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Iron in PDB 4czo: Crystal Structure of the Extralong Fungal Manganese Peroxidase From Ceriporiopsis Subvermispora in Complex with Manganese

Enzymatic activity of Crystal Structure of the Extralong Fungal Manganese Peroxidase From Ceriporiopsis Subvermispora in Complex with Manganese

All present enzymatic activity of Crystal Structure of the Extralong Fungal Manganese Peroxidase From Ceriporiopsis Subvermispora in Complex with Manganese:
1.11.1.13;

Protein crystallography data

The structure of Crystal Structure of the Extralong Fungal Manganese Peroxidase From Ceriporiopsis Subvermispora in Complex with Manganese, PDB code: 4czo 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) 33.461 / 1.20
Space group P 43 21 2
Cell size a, b, c (Å), α, β, γ (°) 108.450, 108.450, 68.530, 90.00, 90.00, 90.00
R / Rfree (%) 13.93 / 15.37

Other elements in 4czo:

The structure of Crystal Structure of the Extralong Fungal Manganese Peroxidase From Ceriporiopsis Subvermispora in Complex with Manganese also contains other interesting chemical elements:

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

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of the Extralong Fungal Manganese Peroxidase From Ceriporiopsis Subvermispora in Complex with Manganese (pdb code 4czo). 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 the Extralong Fungal Manganese Peroxidase From Ceriporiopsis Subvermispora in Complex with Manganese, PDB code: 4czo:

Iron binding site 1 out of 1 in 4czo

Go back to Iron Binding Sites List in 4czo
Iron binding site 1 out of 1 in the Crystal Structure of the Extralong Fungal Manganese Peroxidase From Ceriporiopsis Subvermispora in Complex with Manganese


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 the Extralong Fungal Manganese Peroxidase From Ceriporiopsis Subvermispora in Complex with Manganese within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe1374

b:10.9
occ:1.00
 FE A:HEM1374 0.0 10.9 1.0
NB A:HEM1374 2.0 11.5 1.0
NC A:HEM1374 2.1 10.7 1.0
NA A:HEM1374 2.1 11.3 1.0
ND A:HEM1374 2.1 10.6 1.0
NE2 A:HIS173 2.2 10.9 1.0
O A:HOH2092 2.5 18.7 0.5
C4B A:HEM1374 3.0 11.5 1.0
C1C A:HEM1374 3.1 10.7 1.0
C1D A:HEM1374 3.1 10.2 1.0
C1B A:HEM1374 3.1 10.9 1.0
C4A A:HEM1374 3.1 11.4 1.0
C1A A:HEM1374 3.1 11.0 1.0
C4C A:HEM1374 3.1 10.4 1.0
C4D A:HEM1374 3.1 10.6 1.0
CE1 A:HIS173 3.1 10.7 1.0
CD2 A:HIS173 3.2 10.6 1.0
HE1 A:HIS173 3.3 12.8 1.0
HD2 A:HIS173 3.3 12.7 1.0
CHC A:HEM1374 3.4 11.1 1.0
CHB A:HEM1374 3.4 11.4 1.0
CHD A:HEM1374 3.4 10.5 1.0
CHA A:HEM1374 3.4 11.2 1.0
ND1 A:HIS173 4.2 10.6 1.0
C2D A:HEM1374 4.3 10.5 1.0
C3B A:HEM1374 4.3 12.1 1.0
C3D A:HEM1374 4.3 10.6 1.0
C2B A:HEM1374 4.3 11.6 1.0
C2C A:HEM1374 4.3 10.8 1.0
O A:HOH2086 4.3 21.9 1.0
C3A A:HEM1374 4.3 11.4 1.0
C3C A:HEM1374 4.3 10.6 1.0
CG A:HIS173 4.3 10.5 1.0
C2A A:HEM1374 4.3 11.1 1.0
HG3 A:ARG42 4.3 15.2 1.0
HHC A:HEM1374 4.4 13.2 1.0
HE2 A:PHE190 4.4 14.4 1.0
HHB A:HEM1374 4.4 13.6 1.0
HHD A:HEM1374 4.4 12.6 1.0
HHA A:HEM1374 4.4 13.4 1.0
HD11 A:LEU170 4.4 14.7 1.0
HD12 A:LEU170 4.5 14.7 1.0
HG A:SER172 4.6 17.1 1.0
HD2 A:PHE45 4.7 20.9 1.0
CD1 A:LEU170 4.9 12.3 1.0
OG A:SER172 5.0 14.3 1.0

Reference:

E.Fernandez-Fueyo, S.Acebes, F.J.Ruiz-Duenas, M.J.Martinez, A.Romero, F.J.Medrano, V.Guallar, A.T.Martinez. Structural Implications of the C-Terminal Tail in the Catalytic and Stability Properties of Manganese Peroxidases From Ligninolytic Fungi Acta Crystallogr.,Sect.D V. 70 3253 2014.
ISSN: ISSN 0907-4449
PubMed: 25478843
DOI: 10.1107/S1399004714022755
Page generated: Mon Aug 5 01:00:44 2024

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