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Calcium in PDB 2qpk: Crystal Structure of the Complex of Bovine Lactoperoxidase with Salicylhydroxamic Acid at 2.34 A Resolution

Enzymatic activity of Crystal Structure of the Complex of Bovine Lactoperoxidase with Salicylhydroxamic Acid at 2.34 A Resolution

All present enzymatic activity of Crystal Structure of the Complex of Bovine Lactoperoxidase with Salicylhydroxamic Acid at 2.34 A Resolution:
1.11.1.7;

Protein crystallography data

The structure of Crystal Structure of the Complex of Bovine Lactoperoxidase with Salicylhydroxamic Acid at 2.34 A Resolution, PDB code: 2qpk was solved by A.K.Singh, N.Singh, S.Sharma, P.Kaur, T.P.Singh, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 2.34
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 54.618, 80.553, 77.803, 90.00, 102.56, 90.00
R / Rfree (%) 17.2 / 22

Other elements in 2qpk:

The structure of Crystal Structure of the Complex of Bovine Lactoperoxidase with Salicylhydroxamic Acid at 2.34 A Resolution also contains other interesting chemical elements:

Iodine (I) 8 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 Salicylhydroxamic Acid at 2.34 A Resolution (pdb code 2qpk). 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 Salicylhydroxamic Acid at 2.34 A Resolution, PDB code: 2qpk:

Calcium binding site 1 out of 1 in 2qpk

Go back to Calcium Binding Sites List in 2qpk
Calcium binding site 1 out of 1 in the Crystal Structure of the Complex of Bovine Lactoperoxidase with Salicylhydroxamic Acid at 2.34 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 Salicylhydroxamic Acid at 2.34 A Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca606

b:24.4
occ:1.00
OD1 A:ASP110 2.3 28.1 1.0
O A:ASP110 2.4 22.2 1.0
O A:PHE186 2.5 22.2 1.0
OG A:SER190 2.5 20.4 1.0
OD1 A:ASP188 2.6 22.4 1.0
OG1 A:THR184 2.6 21.5 1.0
O A:THR184 2.6 22.2 1.0
C A:ASP110 3.5 21.5 1.0
CB A:SER190 3.5 22.0 1.0
CG A:ASP188 3.5 22.4 1.0
C A:THR184 3.5 21.5 1.0
CG A:ASP110 3.5 25.9 1.0
C A:PHE186 3.7 20.8 1.0
OD2 A:ASP188 3.8 23.8 1.0
CB A:THR184 3.8 22.0 1.0
CA A:THR184 4.0 21.0 1.0
N A:ASP188 4.0 22.8 1.0
N A:THR184 4.1 21.8 1.0
CA A:ASP110 4.2 21.4 1.0
N A:SER190 4.2 22.2 1.0
N A:PHE186 4.2 19.6 1.0
OD2 A:ASP110 4.3 28.6 1.0
CB A:ASP110 4.3 21.6 1.0
N A:LEU111 4.4 22.0 1.0
CA A:SER190 4.5 21.7 1.0
N A:SER185 4.5 21.7 1.0
CA A:PHE186 4.5 20.2 1.0
C A:SER185 4.5 20.7 1.0
CA A:LEU111 4.6 21.8 1.0
N A:LEU187 4.6 21.8 1.0
CA A:LEU187 4.6 22.6 1.0
O A:HOH728 4.6 14.5 1.0
CB A:ASP188 4.7 21.9 1.0
CA A:ASP188 4.8 21.8 1.0
CG2 A:THR184 4.8 20.8 1.0
C A:LEU187 4.8 23.5 1.0
CD2 A:LEU111 4.8 20.8 1.0
CA A:SER185 4.9 20.9 1.0
N A:ALA189 4.9 20.5 1.0

Reference:

P.K.Singh, H.V.Sirohi, N.Iqbal, P.Tiwari, P.Kaur, S.Sharma, T.P.Singh. Structure of Bovine Lactoperoxidase with A Partially Linked Heme Moiety at 1.98 Angstrom Resolution. Biochim.Biophys.Acta V.1865 329 2017.
ISSN: ISSN 0006-3002
PubMed: 27986533
DOI: 10.1016/J.BBAPAP.2016.12.006
Page generated: Sat Dec 12 03:51:08 2020

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