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Calcium in PDB 4oek: Crystal Structure of the Complex of Goat Lactoperoxidase with Phenylethylamine at 2.47 A Resolution

Enzymatic activity of Crystal Structure of the Complex of Goat Lactoperoxidase with Phenylethylamine at 2.47 A Resolution

All present enzymatic activity of Crystal Structure of the Complex of Goat Lactoperoxidase with Phenylethylamine at 2.47 A Resolution:
1.11.1.7;

Protein crystallography data

The structure of Crystal Structure of the Complex of Goat Lactoperoxidase with Phenylethylamine at 2.47 A Resolution, PDB code: 4oek was solved by M.Kumar, R.P.Singh, M.Sinha, 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) 73.69 / 2.47
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 53.166, 79.891, 75.284, 90.00, 101.80, 90.00
R / Rfree (%) 20.4 / 28.1

Other elements in 4oek:

The structure of Crystal Structure of the Complex of Goat Lactoperoxidase with Phenylethylamine at 2.47 A Resolution also contains other interesting chemical elements:

Iodine (I) 13 atoms
Iron (Fe) 1 atom

Calcium Binding Sites:

The binding sites of Calcium atom in the Crystal Structure of the Complex of Goat Lactoperoxidase with Phenylethylamine at 2.47 A Resolution (pdb code 4oek). 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 Goat Lactoperoxidase with Phenylethylamine at 2.47 A Resolution, PDB code: 4oek:

Calcium binding site 1 out of 1 in 4oek

Go back to Calcium Binding Sites List in 4oek
Calcium binding site 1 out of 1 in the Crystal Structure of the Complex of Goat Lactoperoxidase with Phenylethylamine at 2.47 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 Goat Lactoperoxidase with Phenylethylamine at 2.47 A Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca607

b:27.3
occ:1.00
 OD1 A:ASP110 2.1 30.4 1.0
O A:ASP110 2.2 28.3 1.0
O A:PHE186 2.4 31.6 1.0
O A:THR184 2.4 29.8 1.0
OG A:SER190 2.5 33.0 1.0
OG1 A:THR184 2.5 30.6 1.0
OD1 A:ASP188 2.6 33.1 1.0
CG A:ASP110 3.3 30.2 1.0
C A:ASP110 3.3 28.7 1.0
C A:THR184 3.4 31.1 1.0
CG A:ASP188 3.5 34.4 1.0
C A:PHE186 3.5 32.1 1.0
CB A:SER190 3.6 32.3 1.0
CB A:THR184 3.7 30.3 1.0
OD2 A:ASP188 3.9 33.9 1.0
CA A:THR184 3.9 31.0 1.0
CA A:ASP110 4.1 28.8 1.0
N A:PHE186 4.1 32.8 1.0
N A:THR184 4.1 31.1 1.0
OD2 A:ASP110 4.1 32.8 1.0
CB A:ASP110 4.2 29.4 1.0
N A:ASP188 4.2 34.0 1.0
N A:LEU111 4.3 28.2 1.0
C A:SER185 4.3 32.1 1.0
CA A:PHE186 4.4 32.4 1.0
CA A:LEU111 4.4 28.5 1.0
N A:SER185 4.4 30.9 1.0
N A:SER190 4.4 33.0 1.0
N A:LEU187 4.5 33.0 1.0
CD2 A:LEU111 4.6 27.3 1.0
CA A:SER190 4.6 32.4 1.0
CA A:LEU187 4.7 33.0 1.0
O A:SER185 4.7 33.0 1.0
CB A:ASP188 4.7 35.2 1.0
O A:HOH736 4.8 25.8 1.0
CA A:SER185 4.8 31.1 1.0
CG2 A:VAL183 4.8 28.7 1.0
CG2 A:THR184 4.8 31.3 1.0
CA A:ASP188 4.9 34.5 1.0
C A:LEU187 5.0 33.5 1.0

Reference:

M.Kumar, R.P.Singh, M.Sinha, A.Bhushan, P.Kaur, S.Sharma, T.P.Singh. Crystal Structure of the Complex of Goat Lactoperoxidase with Phenylethylamine at 2.47 A To Be Published.
Page generated: Sat Dec 12 05:02:12 2020

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