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Iron in PDB 1b80: Rec. Lignin Peroxidase H8 Oxidatively Processed

Enzymatic activity of Rec. Lignin Peroxidase H8 Oxidatively Processed

All present enzymatic activity of Rec. Lignin Peroxidase H8 Oxidatively Processed:
1.11.1.14;

Protein crystallography data

The structure of Rec. Lignin Peroxidase H8 Oxidatively Processed, PDB code: 1b80 was solved by W.Blodig, A.T.Smith, W.A.Doyle, K.Piontek, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 1.73
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 73.480, 94.930, 230.130, 90.00, 90.00, 90.00
R / Rfree (%) 17 / 20.8

Other elements in 1b80:

The structure of Rec. Lignin Peroxidase H8 Oxidatively Processed also contains other interesting chemical elements:

Calcium (Ca) 4 atoms

Iron Binding Sites:

The binding sites of Iron atom in the Rec. Lignin Peroxidase H8 Oxidatively Processed (pdb code 1b80). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Rec. Lignin Peroxidase H8 Oxidatively Processed, PDB code: 1b80:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in 1b80

Go back to Iron Binding Sites List in 1b80
Iron binding site 1 out of 2 in the Rec. Lignin Peroxidase H8 Oxidatively Processed


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Rec. Lignin Peroxidase H8 Oxidatively Processed within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe350

b:11.6
occ:1.00
FE A:HEM350 0.0 11.6 1.0
NB A:HEM350 2.0 13.1 1.0
ND A:HEM350 2.0 10.2 1.0
NC A:HEM350 2.0 11.5 1.0
NA A:HEM350 2.0 11.1 1.0
O A:HOH362 2.1 16.8 1.0
NE2 A:HIS176 2.1 9.8 1.0
C1A A:HEM350 3.0 10.1 1.0
C4C A:HEM350 3.0 12.8 1.0
C1B A:HEM350 3.0 14.4 1.0
C4B A:HEM350 3.0 12.5 1.0
C1D A:HEM350 3.1 10.3 1.0
C4A A:HEM350 3.1 12.3 1.0
C1C A:HEM350 3.1 11.4 1.0
C4D A:HEM350 3.1 9.6 1.0
CD2 A:HIS176 3.1 11.2 1.0
CE1 A:HIS176 3.1 10.9 1.0
CHD A:HEM350 3.4 11.0 1.0
CHB A:HEM350 3.4 11.9 1.0
CHA A:HEM350 3.4 9.2 1.0
CHC A:HEM350 3.4 11.0 1.0
ND1 A:HIS176 4.2 11.1 1.0
CG A:HIS176 4.2 8.9 1.0
C2A A:HEM350 4.3 11.7 1.0
C3A A:HEM350 4.3 11.0 1.0
C2D A:HEM350 4.3 10.9 1.0
C2B A:HEM350 4.3 13.9 1.0
C3D A:HEM350 4.3 10.4 1.0
C3C A:HEM350 4.3 12.4 1.0
C2C A:HEM350 4.3 12.2 1.0
C3B A:HEM350 4.3 13.9 1.0
O A:HOH430 4.5 18.1 1.0
O A:HOH519 4.7 33.5 1.0

Iron binding site 2 out of 2 in 1b80

Go back to Iron Binding Sites List in 1b80
Iron binding site 2 out of 2 in the Rec. Lignin Peroxidase H8 Oxidatively Processed


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Rec. Lignin Peroxidase H8 Oxidatively Processed within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe350

b:11.8
occ:1.00
FE B:HEM350 0.0 11.8 1.0
NA B:HEM350 2.0 12.0 1.0
NB B:HEM350 2.0 11.1 1.0
ND B:HEM350 2.0 10.7 1.0
NC B:HEM350 2.0 11.9 1.0
O B:HOH361 2.1 15.0 1.0
NE2 B:HIS176 2.1 10.1 1.0
C4A B:HEM350 3.0 12.7 1.0
C4D B:HEM350 3.0 10.6 1.0
C1B B:HEM350 3.0 13.8 1.0
C1A B:HEM350 3.0 10.6 1.0
C1C B:HEM350 3.1 11.8 1.0
C1D B:HEM350 3.1 10.9 1.0
C4B B:HEM350 3.1 11.9 1.0
CE1 B:HIS176 3.1 11.1 1.0
C4C B:HEM350 3.1 10.7 1.0
CD2 B:HIS176 3.2 9.9 1.0
CHB B:HEM350 3.4 13.4 1.0
CHC B:HEM350 3.4 12.3 1.0
CHA B:HEM350 3.4 9.8 1.0
CHD B:HEM350 3.5 11.8 1.0
C3D B:HEM350 4.2 10.9 1.0
C3A B:HEM350 4.2 12.5 1.0
ND1 B:HIS176 4.2 11.7 1.0
C2D B:HEM350 4.2 11.6 1.0
C2A B:HEM350 4.3 13.2 1.0
C2B B:HEM350 4.3 13.6 1.0
C3B B:HEM350 4.3 12.7 1.0
CG B:HIS176 4.3 11.1 1.0
C2C B:HEM350 4.3 11.1 1.0
C3C B:HEM350 4.3 10.7 1.0
O B:HOH456 4.5 18.6 1.0
O B:HOH486 4.6 27.1 1.0

Reference:

W.Blodig, A.T.Smith, W.A.Doyle, K.Piontek. Crystal Structures of Pristine and Oxidatively Processed Lignin Peroxidase Expressed in Escherichia Coli and of the W171F Variant That Eliminates the Redox Active Tryptophan 171. Implications For the Reaction Mechanism. J.Mol.Biol. V. 305 851 2001.
ISSN: ISSN 0022-2836
PubMed: 11162097
DOI: 10.1006/JMBI.2000.4346
Page generated: Sat Aug 3 02:40:15 2024

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