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Iron in PDB 4fdq: The Crystal Structures of Several Mutants of Pleurotus Eryngii Versatile Peroxidase

Enzymatic activity of The Crystal Structures of Several Mutants of Pleurotus Eryngii Versatile Peroxidase

All present enzymatic activity of The Crystal Structures of Several Mutants of Pleurotus Eryngii Versatile Peroxidase:
1.11.1.16;

Protein crystallography data

The structure of The Crystal Structures of Several Mutants of Pleurotus Eryngii Versatile Peroxidase, PDB code: 4fdq was solved by M.J.Mate, A.Romero, F.J.Ruiz-Duenas, A.T.Martinez, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 48.12 / 1.60
Space group I 41
Cell size a, b, c (Å), α, β, γ (°) 96.230, 96.230, 98.730, 90.00, 90.00, 90.00
R / Rfree (%) 15.3 / 17.9

Other elements in 4fdq:

The structure of The Crystal Structures of Several Mutants of Pleurotus Eryngii Versatile Peroxidase also contains other interesting chemical elements:

Calcium (Ca) 2 atoms

Iron Binding Sites:

The binding sites of Iron atom in the The Crystal Structures of Several Mutants of Pleurotus Eryngii Versatile Peroxidase (pdb code 4fdq). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total only one binding site of Iron was determined in the The Crystal Structures of Several Mutants of Pleurotus Eryngii Versatile Peroxidase, PDB code: 4fdq:

Iron binding site 1 out of 1 in 4fdq

Go back to Iron Binding Sites List in 4fdq
Iron binding site 1 out of 1 in the The Crystal Structures of Several Mutants of Pleurotus Eryngii Versatile Peroxidase


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of The Crystal Structures of Several Mutants of Pleurotus Eryngii Versatile Peroxidase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe403

b:7.8
occ:1.00
 FE A:HEM403 0.0 7.8 1.0
NA A:HEM403 2.0 5.8 1.0
ND A:HEM403 2.0 8.1 1.0
NB A:HEM403 2.1 9.1 1.0
NC A:HEM403 2.1 5.8 1.0
NE2 A:HIS169 2.2 6.8 1.0
O A:HOH671 2.6 15.8 1.0
C1A A:HEM403 3.0 7.3 1.0
C1D A:HEM403 3.0 7.2 1.0
C1C A:HEM403 3.1 6.2 1.0
C4A A:HEM403 3.1 7.0 1.0
C4C A:HEM403 3.1 6.7 1.0
C4B A:HEM403 3.1 7.7 1.0
C4D A:HEM403 3.1 6.6 1.0
CE1 A:HIS169 3.1 6.0 1.0
C1B A:HEM403 3.1 7.0 1.0
CD2 A:HIS169 3.2 7.9 1.0
CHD A:HEM403 3.4 5.5 1.0
CHC A:HEM403 3.5 5.6 1.0
CHA A:HEM403 3.5 5.1 1.0
CHB A:HEM403 3.5 6.3 1.0
C2C A:HEM403 4.3 6.1 1.0
C2D A:HEM403 4.3 6.2 1.0
C3A A:HEM403 4.3 8.2 1.0
ND1 A:HIS169 4.3 5.5 1.0
C3D A:HEM403 4.3 7.2 1.0
C2A A:HEM403 4.3 7.5 1.0
CG A:HIS169 4.3 5.6 1.0
C2B A:HEM403 4.3 5.5 1.0
C3C A:HEM403 4.3 6.9 1.0
C3B A:HEM403 4.3 6.3 1.0
O A:HOH526 4.9 12.7 1.0
CD2 A:LEU166 4.9 9.7 1.0
CE2 A:PHE186 5.0 7.2 1.0
OG A:SER168 5.0 7.5 1.0

Reference:

M.Morales, M.J.Mate, A.Romero, M.J.Martinez, A.T.Martinez, F.J.Ruiz-Duenas. Two Oxidation Sites For Low Redox Potential Substrates: A Directed Mutagenesis, Kinetic, and Crystallographic Study on Pleurotus Eryngii Versatile Peroxidase. J.Biol.Chem. V. 287 41053 2012.
ISSN: ISSN 0021-9258
PubMed: 23071108
DOI: 10.1074/JBC.M112.405548
Page generated: Mon Aug 5 02:13:44 2024

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