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Calcium in PDB 5gh0: Crystal Structure of the Complex of Bovine Lactoperoxidase with Mercaptoimidazole at 2.3 A Resolution

Enzymatic activity of Crystal Structure of the Complex of Bovine Lactoperoxidase with Mercaptoimidazole at 2.3 A Resolution

All present enzymatic activity of Crystal Structure of the Complex of Bovine Lactoperoxidase with Mercaptoimidazole at 2.3 A Resolution:
1.11.1.7;

Protein crystallography data

The structure of Crystal Structure of the Complex of Bovine Lactoperoxidase with Mercaptoimidazole at 2.3 A Resolution, PDB code: 5gh0 was solved by P.K.Singh, H.V.Sirohi, A.K.Singh, A.Bhushan, 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) 20.00 / 2.30
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 54.630, 80.667, 77.680, 90.00, 102.60, 90.00
R / Rfree (%) 14.2 / 19.4

Other elements in 5gh0:

The structure of Crystal Structure of the Complex of Bovine Lactoperoxidase with Mercaptoimidazole at 2.3 A Resolution also contains other interesting chemical elements:

Iron (Fe) 1 atom

Calcium Binding Sites:

The binding sites of Calcium atom in the Crystal Structure of the Complex of Bovine Lactoperoxidase with Mercaptoimidazole at 2.3 A Resolution (pdb code 5gh0). 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 Mercaptoimidazole at 2.3 A Resolution, PDB code: 5gh0:

Calcium binding site 1 out of 1 in 5gh0

Go back to Calcium Binding Sites List in 5gh0
Calcium binding site 1 out of 1 in the Crystal Structure of the Complex of Bovine Lactoperoxidase with Mercaptoimidazole at 2.3 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 Mercaptoimidazole at 2.3 A Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca610

b:14.0
occ:1.00
 OD1 A:ASP110 2.3 15.8 1.0
O A:ASP110 2.3 11.6 1.0
O A:PHE186 2.4 15.5 1.0
OD1 A:ASP188 2.4 15.3 1.0
O A:THR184 2.4 15.2 1.0
OG1 A:THR184 2.5 14.5 1.0
OG A:SER190 2.5 15.2 1.0
C A:THR184 3.4 14.2 1.0
CG A:ASP188 3.4 17.0 1.0
C A:ASP110 3.4 12.6 1.0
CG A:ASP110 3.4 16.3 1.0
CB A:SER190 3.6 15.7 1.0
C A:PHE186 3.6 15.6 1.0
CB A:THR184 3.7 14.2 1.0
OD2 A:ASP188 3.8 16.6 1.0
CA A:THR184 3.9 13.9 1.0
N A:ASP188 4.1 16.5 1.0
N A:THR184 4.1 14.7 1.0
CA A:ASP110 4.1 13.4 1.0
N A:PHE186 4.2 15.5 1.0
CB A:ASP110 4.3 14.1 1.0
N A:SER190 4.3 15.0 1.0
OD2 A:ASP110 4.3 19.2 1.0
N A:LEU111 4.3 12.4 1.0
N A:SER185 4.4 14.4 1.0
C A:SER185 4.5 15.6 1.0
CA A:PHE186 4.5 14.3 1.0
CA A:LEU111 4.5 12.0 1.0
N A:LEU187 4.5 16.4 1.0
CB A:ASP188 4.6 16.1 1.0
CA A:SER190 4.6 15.4 1.0
CA A:LEU187 4.6 16.8 1.0
O A:HOH748 4.6 9.2 1.0
CA A:ASP188 4.8 15.4 1.0
CD2 A:LEU111 4.8 12.1 1.0
CG2 A:THR184 4.8 14.2 1.0
C A:LEU187 4.8 16.2 1.0
CA A:SER185 4.9 15.1 1.0
O A:SER185 4.9 16.3 1.0

Reference:

H.V.Sirohi, P.K.Singh, N.Iqbal, P.Sharma, A.K.Singh, P.Kaur, S.Sharma, T.P.Singh. Design of Anti-Thyroid Drugs: Binding Studies and Structure Determination of the Complex of Lactoperoxidase with 2-Mercaptoimidazole at 2.30 Angstrom Resolution Proteins V. 85 1882 2017.
ISSN: ESSN 1097-0134
PubMed: 28653416
DOI: 10.1002/PROT.25342
Page generated: Sun Jul 14 19:34:20 2024

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