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Bromine in PDB 5wv3: Crystal Structure of Bovine Lactoperoxidase with A Partial GLU258-Heme Linkage at 2.07 A Resolution.

Enzymatic activity of Crystal Structure of Bovine Lactoperoxidase with A Partial GLU258-Heme Linkage at 2.07 A Resolution.

All present enzymatic activity of Crystal Structure of Bovine Lactoperoxidase with A Partial GLU258-Heme Linkage at 2.07 A Resolution.:
1.11.1.7;

Protein crystallography data

The structure of Crystal Structure of Bovine Lactoperoxidase with A Partial GLU258-Heme Linkage at 2.07 A Resolution., PDB code: 5wv3 was solved by P.K.Singh, H.V.Sirohi, 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) 34.17 / 2.07
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 54.012, 79.809, 66.106, 90.00, 93.01, 90.00
R / Rfree (%) 16.7 / 23.6

Other elements in 5wv3:

The structure of Crystal Structure of Bovine Lactoperoxidase with A Partial GLU258-Heme Linkage at 2.07 A Resolution. also contains other interesting chemical elements:

Iodine (I) 3 atoms
Iron (Fe) 1 atom
Calcium (Ca) 1 atom

Bromine Binding Sites:

The binding sites of Bromine atom in the Crystal Structure of Bovine Lactoperoxidase with A Partial GLU258-Heme Linkage at 2.07 A Resolution. (pdb code 5wv3). 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 Bovine Lactoperoxidase with A Partial GLU258-Heme Linkage at 2.07 A Resolution., PDB code: 5wv3:

Bromine binding site 1 out of 1 in 5wv3

Go back to Bromine Binding Sites List in 5wv3
Bromine binding site 1 out of 1 in the Crystal Structure of Bovine Lactoperoxidase with A Partial GLU258-Heme Linkage at 2.07 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 Bovine Lactoperoxidase with A Partial GLU258-Heme Linkage at 2.07 A Resolution. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Br620

b:53.2
occ:0.50
 OE2 A:GLU258 1.4 42.8 0.5
OE1 A:GLU258 1.6 44.5 0.5
CD A:GLU258 1.7 43.9 0.5
O A:HOH811 2.9 39.6 1.0
CG A:GLU258 3.2 43.7 0.5
O A:HOH838 3.4 68.1 1.0
C4A A:HEM602 3.5 28.2 1.0
O A:HOH889 3.5 40.5 1.0
CG A:GLU258 3.6 40.8 0.5
NE2 A:HIS109 3.7 33.8 1.0
C3A A:HEM602 3.7 28.1 1.0
CE1 A:HIS109 3.7 34.8 1.0
NA A:HEM602 3.8 25.8 1.0
CD A:ARG255 3.8 35.4 1.0
CHB A:HEM602 3.9 27.6 1.0
C2A A:HEM602 3.9 27.5 1.0
C1A A:HEM602 4.0 26.1 1.0
CB A:ARG255 4.0 36.1 1.0
CD A:GLU258 4.0 41.4 0.5
CG A:ARG255 4.1 36.7 1.0
CB A:GLU258 4.2 40.9 1.0
NE2 A:GLN105 4.2 28.9 1.0
CMA A:HEM602 4.3 30.4 1.0
OE1 A:GLU258 4.4 45.1 0.5
C1B A:HEM602 4.4 25.9 1.0
OE2 A:GLU258 4.6 40.7 0.5
CHA A:HEM602 4.7 26.2 1.0
CAA A:HEM602 4.8 28.7 1.0
FE A:HEM602 4.8 28.0 1.0
NB A:HEM602 4.8 27.2 1.0
CD2 A:HIS109 5.0 32.1 1.0
NE A:ARG255 5.0 34.3 1.0

Reference:

P.K.Singh, N.Iqbal, H.V.Sirohi, H.R.Bairagya, P.Kaur, S.Sharma, T.P.Singh. Structural Basis of Activation of Mammalian Heme Peroxidases Prog. Biophys. Mol. Biol. V. 133 49 2018.
ISSN: ISSN 1873-1732
PubMed: 29174286
DOI: 10.1016/J.PBIOMOLBIO.2017.11.003
Page generated: Thu Jul 11 01:16:49 2024

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