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Sodium 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
Calcium (Ca) 2 atoms

Sodium Binding Sites:

The binding sites of Sodium atom in the Banyan Peroxidase with Glycosylation (pdb code 4cuo). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total only one binding site of Sodium was determined in the Banyan Peroxidase with Glycosylation, PDB code: 4cuo:

Sodium binding site 1 out of 1 in 4cuo

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


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Banyan Peroxidase with Glycosylation within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na1328

b:24.3
occ:0.50
CA A:CA1327 0.6 34.8 0.5
OG A:SER52 2.2 32.0 1.0
OD1 A:ASP43 2.2 30.1 1.0
OD1 A:ASP50 2.4 31.5 1.0
O A:ASP43 2.5 30.0 1.0
O A:VAL46 2.6 32.5 1.0
O A:GLY48 2.6 30.4 1.0
CB A:SER52 3.3 32.8 1.0
C A:ASP43 3.3 27.0 1.0
CG A:ASP43 3.4 29.3 1.0
CG A:ASP50 3.5 32.8 1.0
N A:SER52 3.6 30.5 1.0
CA A:ASP43 3.6 25.7 1.0
C A:VAL46 3.7 32.8 1.0
C A:GLY48 3.9 30.7 1.0
CA A:SER52 3.9 30.8 1.0
N A:ASP50 4.0 30.1 1.0
CB A:ASP43 4.1 26.8 1.0
OD2 A:ASP50 4.1 34.5 1.0
O A:HOH2070 4.2 42.6 1.0
N A:GLY48 4.3 35.4 1.0
CB A:VAL46 4.3 29.7 1.0
N A:LEU53 4.4 30.3 1.0
OD2 A:ASP43 4.4 29.4 1.0
CA A:VAL46 4.4 31.5 1.0
N A:CYS44 4.4 27.7 1.0
OE1 A:GLU64 4.4 32.5 1.0
N A:VAL46 4.5 32.2 1.0
N A:GLY51 4.5 29.3 1.0
C A:ASN47 4.6 38.7 1.0
CB A:ASP50 4.6 30.2 1.0
C A:SER52 4.6 29.4 1.0
C A:ASP50 4.7 30.0 1.0
CA A:ASP50 4.7 29.8 1.0
C A:GLY51 4.7 27.1 1.0
O A:HIS42 4.7 30.4 1.0
CA A:GLY48 4.8 33.5 1.0
N A:ASN47 4.8 32.7 1.0
O A:HOH2075 4.8 39.3 1.0
N A:CYS49 4.8 31.3 1.0
CA A:CYS49 4.9 29.8 1.0
OE2 A:GLU64 4.9 34.9 1.0
CB A:ASN47 4.9 37.9 1.0
C A:CYS49 4.9 31.4 1.0
N A:ASP43 5.0 29.1 1.0
CA A:CYS44 5.0 28.2 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: Mon Oct 7 14:48:12 2024

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