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Chlorine 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
Calcium (Ca) 2 atoms
Sodium (Na) 1 atom

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Banyan Peroxidase with Glycosylation (pdb code 4cuo). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 3 binding sites of Chlorine where determined in the Banyan Peroxidase with Glycosylation, PDB code: 4cuo:
Jump to Chlorine binding site number: 1; 2; 3;

Chlorine binding site 1 out of 3 in 4cuo

Go back to Chlorine Binding Sites List in 4cuo
Chlorine binding site 1 out of 3 in the Banyan Peroxidase with Glycosylation


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Banyan Peroxidase with Glycosylation within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl1329

b:29.9
occ:0.30
O A:HOH2060 1.8 31.4 0.7
FE A:HEM1307 2.6 27.9 1.0
NE A:ARG38 2.8 27.2 1.0
NA A:HEM1307 2.9 27.1 1.0
NB A:HEM1307 3.0 30.3 1.0
NE2 A:HIS42 3.1 32.5 1.0
ND A:HEM1307 3.2 28.1 1.0
CE2 A:PHE41 3.2 31.7 1.0
NC A:HEM1307 3.3 27.2 1.0
O A:HOH2060 3.3 42.7 0.3
CD2 A:PHE41 3.4 29.2 1.0
CG A:ARG38 3.5 26.6 1.0
C4A A:HEM1307 3.6 26.8 1.0
CD A:ARG38 3.6 26.4 1.0
O A:HOH2066 3.7 41.2 0.5
C1B A:HEM1307 3.7 28.2 1.0
C1A A:HEM1307 3.7 26.8 1.0
CZ A:ARG38 3.8 29.5 1.0
NH2 A:ARG38 3.8 33.4 1.0
CD2 A:HIS42 3.9 28.6 1.0
CHB A:HEM1307 3.9 28.9 1.0
C4B A:HEM1307 3.9 26.8 1.0
C4C A:HEM1307 3.9 26.2 1.0
C4D A:HEM1307 4.0 26.1 1.0
CE1 A:HIS42 4.0 29.7 1.0
C1C A:HEM1307 4.0 29.6 1.0
C1D A:HEM1307 4.1 28.0 1.0
CHA A:HEM1307 4.2 26.1 1.0
CHC A:HEM1307 4.3 28.1 1.0
CHD A:HEM1307 4.4 28.7 1.0
CZ A:PHE41 4.5 33.4 1.0
C3A A:HEM1307 4.6 27.6 1.0
O A:HOH2066 4.6 37.4 0.5
C2A A:HEM1307 4.7 27.7 1.0
NE2 A:HIS169 4.7 26.4 1.0
CB A:ARG38 4.8 25.4 1.0
CG A:PHE41 4.8 28.5 1.0
C2B A:HEM1307 4.8 29.4 1.0
C2C A:HEM1307 4.9 27.4 1.0
C3C A:HEM1307 4.9 26.9 1.0
CG A:HIS42 4.9 29.3 1.0
ND1 A:HIS42 5.0 29.2 1.0
C3B A:HEM1307 5.0 29.0 1.0

Chlorine binding site 2 out of 3 in 4cuo

Go back to Chlorine Binding Sites List in 4cuo
Chlorine binding site 2 out of 3 in the Banyan Peroxidase with Glycosylation


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Banyan Peroxidase with Glycosylation within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl1330

b:38.7
occ:0.40
O A:HOH2233 1.4 30.7 0.3
O A:HOH2232 1.5 24.8 0.3
O A:HOH2231 2.9 49.3 1.0
ND2 A:ASN219 3.2 29.3 1.0
OG1 A:THR218 3.3 32.4 1.0
N A:ASN219 3.3 30.3 1.0
CG A:ASN219 3.4 30.9 1.0
CA A:THR218 3.7 31.1 1.0
OD1 A:ASN219 3.9 31.5 1.0
O A:HOH2239 3.9 43.5 1.0
C A:THR218 3.9 31.9 1.0
CB A:ASN219 4.0 30.8 1.0
CB A:THR218 4.1 31.0 1.0
CA A:ASN219 4.3 29.8 1.0
O A:HOH2234 4.4 34.6 1.0
NE2 A:GLN222 4.6 30.3 1.0
O A:ILE217 4.6 34.9 1.0
N A:THR218 5.0 30.6 1.0

Chlorine binding site 3 out of 3 in 4cuo

Go back to Chlorine Binding Sites List in 4cuo
Chlorine binding site 3 out of 3 in the Banyan Peroxidase with Glycosylation


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Banyan Peroxidase with Glycosylation within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl1331

b:36.4
occ:0.70
O A:HOH2160 1.3 23.1 0.3
O A:HOH2155 1.6 24.3 0.3
O A:HOH2064 2.8 34.2 1.0
O A:HOH2144 3.3 35.2 1.0
NE1 A:TRP117 3.6 37.6 1.0
CD A:PRO120 3.7 34.8 1.0
CG2 A:THR102 3.7 30.5 1.0
O A:HOH2159 3.7 37.4 1.0
O A:MET279 3.9 34.0 1.0
CA A:ILE280 3.9 36.1 1.0
CG1 A:ILE280 4.0 40.0 1.0
CG1 A:VAL119 4.1 34.3 1.0
C A:MET279 4.2 36.0 1.0
NH2 A:ARG123 4.3 32.0 1.0
N A:ILE280 4.3 35.5 1.0
CD1 A:TRP117 4.5 37.6 1.0
CB A:ILE280 4.6 37.6 1.0
N A:PRO120 4.6 34.6 1.0
CE2 A:TRP117 4.6 36.2 1.0
CA A:VAL119 4.7 35.3 1.0
CG A:PRO120 4.7 38.4 1.0
CA A:GLY283 4.7 31.8 1.0
CB A:VAL119 4.8 35.1 1.0
CZ2 A:TRP117 4.9 36.7 1.0
C A:ILE280 4.9 36.4 1.0
O A:ILE280 4.9 35.9 1.0
O A:PRO120 4.9 33.5 1.0
CB A:MET279 5.0 33.9 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: Fri Jul 11 14:08:03 2025

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