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Manganese in PDB 2j18: Chloroperoxidase Mixture of Ferric and Ferrous States (Low Dose Data Set)

Enzymatic activity of Chloroperoxidase Mixture of Ferric and Ferrous States (Low Dose Data Set)

All present enzymatic activity of Chloroperoxidase Mixture of Ferric and Ferrous States (Low Dose Data Set):
1.11.1.10;

Protein crystallography data

The structure of Chloroperoxidase Mixture of Ferric and Ferrous States (Low Dose Data Set), PDB code: 2j18 was solved by T.Beitlich, K.Kuhnel, C.Schulze-Briese, R.L.Shoeman, I.Schlichting, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.75 / 1.75
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 57.730, 150.460, 100.750, 90.00, 90.00, 90.00
R / Rfree (%) 17.4 / 20.6

Other elements in 2j18:

The structure of Chloroperoxidase Mixture of Ferric and Ferrous States (Low Dose Data Set) 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 Mixture of Ferric and Ferrous States (Low Dose Data Set) (pdb code 2j18). 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 Mixture of Ferric and Ferrous States (Low Dose Data Set), PDB code: 2j18:

Manganese binding site 1 out of 1 in 2j18

Go back to Manganese Binding Sites List in 2j18
Manganese binding site 1 out of 1 in the Chloroperoxidase Mixture of Ferric and Ferrous States (Low Dose Data Set)


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Chloroperoxidase Mixture of Ferric and Ferrous States (Low Dose Data Set) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn1299

b:5.6
occ:0.60
 O A:HIS105 2.0 8.5 1.0
OE2 A:GLU104 2.0 10.6 1.0
O1A A:HEM1300 2.0 8.6 1.0
OG A:SER108 2.0 6.5 1.0
O A:HOH2333 2.3 10.3 1.0
O A:HOH2334 2.4 8.4 1.0
CD A:GLU104 3.1 9.5 1.0
CGA A:HEM1300 3.1 8.3 1.0
C A:HIS105 3.2 8.1 1.0
CB A:SER108 3.3 7.0 1.0
O2A A:HEM1300 3.5 8.5 1.0
N A:HIS105 3.6 7.7 1.0
CG A:GLU104 3.6 7.1 1.0
CA A:HIS105 4.0 8.8 1.0
O A:HOH2162 4.1 9.4 1.0
OE1 A:GLU104 4.2 7.9 1.0
O A:HOH2059 4.2 5.3 1.0
N A:ASP106 4.3 9.6 1.0
CA A:SER108 4.4 7.7 1.0
N A:SER108 4.4 7.0 1.0
ND1 A:HIS105 4.4 8.8 1.0
CBA A:HEM1300 4.4 7.7 1.0
O A:ASN127 4.5 8.4 1.0
CA A:ASP106 4.6 8.4 1.0
C A:GLU104 4.6 9.0 1.0
OD1 A:ASP113 4.6 9.8 1.0
CB A:ARG111 4.6 8.1 1.0
C A:ASP106 4.7 8.1 1.0
CG A:HIS105 4.7 9.0 1.0
O A:ASP106 4.7 7.8 1.0
O A:LYS112 4.8 9.1 1.0
CB A:GLU104 4.8 8.7 1.0
CE1 A:HIS105 4.8 8.4 1.0
CA A:GLU104 4.8 8.4 1.0
CB A:HIS105 5.0 7.8 1.0
CAA A:HEM1300 5.0 6.2 1.0

Reference:

T.Beitlich, K.Kuhnel, C.Schulze-Briese, R.L.Shoeman, I.Schlichting. Cryoradiolytic Reduction of Crystalline Heme Proteins: Analysis By Uv-Vis Spectroscopy and X- Ray Crystallography J.Synchrotron Radiat. V. 14 11 2007.
ISSN: ISSN 0909-0495
PubMed: 17211068
DOI: 10.1107/S0909049506049806
Page generated: Tue Dec 15 04:03:02 2020

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