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Calcium 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:

Bromine (Br) 1 atom
Iodine (I) 9 atoms
Iron (Fe) 1 atom

Calcium Binding Sites:

The binding sites of Calcium 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 Calcium atom.
In total only one binding site of Calcium was determined in the Crystal Structure of the Complex of Bovine Lactoperoxidase with Carbon Monoxide at 2.0 A Resolution, PDB code: 3v6q:

Calcium binding site 1 out of 1 in 3v6q

Go back to Calcium Binding Sites List in 3v6q
Calcium 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 Calcium with other atoms in the Ca 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:Ca602

b:24.7
occ:1.00
 O A:ASP110 2.2 23.0 1.0
O A:THR184 2.3 21.7 1.0
OD1 A:ASP188 2.3 22.8 1.0
O A:PHE186 2.4 25.5 1.0
OD1 A:ASP110 2.4 27.4 1.0
OG1 A:THR184 2.5 23.6 1.0
OG A:SER190 2.6 25.5 1.0
C A:ASP110 3.2 22.7 1.0
CG A:ASP188 3.3 26.6 1.0
C A:THR184 3.3 22.5 1.0
CB A:SER190 3.5 26.9 1.0
CG A:ASP110 3.5 27.3 1.0
C A:PHE186 3.6 26.2 1.0
OD2 A:ASP188 3.6 29.5 1.0
CB A:THR184 3.7 22.0 1.0
CA A:THR184 3.8 21.3 1.0
N A:ASP188 3.9 24.8 1.0
N A:THR184 3.9 21.7 1.0
CA A:ASP110 4.1 23.8 1.0
N A:PHE186 4.2 25.6 1.0
N A:LEU111 4.2 23.7 1.0
CB A:ASP110 4.3 23.7 1.0
N A:SER190 4.3 26.7 1.0
N A:SER185 4.4 23.0 1.0
CA A:LEU111 4.4 21.4 1.0
CA A:PHE186 4.5 25.8 1.0
C A:SER185 4.5 23.7 1.0
OD2 A:ASP110 4.5 30.9 1.0
N A:LEU187 4.5 25.6 1.0
CB A:ASP188 4.5 24.7 1.0
CA A:LEU187 4.5 25.4 1.0
CA A:SER190 4.6 25.6 1.0
CA A:ASP188 4.7 25.3 1.0
O A:HOH766 4.7 20.8 1.0
CD2 A:LEU111 4.7 17.5 1.0
C A:LEU187 4.8 25.2 1.0
CA A:SER185 4.8 24.2 1.0
CG2 A:THR184 4.8 19.8 1.0
O A:SER185 4.9 24.3 1.0
C A:VAL183 5.0 20.7 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 Jul 13 20:35:32 2024

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