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Manganese in PDB 4czp: Crystal Structure of the Extralong Fungal Manganese Peroxidase From Ceriporiopsis Subvermispora in Complex with Manganese (Anomalous Data)

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

All present enzymatic activity of Crystal Structure of the Extralong Fungal Manganese Peroxidase From Ceriporiopsis Subvermispora in Complex with Manganese (Anomalous Data):
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 (Anomalous Data), PDB code: 4czp 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) 48.576 / 1.90
Space group P 43 21 2
Cell size a, b, c (Å), α, β, γ (°) 108.620, 108.620, 68.200, 90.00, 90.00, 90.00
R / Rfree (%) 16.73 / 19.13

Other elements in 4czp:

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

Iron (Fe) 1 atom
Calcium (Ca) 2 atoms

Manganese Binding Sites:

The binding sites of Manganese atom in the Crystal Structure of the Extralong Fungal Manganese Peroxidase From Ceriporiopsis Subvermispora in Complex with Manganese (Anomalous Data) (pdb code 4czp). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the Crystal Structure of the Extralong Fungal Manganese Peroxidase From Ceriporiopsis Subvermispora in Complex with Manganese (Anomalous Data), PDB code: 4czp:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in 4czp

Go back to Manganese Binding Sites List in 4czp
Manganese binding site 1 out of 2 in the Crystal Structure of the Extralong Fungal Manganese Peroxidase From Ceriporiopsis Subvermispora in Complex with Manganese (Anomalous Data)


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Crystal Structure of the Extralong Fungal Manganese Peroxidase From Ceriporiopsis Subvermispora in Complex with Manganese (Anomalous Data) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn1372

b:25.2
occ:1.00
 OE2 A:GLU39 2.1 26.4 1.0
O1D A:HEM1374 2.1 23.7 1.0
O A:HOH2043 2.1 22.7 1.0
OD2 A:ASP179 2.2 25.8 1.0
OE2 A:GLU35 2.2 24.0 1.0
O A:HOH2035 2.2 22.9 1.0
CD A:GLU39 3.0 26.5 1.0
CGD A:HEM1374 3.1 22.6 1.0
CG A:ASP179 3.1 25.8 1.0
CD A:GLU35 3.2 22.8 1.0
OE1 A:GLU35 3.4 26.6 1.0
CG A:GLU39 3.6 21.5 1.0
OD1 A:ASP179 3.6 23.8 1.0
O2D A:HEM1374 3.7 21.2 1.0
CBD A:HEM1374 4.0 19.6 1.0
OE1 A:GLU39 4.0 26.3 1.0
O A:HOH2034 4.2 22.8 1.0
O A:HOH2036 4.2 27.1 1.0
O A:ARG177 4.3 20.5 1.0
CB A:ASP179 4.4 24.6 1.0
O A:HOH2042 4.4 40.1 1.0
O A:HOH2044 4.4 34.8 1.0
O A:HOH2085 4.4 42.1 1.0
O2A A:HEM1374 4.4 24.0 1.0
CG A:GLU35 4.5 22.4 1.0
N A:ASP179 4.9 24.3 1.0
C A:ARG177 5.0 20.2 1.0

Manganese binding site 2 out of 2 in 4czp

Go back to Manganese Binding Sites List in 4czp
Manganese binding site 2 out of 2 in the Crystal Structure of the Extralong Fungal Manganese Peroxidase From Ceriporiopsis Subvermispora in Complex with Manganese (Anomalous Data)


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Crystal Structure of the Extralong Fungal Manganese Peroxidase From Ceriporiopsis Subvermispora in Complex with Manganese (Anomalous Data) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn1373

b:52.9
occ:1.00
 O A:HOH2295 1.8 48.1 1.0
O A:HOH2085 2.0 42.1 1.0
OD2 A:ASP85 2.1 33.2 1.0
O A:HOH2086 2.2 42.5 1.0
O A:HOH2083 2.4 38.7 1.0
O A:HOH2042 2.5 40.1 1.0
CG A:ASP85 3.1 35.2 1.0
OD1 A:ASP85 3.6 34.1 1.0
O A:HOH2036 3.8 27.1 1.0
CB A:ASP85 4.3 29.0 1.0
O A:GLY82 4.4 27.6 1.0
OD2 A:ASP179 4.5 25.8 1.0
O A:HOH2044 4.6 34.8 1.0
O A:HOH2172 4.8 43.6 1.0
OD1 A:ASP84 4.8 31.6 1.0
CB A:ASP179 4.9 24.6 1.0
CE A:LYS180 4.9 34.5 1.0
CA A:GLY82 4.9 30.2 1.0
OE2 A:GLU39 5.0 26.4 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: Sat Aug 16 13:39:29 2025

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