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Manganese in PDB 2cix: Chloroperoxidase Complexed with Cyclopentanedione

Enzymatic activity of Chloroperoxidase Complexed with Cyclopentanedione

All present enzymatic activity of Chloroperoxidase Complexed with Cyclopentanedione:
1.11.1.10;

Protein crystallography data

The structure of Chloroperoxidase Complexed with Cyclopentanedione, PDB code: 2cix 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) 19.73 / 1.8
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 57.440, 150.350, 99.620, 90.00, 90.00, 90.00
R / Rfree (%) 17.8 / 21.7

Other elements in 2cix:

The structure of Chloroperoxidase Complexed with Cyclopentanedione also contains other interesting chemical elements:

Bromine (Br) 3 atoms
Iron (Fe) 1 atom

Manganese Binding Sites:

The binding sites of Manganese atom in the Chloroperoxidase Complexed with Cyclopentanedione (pdb code 2cix). 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 Cyclopentanedione, PDB code: 2cix:

Manganese binding site 1 out of 1 in 2cix

Go back to Manganese Binding Sites List in 2cix
Manganese binding site 1 out of 1 in the Chloroperoxidase Complexed with Cyclopentanedione


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 Cyclopentanedione within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn1299

b:20.3
occ:1.00
OE2 A:GLU104 2.0 17.4 1.0
O A:HIS105 2.0 16.9 1.0
OG A:SER108 2.0 15.7 1.0
O1A A:HEM1300 2.0 15.0 1.0
O A:HOH2315 2.2 17.3 1.0
O A:HOH2316 2.3 17.0 1.0
CD A:GLU104 3.1 19.1 1.0
CGA A:HEM1300 3.1 14.3 1.0
C A:HIS105 3.2 16.4 1.0
CB A:SER108 3.3 15.9 1.0
O2A A:HEM1300 3.5 15.4 1.0
CG A:GLU104 3.6 15.1 1.0
N A:HIS105 3.6 15.8 1.0
CA A:HIS105 4.1 16.4 1.0
OE1 A:GLU104 4.1 19.0 1.0
O A:HOH2058 4.2 12.6 1.0
O A:HOH2155 4.2 17.4 1.0
N A:ASP106 4.3 16.7 1.0
CA A:SER108 4.4 16.2 1.0
O A:ASN127 4.4 17.9 1.0
N A:SER108 4.4 15.8 1.0
CBA A:HEM1300 4.5 12.4 1.0
ND1 A:HIS105 4.5 16.4 1.0
CA A:ASP106 4.6 15.7 1.0
CB A:ARG111 4.6 13.4 1.0
C A:GLU104 4.6 16.7 1.0
OD1 A:ASP113 4.6 20.1 1.0
C A:ASP106 4.7 15.0 1.0
O A:LYS112 4.7 16.5 1.0
O A:ASP106 4.7 15.5 1.0
CG A:HIS105 4.7 16.7 1.0
CB A:GLU104 4.8 16.2 1.0
CE1 A:HIS105 4.8 14.7 1.0
CA A:GLU104 4.8 15.8 1.0
CAA A:HEM1300 5.0 11.4 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 13:38:50 2024

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