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Bromine in PDB 3v6q: Crystal Structure of the Complex of Bovine Lactoperoxidase with Carbon Monoxide at 2.0 A Resolution

Enzymatic activity of Crystal Structure of the Complex of Bovine Lactoperoxidase with Carbon Monoxide at 2.0 A Resolution

All present enzymatic activity of Crystal Structure of the Complex of Bovine Lactoperoxidase with Carbon Monoxide at 2.0 A Resolution:
1.11.1.7;

Protein crystallography data

The structure of Crystal Structure of the Complex of Bovine Lactoperoxidase with Carbon Monoxide at 2.0 A Resolution, PDB code: 3v6q was solved by S.Yamini, A.K.Singh, N.Pandey, M.Sinha, P.Kaur, S.Sharma, T.P.Singh, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 44.13 / 2.00
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 54.300, 80.004, 76.551, 90.00, 103.02, 90.00
R / Rfree (%) 19.1 / 24.8

Other elements in 3v6q:

The structure of Crystal Structure of the Complex of Bovine Lactoperoxidase with Carbon Monoxide at 2.0 A Resolution also contains other interesting chemical elements:

Iodine (I) 9 atoms
Iron (Fe) 1 atom
Calcium (Ca) 1 atom

Bromine Binding Sites:

The binding sites of Bromine atom in the Crystal Structure of the Complex of Bovine Lactoperoxidase with Carbon Monoxide at 2.0 A Resolution (pdb code 3v6q). 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 the Complex of Bovine Lactoperoxidase with Carbon Monoxide at 2.0 A Resolution, PDB code: 3v6q:

Bromine binding site 1 out of 1 in 3v6q

Go back to Bromine Binding Sites List in 3v6q
Bromine binding site 1 out of 1 in the Crystal Structure of the Complex of Bovine Lactoperoxidase with Carbon Monoxide at 2.0 A Resolution


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 the Complex of Bovine Lactoperoxidase with Carbon Monoxide at 2.0 A Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Br616

b:29.6
occ:1.00
 O A:HOH1148 3.1 38.5 1.0
O A:HOH1151 3.5 34.5 1.0
O A:CMO621 3.6 36.4 1.0
C4A A:HEM601 3.7 24.5 1.0
CD A:ARG255 3.8 24.7 1.0
CB A:ARG255 3.8 28.6 1.0
C3A A:HEM601 3.8 22.5 1.0
CG A:GLU258 3.8 25.9 1.0
CG A:ARG255 3.9 27.2 1.0
C A:CMO621 3.9 33.2 1.0
NE2 A:HIS109 4.0 26.2 1.0
NA A:HEM601 4.0 25.1 1.0
CHB A:HEM601 4.1 21.3 1.0
CB A:GLU258 4.1 26.9 1.0
CE1 A:HIS109 4.1 24.5 1.0
C2A A:HEM601 4.1 24.8 1.0
CD A:GLU258 4.3 26.9 1.0
C1A A:HEM601 4.3 25.2 1.0
CMA A:HEM601 4.3 19.2 1.0
OE1 A:GLU258 4.6 20.2 1.0
C1B A:HEM601 4.7 23.2 1.0
OE2 A:GLU258 4.8 24.2 1.0
NE2 A:GLN105 4.9 24.7 1.0
O A:ARG255 5.0 27.0 1.0
CAA A:HEM601 5.0 23.2 1.0

Reference:

S.Yamini, A.K.Singh, N.Pandey, M.Sinha, P.Kaur, S.Sharma, T.P.Singh. Crystal Structure of the Complex of Bovine Lactoperoxidase with Carbon Monoxide at 2.0 A Resolution To Be Published.
Page generated: Sat Dec 12 02:16:25 2020

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