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Manganese in PDB 2cj1: Chloroperoxidase Complexed with Formate (Ethylene Glycol Cryoprotectant)

Enzymatic activity of Chloroperoxidase Complexed with Formate (Ethylene Glycol Cryoprotectant)

All present enzymatic activity of Chloroperoxidase Complexed with Formate (Ethylene Glycol Cryoprotectant):
1.11.1.10;

Protein crystallography data

The structure of Chloroperoxidase Complexed with Formate (Ethylene Glycol Cryoprotectant), PDB code: 2cj1 was solved by K.Kuhnel, W.Blankenfeldt, J.Terner, I.Schlichting, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.75 / 1.7
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 58.280, 150.330, 99.690, 90.00, 90.00, 90.00
R / Rfree (%) 18.9 / 22.9

Other elements in 2cj1:

The structure of Chloroperoxidase Complexed with Formate (Ethylene Glycol Cryoprotectant) also contains other interesting chemical elements:

Iron (Fe) 1 atom

Manganese Binding Sites:

The binding sites of Manganese atom in the Chloroperoxidase Complexed with Formate (Ethylene Glycol Cryoprotectant) (pdb code 2cj1). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total only one binding site of Manganese was determined in the Chloroperoxidase Complexed with Formate (Ethylene Glycol Cryoprotectant), PDB code: 2cj1:

Manganese binding site 1 out of 1 in 2cj1

Go back to Manganese Binding Sites List in 2cj1
Manganese binding site 1 out of 1 in the Chloroperoxidase Complexed with Formate (Ethylene Glycol Cryoprotectant)


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Chloroperoxidase Complexed with Formate (Ethylene Glycol Cryoprotectant) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn1299

b:20.8
occ:1.00
 O A:HIS105 2.0 17.4 1.0
OE2 A:GLU104 2.0 15.9 1.0
O1A A:HEM1300 2.0 17.3 1.0
OG A:SER108 2.0 14.8 1.0
O A:HOH2321 2.3 14.1 1.0
O A:HOH2320 2.4 18.0 1.0
CD A:GLU104 3.0 15.2 1.0
CGA A:HEM1300 3.1 13.1 1.0
C A:HIS105 3.2 16.2 1.0
CB A:SER108 3.3 14.7 1.0
CG A:GLU104 3.5 13.2 1.0
O2A A:HEM1300 3.5 13.8 1.0
N A:HIS105 3.6 15.4 1.0
CA A:HIS105 4.0 16.0 1.0
O A:HOH2074 4.1 13.8 1.0
OE1 A:GLU104 4.1 16.3 1.0
O A:HOH2174 4.2 16.2 1.0
N A:ASP106 4.3 17.0 1.0
CA A:SER108 4.4 15.4 1.0
N A:SER108 4.4 15.0 1.0
ND1 A:HIS105 4.4 15.4 1.0
CBA A:HEM1300 4.4 14.0 1.0
O A:ASN127 4.5 16.2 1.0
CA A:ASP106 4.6 15.9 1.0
C A:GLU104 4.6 15.8 1.0
OD1 A:ASP113 4.6 20.6 1.0
CB A:ARG111 4.6 14.9 1.0
CG A:HIS105 4.7 15.6 1.0
C A:ASP106 4.7 15.7 1.0
CB A:GLU104 4.7 14.4 1.0
O A:ASP106 4.8 15.4 1.0
CA A:GLU104 4.8 15.0 1.0
O A:LYS112 4.8 17.7 1.0
CE1 A:HIS105 4.8 15.6 1.0
CB A:HIS105 5.0 15.7 1.0
CAA A:HEM1300 5.0 11.2 1.0

Reference:

K.Kuhnel, W.Blankenfeldt, J.Terner, I.Schlichting. Crystal Structures of Chloroperoxidase with Its Bound Substrates and Complexed with Formate, Acetate, and Nitrate. J.Biol.Chem. V. 281 23990 2006.
ISSN: ISSN 0021-9258
PubMed: 16790441
DOI: 10.1074/JBC.M603166200
Page generated: Sat Oct 5 13:39:26 2024

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