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Calcium in PDB 4cuo: Banyan Peroxidase with Glycosylation

Enzymatic activity of Banyan Peroxidase with Glycosylation

All present enzymatic activity of Banyan Peroxidase with Glycosylation:
1.11.1.7;

Protein crystallography data

The structure of Banyan Peroxidase with Glycosylation, PDB code: 4cuo was solved by G.J.Palm, A.Sharma, W.Hinrichs, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 63.32 / 1.67
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 73.115, 73.115, 164.596, 90.00, 90.00, 120.00
R / Rfree (%) 15.654 / 18.029

Other elements in 4cuo:

The structure of Banyan Peroxidase with Glycosylation also contains other interesting chemical elements:

Iron (Fe) 1 atom
Chlorine (Cl) 3 atoms
Sodium (Na) 1 atom

Calcium Binding Sites:

The binding sites of Calcium atom in the Banyan Peroxidase with Glycosylation (pdb code 4cuo). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Banyan Peroxidase with Glycosylation, PDB code: 4cuo:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in 4cuo

Go back to Calcium Binding Sites List in 4cuo
Calcium binding site 1 out of 2 in the Banyan Peroxidase with Glycosylation


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Banyan Peroxidase with Glycosylation within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca1326

b:32.4
occ:1.00
O A:THR170 2.3 29.0 1.0
OD2 A:ASP221 2.3 31.8 1.0
O A:ALA227 2.3 32.5 1.0
O A:THR224 2.4 32.0 1.0
OG1 A:THR224 2.4 37.3 1.0
OD1 A:ASP229 2.5 34.8 1.0
OG1 A:THR170 2.5 31.4 1.0
CG A:ASP221 3.3 33.0 1.0
C A:THR170 3.4 28.6 1.0
CG A:ASP229 3.4 36.4 1.0
C A:THR224 3.4 33.5 1.0
CB A:THR224 3.5 37.8 1.0
C A:ALA227 3.6 33.6 1.0
CB A:THR170 3.6 29.5 1.0
CA A:THR170 3.8 28.3 1.0
OD2 A:ASP229 3.8 39.2 1.0
CA A:THR224 3.9 34.9 1.0
CB A:ASP221 3.9 32.0 1.0
OD1 A:ASP221 4.2 31.8 1.0
N A:ASP229 4.2 34.9 1.0
N A:ALA227 4.3 33.6 1.0
CG2 A:THR170 4.3 29.3 1.0
CA A:ALA227 4.3 34.6 1.0
N A:THR224 4.3 33.4 1.0
CB A:LYS231 4.5 37.2 1.0
N A:PHE171 4.5 28.4 1.0
CB A:ALA227 4.5 34.6 1.0
N A:PRO225 4.6 32.9 1.0
N A:PHE228 4.6 32.3 1.0
O A:ASP229 4.7 34.2 1.0
CB A:ASP229 4.7 35.8 1.0
CA A:PHE228 4.8 32.3 1.0
CA A:ASP229 4.9 35.6 1.0
CG2 A:THR224 4.9 37.5 1.0
C A:PRO225 4.9 30.4 1.0
C A:ASP229 4.9 36.9 1.0
N A:LYS231 4.9 35.3 1.0
C A:PHE228 5.0 35.7 1.0
CA A:PRO225 5.0 31.5 1.0

Calcium binding site 2 out of 2 in 4cuo

Go back to Calcium Binding Sites List in 4cuo
Calcium binding site 2 out of 2 in the Banyan Peroxidase with Glycosylation


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Banyan Peroxidase with Glycosylation within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca1327

b:34.8
occ:0.50
NA A:NA1328 0.6 24.3 0.5
O A:VAL46 2.2 32.5 1.0
O A:GLY48 2.2 30.4 1.0
O A:ASP43 2.3 30.0 1.0
OD1 A:ASP50 2.5 31.5 1.0
OD1 A:ASP43 2.5 30.1 1.0
OG A:SER52 2.7 32.0 1.0
C A:ASP43 3.2 27.0 1.0
C A:VAL46 3.3 32.8 1.0
CG A:ASP50 3.4 32.8 1.0
C A:GLY48 3.4 30.7 1.0
CG A:ASP43 3.7 29.3 1.0
CB A:SER52 3.7 32.8 1.0
N A:GLY48 3.7 35.4 1.0
CA A:ASP43 3.8 25.7 1.0
OD2 A:ASP50 3.9 34.5 1.0
N A:ASP50 4.0 30.1 1.0
C A:ASN47 4.0 38.7 1.0
N A:SER52 4.1 30.5 1.0
CA A:VAL46 4.1 31.5 1.0
N A:VAL46 4.1 32.2 1.0
CA A:GLY48 4.2 33.5 1.0
O A:HOH2070 4.2 42.6 1.0
CB A:VAL46 4.2 29.7 1.0
N A:ASN47 4.3 32.7 1.0
N A:CYS44 4.3 27.7 1.0
CB A:ASP43 4.3 26.8 1.0
N A:CYS49 4.4 31.3 1.0
CA A:SER52 4.4 30.8 1.0
O A:ASN47 4.5 46.8 1.0
CA A:ASN47 4.5 35.7 1.0
CB A:ASP50 4.5 30.2 1.0
CB A:ASN47 4.5 37.9 1.0
CA A:CYS49 4.6 29.8 1.0
OD2 A:ASP43 4.6 29.4 1.0
CA A:CYS44 4.7 28.2 1.0
CA A:ASP50 4.7 29.8 1.0
C A:CYS44 4.7 28.1 1.0
C A:CYS49 4.8 31.4 1.0
O A:HOH2075 4.8 39.3 1.0
O A:CYS44 4.8 31.9 1.0
N A:GLY51 4.8 29.3 1.0
OE1 A:GLU64 4.9 32.5 1.0
C A:ASP50 4.9 30.0 1.0
O A:HIS42 4.9 30.4 1.0
N A:LEU53 5.0 30.3 1.0

Reference:

G.J.Palm, A.Sharma, M.Kumari, S.Panjikar, D.Albrecht, M.V.Jagannadham, W.Hinrichs. Post-Translational Modification and Extended Glycosylation Pattern of A Plant Latex Peroxidase of Native Source Characterized By X-Ray Crystallography. Febs J. V. 281 4319 2014.
ISSN: ISSN 1742-464X
PubMed: 24980207
DOI: 10.1111/FEBS.12900
Page generated: Sat Dec 12 04:42:53 2020

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