Bromine in PDB 2hyp: Crystal Structure of RV0805 D66A Mutant

All present enzymatic activity of Crystal Structure of RV0805 D66A Mutant:
3.1.4.17;

The structure of Crystal Structure of RV0805 D66A Mutant, PDB code: 2hyp was solved by A.R.Shenoy, M.Capuder, P.Draskovic, D.Lamba, S.S.Visweswariah, M.Podobnik, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 2.05
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	55.297, 93.709, 50.924, 90.00, 90.00, 90.00
R / Rfree (%)	20.8 / 25.7

The structure of Crystal Structure of RV0805 D66A Mutant also contains other interesting chemical elements:

Arsenic	(As)	1 atom
Manganese	(Mn)	1 atom
Iron	(Fe)	1 atom

The binding sites of Bromine atom in the Crystal Structure of RV0805 D66A Mutant (pdb code 2hyp). This binding sites where shown within 5.0 Angstroms radius around Bromine atom.
In total 4 binding sites of Bromine where determined in the Crystal Structure of RV0805 D66A Mutant, PDB code: 2hyp:
Jump to Bromine binding site number: 1; 2; 3; 4;

Bromine binding site 1 out of 4 in the Crystal Structure of RV0805 D66A 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 RV0805 D66A Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:Br301 b:60.4 occ:0.40 O A:HOH601 3.4 51.7 1.0 C A:PRO113 3.6 62.7 1.0 N A:SER114 3.7 61.9 1.0 O A:PRO113 3.7 62.8 1.0 CA A:SER114 3.8 61.0 1.0 CB A:ALA102 3.8 58.4 1.0 CB A:PRO113 3.9 63.2 1.0 C A:SER114 4.0 60.2 1.0 N A:MET115 4.2 59.5 1.0 CA A:PRO113 4.4 63.2 1.0 CG A:MET115 4.4 59.9 1.0 O A:SER114 4.6 59.8 1.0 CG A:PRO113 4.8 63.4 1.0 CA A:ALA102 4.9 58.6 1.0

Bromine binding site 2 out of 4 in the Crystal Structure of RV0805 D66A Mutant


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 2 of Crystal Structure of RV0805 D66A Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:Br302 b:47.2 occ:0.40 N A:ASP257 3.4 58.5 1.0 CB A:TYR255 3.7 55.9 1.0 CB A:ASP257 3.7 60.1 1.0 CG2 A:THR258 3.9 56.8 1.0 CA A:ASP257 3.9 59.1 1.0 N A:THR258 4.0 57.5 1.0 OD2 A:ASP257 4.1 66.0 1.0 CD A:PRO256 4.2 57.0 1.0 C A:ASP257 4.2 58.4 1.0 N A:PRO256 4.2 57.4 1.0 CG A:ASP257 4.4 62.8 1.0 CG A:TYR255 4.5 56.2 1.0 C A:PRO256 4.5 58.3 1.0 C A:TYR255 4.6 56.2 1.0 CB A:THR258 4.6 57.2 1.0 CB A:PRO256 4.7 57.8 1.0 CA A:PRO256 4.7 57.9 1.0 CA A:TYR255 4.8 55.9 1.0 CD1 A:TYR255 4.8 56.0 1.0 CA A:THR258 4.9 57.0 1.0 CG A:PRO256 4.9 58.0 1.0

Bromine binding site 3 out of 4 in the Crystal Structure of RV0805 D66A Mutant


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 3 of Crystal Structure of RV0805 D66A Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:Br303 b:31.4 occ:0.35 NH1 A:ARG145 2.9 66.8 1.0 NH1 A:ARG101 3.1 57.9 1.0 NH2 A:ARG101 3.6 55.8 1.0 CZ A:ARG101 3.8 56.1 1.0 O A:HOH562 4.1 47.2 1.0 CZ A:ARG145 4.2 66.8 1.0 CD A:PRO137 4.3 53.6 1.0 CG A:PRO117 4.4 57.0 1.0 CG A:PRO137 4.7 53.0 1.0 CD A:PRO117 4.7 56.4 1.0 CD A:ARG145 4.9 65.3 1.0 O A:MET115 5.0 58.5 1.0 NH2 A:ARG145 5.0 68.6 1.0 O A:SER135 5.0 55.4 1.0

Bromine binding site 4 out of 4 in the Crystal Structure of RV0805 D66A Mutant


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 4 of Crystal Structure of RV0805 D66A Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:Br304 b:53.7 occ:0.50 O A:HOH603 3.0 66.9 1.0 N A:VAL121 3.3 63.7 1.0 CB A:VAL121 3.9 64.0 1.0 CG2 A:VAL121 4.0 64.2 1.0 CA A:ARG120 4.0 64.1 1.0 CD A:ARG120 4.0 67.8 1.0 C A:ARG120 4.1 63.9 1.0 CA A:VAL121 4.1 64.2 1.0 O A:VAL121 4.2 64.1 1.0 CG A:ARG120 4.3 66.6 1.0 CZ2 A:TRP151 4.4 58.7 1.0 C A:VAL121 4.7 64.2 1.0 CB A:ARG120 4.7 64.3 1.0 O A:ASP119 5.0 62.1 1.0

A.R.Shenoy, M.Capuder, P.Draskovic, D.Lamba, S.S.Visweswariah, M.Podobnik. Structural and Biochemical Analysis of the RV0805 Cyclic Nucleotide Phosphodiesterase From Mycobacterium Tuberculosis. J.Mol.Biol. V. 365 211 2007.
ISSN: ISSN 0022-2836
PubMed: 17059828
DOI: 10.1016/J.JMB.2006.10.005