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Calcium in PDB 3gc1: Crystal Structure of Bovine Lactoperoxidase

Enzymatic activity of Crystal Structure of Bovine Lactoperoxidase

All present enzymatic activity of Crystal Structure of Bovine Lactoperoxidase:
1.11.1.7;

Protein crystallography data

The structure of Crystal Structure of Bovine Lactoperoxidase, PDB code: 3gc1 was solved by A.K.Singh, N.Singh, M.Sinha, P.Kaur, A.Srinivasan, S.Sharma, T.P.Singh, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 24.97 / 2.50
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 53.650, 80.710, 75.680, 90.00, 101.75, 90.00
R / Rfree (%) 24.7 / 26.8

Other elements in 3gc1:

The structure of Crystal Structure of Bovine Lactoperoxidase also contains other interesting chemical elements:

Iodine (I) 7 atoms
Iron (Fe) 1 atom

Calcium Binding Sites:

The binding sites of Calcium atom in the Crystal Structure of Bovine Lactoperoxidase (pdb code 3gc1). 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 Bovine Lactoperoxidase, PDB code: 3gc1:

Calcium binding site 1 out of 1 in 3gc1

Go back to Calcium Binding Sites List in 3gc1
Calcium binding site 1 out of 1 in the Crystal Structure of Bovine Lactoperoxidase


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 Bovine Lactoperoxidase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca606

b:44.3
occ:1.00
O A:ASP110 2.3 35.0 1.0
O A:PHE186 2.3 37.0 1.0
OG A:SER190 2.5 38.7 1.0
OG1 A:THR184 2.5 30.4 1.0
O A:THR184 2.5 34.6 1.0
OD1 A:ASP110 2.7 36.2 1.0
OD1 A:ASP188 2.7 41.1 1.0
C A:ASP110 3.3 35.0 1.0
CG A:ASP188 3.4 41.4 1.0
CB A:SER190 3.4 35.4 1.0
C A:PHE186 3.5 39.1 1.0
C A:THR184 3.5 34.5 1.0
CG A:ASP110 3.5 34.6 1.0
OD2 A:ASP188 3.5 43.7 1.0
CB A:THR184 3.7 33.4 1.0
CA A:THR184 3.9 34.3 1.0
N A:THR184 4.0 35.9 1.0
N A:ASP188 4.0 41.3 1.0
N A:PHE186 4.0 39.7 1.0
CA A:ASP110 4.1 34.8 1.0
N A:LEU111 4.1 34.9 1.0
OD2 A:ASP110 4.2 35.8 1.0
N A:SER190 4.2 36.4 1.0
CA A:PHE186 4.2 39.2 1.0
CA A:LEU111 4.2 34.8 1.0
CB A:ASP110 4.3 34.9 1.0
N A:LEU187 4.5 40.1 1.0
CA A:SER190 4.5 37.2 1.0
CB A:ASP188 4.5 41.2 1.0
CD2 A:LEU111 4.6 38.3 1.0
CA A:LEU187 4.6 40.6 1.0
C A:SER185 4.6 39.1 1.0
N A:SER185 4.6 37.1 1.0
O A:HOH757 4.7 27.4 1.0
CA A:ASP188 4.8 40.3 1.0
CB A:PHE186 4.8 39.5 1.0
C A:LEU187 4.8 41.4 1.0
CG2 A:THR184 4.8 31.9 1.0
N A:ALA189 4.9 38.3 1.0

Reference:

A.K.Singh, R.P.Kumar, N.Pandey, N.Singh, M.Sinha, A.Bhushan, P.Kaur, S.Sharma, T.P.Singh. Mode of Binding of the Tuberculosis Prodrug Isoniazid to Heme Peroxidases: Binding Studies and Crystal Structure of Bovine Lactoperoxidase with Isoniazid at 2.7 A Resolution. J.Biol.Chem. V. 285 1569 2010.
ISSN: ISSN 0021-9258
PubMed: 19907057
DOI: 10.1074/JBC.M109.060327
Page generated: Sat Jul 13 10:34:18 2024

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