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Bromine in PDB 8y9x: Crystal Structure of the Complex of Lactoperoxidase with Four Inorganic Substrates, Scn, I, Br and Cl

Enzymatic activity of Crystal Structure of the Complex of Lactoperoxidase with Four Inorganic Substrates, Scn, I, Br and Cl

All present enzymatic activity of Crystal Structure of the Complex of Lactoperoxidase with Four Inorganic Substrates, Scn, I, Br and Cl:
1.11.1.7;

Protein crystallography data

The structure of Crystal Structure of the Complex of Lactoperoxidase with Four Inorganic Substrates, Scn, I, Br and Cl, PDB code: 8y9x was solved by V.Viswanathan, 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) 43.52 / 2.00
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 53.35, 80.332, 73.391, 90, 103.94, 90
R / Rfree (%) 15.1 / 19.5

Other elements in 8y9x:

The structure of Crystal Structure of the Complex of Lactoperoxidase with Four Inorganic Substrates, Scn, I, Br and Cl also contains other interesting chemical elements:

Chlorine (Cl) 1 atom
Iron (Fe) 1 atom
Iodine (I) 17 atoms
Calcium (Ca) 1 atom

Bromine Binding Sites:

The binding sites of Bromine atom in the Crystal Structure of the Complex of Lactoperoxidase with Four Inorganic Substrates, Scn, I, Br and Cl (pdb code 8y9x). 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 Lactoperoxidase with Four Inorganic Substrates, Scn, I, Br and Cl, PDB code: 8y9x:

Bromine binding site 1 out of 1 in 8y9x

Go back to Bromine Binding Sites List in 8y9x
Bromine binding site 1 out of 1 in the Crystal Structure of the Complex of Lactoperoxidase with Four Inorganic Substrates, Scn, I, Br and Cl


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 Lactoperoxidase with Four Inorganic Substrates, Scn, I, Br and Cl within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Br611

b:26.5
occ:0.60
 O A:HOH1085 1.6 4.1 0.3
CL A:CL612 2.8 18.0 0.7
O A:HOH1105 3.1 43.0 1.0
O A:HOH978 3.5 29.4 1.0
O A:HOH785 3.6 21.9 1.0
C4A A:HEM601 3.6 14.3 1.0
C3A A:HEM601 3.7 15.1 1.0
CG A:GLU258 3.7 14.8 1.0
O A:HOH1085 3.8 7.5 0.3
CD A:ARG255 3.8 18.5 1.0
NA A:HEM601 3.9 13.4 1.0
CB A:ARG255 3.9 16.8 1.0
CG A:ARG255 3.9 18.4 1.0
CHB A:HEM601 4.0 13.9 1.0
C2A A:HEM601 4.0 16.4 1.0
CB A:GLU258 4.0 14.6 1.0
C1A A:HEM601 4.1 14.5 1.0
NE2 A:HIS109 4.2 14.9 1.0
CE1 A:HIS109 4.2 13.1 1.0
CMA A:HEM601 4.2 13.7 1.0
CD A:GLU258 4.3 15.4 1.0
OE1 A:GLU258 4.6 15.4 1.0
C1B A:HEM601 4.7 13.9 1.0
NE2 A:GLN105 4.8 14.2 1.0
OE2 A:GLU258 4.8 16.4 1.0
CAA A:HEM601 4.8 17.0 1.0
CHA A:HEM601 4.9 14.8 1.0
O A:ARG255 5.0 18.7 1.0

Reference:

V.Viswanathan, A.K.Singh, N.Pandey, M.Sinha, P.Kaur, S.Sharma, T.P.Singh. Structural Evidence For the Order of Preference of Inorganic Substrates in Mammalian Heme Peroxidases: Crystal Structure of the Complex of Lactoperoxidase with Four Inorganic Substrates, Scn, I, Br and Cl To Be Published.
Page generated: Mon Jul 7 12:44:27 2025

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