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Iron in PDB 1h3j: Structure of Recombinant Coprinus Cinereus Peroxidase Determined to 2.0 A

Enzymatic activity of Structure of Recombinant Coprinus Cinereus Peroxidase Determined to 2.0 A

All present enzymatic activity of Structure of Recombinant Coprinus Cinereus Peroxidase Determined to 2.0 A:
1.11.1.7;

Protein crystallography data

The structure of Structure of Recombinant Coprinus Cinereus Peroxidase Determined to 2.0 A, PDB code: 1h3j was solved by J.F.W.Petersen, K.Houborg, P.Harris, S.Larsen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 8.00 / 2.00
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 127.180, 75.530, 76.600, 90.00, 90.00, 90.00
R / Rfree (%) 18.6 / 25.6

Other elements in 1h3j:

The structure of Structure of Recombinant Coprinus Cinereus Peroxidase Determined to 2.0 A also contains other interesting chemical elements:

Magnesium (Mg) 1 atom
Calcium (Ca) 4 atoms

Iron Binding Sites:

The binding sites of Iron atom in the Structure of Recombinant Coprinus Cinereus Peroxidase Determined to 2.0 A (pdb code 1h3j). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Structure of Recombinant Coprinus Cinereus Peroxidase Determined to 2.0 A, PDB code: 1h3j:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in 1h3j

Go back to Iron Binding Sites List in 1h3j
Iron binding site 1 out of 2 in the Structure of Recombinant Coprinus Cinereus Peroxidase Determined to 2.0 A


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Structure of Recombinant Coprinus Cinereus Peroxidase Determined to 2.0 A within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe401

b:13.5
occ:1.00
FE A:HEM401 0.0 13.5 1.0
ND A:HEM401 2.0 12.8 1.0
NA A:HEM401 2.0 12.1 1.0
NB A:HEM401 2.0 7.4 1.0
NC A:HEM401 2.1 9.6 1.0
NE2 A:HSO183 2.2 9.6 1.0
O A:HOH629 2.4 7.3 1.0
C4A A:HEM401 3.0 10.4 1.0
C1D A:HEM401 3.0 9.5 1.0
C4D A:HEM401 3.0 13.2 1.0
C1B A:HEM401 3.0 7.0 1.0
C4C A:HEM401 3.1 7.0 1.0
C1A A:HEM401 3.1 11.9 1.0
C4B A:HEM401 3.1 7.7 1.0
C1C A:HEM401 3.2 7.6 1.0
CE1 A:HSO183 3.2 12.1 1.0
CD2 A:HSO183 3.2 12.5 1.0
CHB A:HEM401 3.4 8.7 1.0
CHD A:HEM401 3.4 8.9 1.0
CHA A:HEM401 3.5 13.4 1.0
CHC A:HEM401 3.6 7.4 1.0
C3A A:HEM401 4.2 11.2 1.0
C2D A:HEM401 4.2 10.0 1.0
C3D A:HEM401 4.2 11.0 1.0
C2A A:HEM401 4.2 11.7 1.0
C2B A:HEM401 4.3 8.1 1.0
C3B A:HEM401 4.3 9.2 1.0
ND1 A:HSO183 4.4 12.7 1.0
CG A:HSO183 4.4 11.8 1.0
C3C A:HEM401 4.4 6.5 1.0
C2C A:HEM401 4.4 9.0 1.0
O A:HOH675 4.8 12.1 1.0
CG A:ARG51 5.0 16.4 1.0

Iron binding site 2 out of 2 in 1h3j

Go back to Iron Binding Sites List in 1h3j
Iron binding site 2 out of 2 in the Structure of Recombinant Coprinus Cinereus Peroxidase Determined to 2.0 A


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Structure of Recombinant Coprinus Cinereus Peroxidase Determined to 2.0 A within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe401

b:12.9
occ:1.00
FE B:HEM401 0.0 12.9 1.0
ND B:HEM401 1.9 11.5 1.0
NA B:HEM401 2.0 11.3 1.0
NC B:HEM401 2.0 9.1 1.0
NB B:HEM401 2.0 6.2 1.0
NE2 B:HSO183 2.2 8.2 1.0
O B:HOH629 2.3 7.8 1.0
C4A B:HEM401 3.0 8.8 1.0
C1D B:HEM401 3.0 9.8 1.0
C1B B:HEM401 3.0 6.8 1.0
CE1 B:HSO183 3.0 9.8 1.0
C4C B:HEM401 3.0 6.8 1.0
C4D B:HEM401 3.0 10.8 1.0
C1C B:HEM401 3.1 8.4 1.0
C4B B:HEM401 3.1 8.1 1.0
C1A B:HEM401 3.1 10.2 1.0
CD2 B:HSO183 3.2 9.1 1.0
CHB B:HEM401 3.3 6.3 1.0
CHD B:HEM401 3.4 7.4 1.0
CHC B:HEM401 3.5 7.7 1.0
CHA B:HEM401 3.5 9.2 1.0
C2D B:HEM401 4.2 10.0 1.0
C3D B:HEM401 4.2 10.0 1.0
C2B B:HEM401 4.2 8.2 1.0
ND1 B:HSO183 4.2 10.6 1.0
C3A B:HEM401 4.2 7.5 1.0
C3B B:HEM401 4.3 6.9 1.0
C2A B:HEM401 4.3 10.0 1.0
C3C B:HEM401 4.3 7.4 1.0
C2C B:HEM401 4.3 6.3 1.0
CG B:HSO183 4.3 8.2 1.0
O B:HOH591 4.4 26.2 1.0
CG B:ARG51 4.9 14.0 1.0
O B:HOH637 4.9 13.4 1.0

Reference:

K.Houborg, P.Harris, J.F.W.Petersen, P.Rowland, J.Poulsen, P.Schneider, J.Vind, S.Larsen. Impact of the Physical and Chemical Environment on the Molecular Structure of Coprinus Cinereus Peroxidase Acta Crystallogr.,Sect.D V. 59 989 2003.
ISSN: ISSN 0907-4449
PubMed: 12777760
DOI: 10.1107/S0907444903006772
Page generated: Sun Dec 13 14:16:46 2020

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