Bromine in PDB 5opp: Crystal Structure of S408R Cn-II Mutant

All present enzymatic activity of Crystal Structure of S408R Cn-II Mutant:
3.1.3.5;

The structure of Crystal Structure of S408R Cn-II Mutant, PDB code: 5opp was solved by A.Hnizda, P.Pachl, P.Rezacova, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	45.83 / 1.70
Space group	I 2 2 2
Cell size a, b, c (Å), α, β, γ (°)	91.668, 127.025, 130.462, 90.00, 90.00, 90.00
R / Rfree (%)	19.1 / 21.5

The structure of Crystal Structure of S408R Cn-II Mutant also contains other interesting chemical elements:

Magnesium

(Mg)

1 atom

The binding sites of Bromine atom in the Crystal Structure of S408R Cn-II Mutant (pdb code 5opp). 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 Crystal Structure of S408R Cn-II Mutant, PDB code: 5opp:

Bromine binding site 1 out of 1 in the Crystal Structure of S408R Cn-II Mutant


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 1 of Crystal Structure of S408R Cn-II Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:Br505 b:33.1 occ:1.00 O A:HOH701 3.5 33.1 1.0 CE A:LYS258 4.0 40.9 1.0 CD A:LYS258 4.0 37.5 1.0 CD1 A:TYR255 4.1 27.3 1.0 CE A:LYS254 4.1 43.2 1.0 CA A:TYR255 4.2 26.0 1.0 CG A:LYS254 4.3 36.5 1.0 CB A:LYS215 4.3 32.0 1.0 CB A:TYR255 4.4 26.5 1.0 N A:TYR255 4.4 27.0 1.0 CD A:LYS254 4.5 40.8 1.0 CG1 A:VAL219 4.6 32.3 1.0 CG2 A:VAL219 4.6 35.3 1.0 CG A:TYR255 4.7 26.5 1.0 C A:LYS254 4.8 27.7 1.0 NZ A:LYS254 4.8 46.5 1.0 CD A:LYS215 4.9 37.5 1.0 O A:LYS254 4.9 26.7 1.0 C A:LYS215 4.9 31.7 1.0 O A:LYS215 5.0 31.0 1.0

A.Hnizda, M.Fabry, T.Moriyama, P.Pachl, M.Kugler, V.Brinsa, D.B.Ascher, W.L.Carroll, P.Novak, M.Zaliova, J.Trka, P.Rezacova, J.J.Yang, V.Veverka. Relapsed Acute Lymphoblastic Leukemia-Specific Mutations in NT5C2 Cluster Into Hotspots Driving Intersubunit Stimulation. Leukemia V. 32 1393 2018.
ISSN: ESSN 1476-5551
PubMed: 29535428
DOI: 10.1038/S41375-018-0073-5