Iron in PDB 8qx0: Ligninolytic Manganese Peroxidase Ape-MNP1 From Agaricales Mushrooms in Complex with A Manganese Ion

Enzymatic activity of Ligninolytic Manganese Peroxidase Ape-MNP1 From Agaricales Mushrooms in Complex with A Manganese Ion

All present enzymatic activity of Ligninolytic Manganese Peroxidase Ape-MNP1 From Agaricales Mushrooms in Complex with A Manganese Ion:
1.11.1.13;

Protein crystallography data

The structure of Ligninolytic Manganese Peroxidase Ape-MNP1 From Agaricales Mushrooms in Complex with A Manganese Ion, PDB code: 8qx0 was solved by E.Santillana, A.Romero, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 62.28 / 1.25
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 62.63, 39.811, 63.56, 90, 101.5, 90
R / Rfree (%) 17.8 / 19.9

Other elements in 8qx0:

The structure of Ligninolytic Manganese Peroxidase Ape-MNP1 From Agaricales Mushrooms in Complex with A Manganese Ion also contains other interesting chemical elements:

Manganese (Mn) 1 atom
Calcium (Ca) 2 atoms

Iron Binding Sites:

The binding sites of Iron atom in the Ligninolytic Manganese Peroxidase Ape-MNP1 From Agaricales Mushrooms in Complex with A Manganese Ion (pdb code 8qx0). 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 Ligninolytic Manganese Peroxidase Ape-MNP1 From Agaricales Mushrooms in Complex with A Manganese Ion, PDB code: 8qx0:

Iron binding site 1 out of 1 in 8qx0

Go back to Iron Binding Sites List in 8qx0
Iron binding site 1 out of 1 in the Ligninolytic Manganese Peroxidase Ape-MNP1 From Agaricales Mushrooms in Complex with A Manganese Ion


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Ligninolytic Manganese Peroxidase Ape-MNP1 From Agaricales Mushrooms in Complex with A Manganese Ion within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe402

b:7.9
occ:1.00
 FE A:HEM402 0.0 7.9 1.0
NB A:HEM402 2.0 6.5 1.0
NC A:HEM402 2.0 6.9 1.0
ND A:HEM402 2.0 7.7 1.0
NA A:HEM402 2.1 7.0 1.0
NE2 A:HIS171 2.1 8.5 1.0
C4B A:HEM402 3.0 6.6 1.0
C4D A:HEM402 3.0 7.6 1.0
C1D A:HEM402 3.0 6.8 1.0
C1C A:HEM402 3.1 6.8 1.0
CE1 A:HIS171 3.1 8.2 1.0
C4C A:HEM402 3.1 7.1 1.0
C1B A:HEM402 3.1 6.2 1.0
C1A A:HEM402 3.1 7.9 1.0
CD2 A:HIS171 3.1 7.7 1.0
C4A A:HEM402 3.1 7.0 1.0
CHC A:HEM402 3.4 7.0 1.0
CHD A:HEM402 3.4 7.4 1.0
CHB A:HEM402 3.4 6.6 1.0
CHA A:HEM402 3.5 6.9 1.0
ND1 A:HIS171 4.2 9.2 1.0
C3D A:HEM402 4.3 6.4 1.0
C2A A:HEM402 4.3 7.2 1.0
C2C A:HEM402 4.3 7.1 1.0
CG A:HIS171 4.3 7.8 1.0
C2D A:HEM402 4.3 7.6 1.0
C3B A:HEM402 4.3 7.2 1.0
C3A A:HEM402 4.3 7.3 1.0
C2B A:HEM402 4.3 7.1 1.0
C3C A:HEM402 4.4 7.0 1.0
O A:HOH658 4.6 23.5 1.0
CD2 A:PHE45 4.9 11.5 1.0

Reference:

M.I.Sanchez-Ruiz, E.Santillana, D.Linde, A.Romero, A.T.Martinez, F.J.Ruiz-Duenas. Structure-Function Characterization of Two Enzymes From Novel Subfamilies of Manganese Peroxidases Secreted By the Lignocellulose-Degrading Agaricales Fungi Agrocybe Pediades and Cyathus Striatus. Biotechnol Biofuels Bioprod V. 17 74 2024.
ISSN: ISSN 2731-3654
PubMed: 38824538
DOI: 10.1186/S13068-024-02517-1
Page generated: Sat Aug 10 15:55:52 2024

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