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Iron in PDB 4bm4: Crystal Structure of Manganese Peroxidase 4 From Pleurotus Ostreatus - Crystal Form IV

Enzymatic activity of Crystal Structure of Manganese Peroxidase 4 From Pleurotus Ostreatus - Crystal Form IV

All present enzymatic activity of Crystal Structure of Manganese Peroxidase 4 From Pleurotus Ostreatus - Crystal Form IV:
1.11.1.13;

Protein crystallography data

The structure of Crystal Structure of Manganese Peroxidase 4 From Pleurotus Ostreatus - Crystal Form IV, PDB code: 4bm4 was solved by F.J.Medrano, A.Romero, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 43.250 / 2.30
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 123.870, 86.500, 41.400, 90.00, 108.05, 90.00
R / Rfree (%) 22.49 / 29.71

Other elements in 4bm4:

The structure of Crystal Structure of Manganese Peroxidase 4 From Pleurotus Ostreatus - Crystal Form IV also contains other interesting chemical elements:

Calcium (Ca) 2 atoms

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of Manganese Peroxidase 4 From Pleurotus Ostreatus - Crystal Form IV (pdb code 4bm4). 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 Crystal Structure of Manganese Peroxidase 4 From Pleurotus Ostreatus - Crystal Form IV, PDB code: 4bm4:

Iron binding site 1 out of 1 in 4bm4

Go back to Iron Binding Sites List in 4bm4
Iron binding site 1 out of 1 in the Crystal Structure of Manganese Peroxidase 4 From Pleurotus Ostreatus - Crystal Form IV


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Crystal Structure of Manganese Peroxidase 4 From Pleurotus Ostreatus - Crystal Form IV within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe500

b:18.1
occ:1.00
 FE A:HEM500 0.0 18.1 1.0
NC A:HEM500 2.0 5.8 1.0
NA A:HEM500 2.1 22.1 1.0
ND A:HEM500 2.1 8.9 1.0
NB A:HEM500 2.1 1.6 1.0
NE2 A:HIS176 2.3 7.4 1.0
O A:HOH2022 2.6 7.0 1.0
C4C A:HEM500 3.0 0.0 1.0
C1D A:HEM500 3.1 6.1 1.0
C4A A:HEM500 3.1 15.4 1.0
C1A A:HEM500 3.1 27.1 1.0
C4D A:HEM500 3.1 8.5 1.0
C1C A:HEM500 3.1 2.6 1.0
C1B A:HEM500 3.1 10.1 1.0
C4B A:HEM500 3.2 13.4 1.0
CE1 A:HIS176 3.2 21.8 1.0
CD2 A:HIS176 3.4 23.6 1.0
CHD A:HEM500 3.4 0.0 1.0
CHB A:HEM500 3.4 11.3 1.0
CHA A:HEM500 3.5 23.7 1.0
CHC A:HEM500 3.5 22.1 1.0
O A:HOH2025 3.7 14.0 1.0
C3C A:HEM500 4.2 7.2 1.0
C3A A:HEM500 4.3 22.4 1.0
C2C A:HEM500 4.3 2.9 1.0
C2D A:HEM500 4.3 3.3 1.0
C2A A:HEM500 4.3 26.8 1.0
C3D A:HEM500 4.3 1.1 1.0
C2B A:HEM500 4.4 18.9 1.0
ND1 A:HIS176 4.4 27.2 1.0
C3B A:HEM500 4.4 11.2 1.0
CG A:HIS176 4.5 26.9 1.0
CG A:ARG44 4.7 45.9 1.0
O A:HOH2021 4.8 43.2 1.0
OG A:SER175 4.8 16.2 1.0
CD2 A:PHE47 4.9 32.4 1.0
CD A:ARG44 5.0 53.7 1.0
CD2 A:LEU173 5.0 31.8 1.0

Reference:

E.Fernandez-Fueyo, F.J.Ruiz-Duenas, M.J.Martinez, A.Romero, K.E.Hammel, F.J.Medrano, A.T.Martinez. Ligninolytic Peroxidase Genes in the Oyster Mushroom Genome: Heterologous Expression, Molecular Structure, Catalytic and Stability Properties, and Lignin-Degrading Ability. Biotechnol.Biofuels V. 7 2 2014.
ISSN: ISSN 1754-6834
PubMed: 24387130
DOI: 10.1186/1754-6834-7-2
Page generated: Mon Aug 5 00:07:18 2024

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