe atom residue distance (Å) B Occ A:Br405 b:54.1 occ:0.61 NE2 A:GLN293 3.2 64.9 1.0 ND2 A:ASN41 3.3 45.3 1.0 CG A:GLN293 3.4 57.1 1.0 CB A:ASN41 3.8 43.7 1.0 CD A:GLN293 3.8 63.2 1.0 CG A:ASN41 4.0 45.0 1.0 CD1 A:LEU44 4.4 48.8 1.0 ND2 A:ASN335 4.5 36.5 1.0 CD2 A:LEU44 4.5 43.9 1.0 CB A:GLN293 4.7 55.8 1.0 CG A:ASN335 4.7 36.1 1.0 CG A:LEU44 4.8 47.5 1.0 OD1 A:ASN335 5.0 40.4 1.0

C.S.Robb, A.A.Mystkowska, J.H.Hehemann. Crystal Structure of A Marine Glycoside Hydrolase Family 99-Related Protein Lacking Catalytic Machinery. Protein Sci. V. 26 2445 2017.
ISSN: ESSN 1469-896X
PubMed: 28884852
DOI: 10.1002/PRO.3291