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Manganese 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:

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 (pdb code 4czo). 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, PDB code: 4czo:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in 4czo

Go back to Manganese Binding Sites List in 4czo
Manganese binding site 1 out of 2 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 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 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn1372

b:11.6
occ:1.00
 OE2 A:GLU39 2.1 12.5 1.0
O1D A:HEM1374 2.1 11.2 1.0
O A:HOH2078 2.2 12.5 1.0
OE2 A:GLU35 2.2 11.8 1.0
OD2 A:ASP179 2.2 13.3 1.0
O A:HOH2070 2.3 11.7 1.0
CD A:GLU39 3.1 12.8 1.0
CGD A:HEM1374 3.1 11.3 1.0
CG A:ASP179 3.1 12.7 1.0
CD A:GLU35 3.2 11.4 1.0
HG2 A:GLU39 3.2 14.7 1.0
OE1 A:GLU35 3.4 11.9 1.0
OD1 A:ASP179 3.6 12.7 1.0
CG A:GLU39 3.6 12.2 1.0
HG3 A:GLU39 3.7 14.7 1.0
O2D A:HEM1374 3.8 11.1 1.0
HBD A:HEM1374 3.8 12.9 1.0
CBD A:HEM1374 4.0 10.8 1.0
OE1 A:GLU39 4.1 12.9 1.0
O A:HOH2079 4.2 32.7 1.0
O A:HOH2080 4.2 24.7 1.0
O A:HOH2069 4.3 11.1 1.0
O A:HOH2072 4.3 15.4 1.0
O A:HOH2161 4.3 26.4 1.0
O A:ARG177 4.3 10.8 1.0
HB2 A:ASP179 4.3 15.6 1.0
CB A:ASP179 4.4 13.0 1.0
O2A A:HEM1374 4.4 12.4 1.0
HBDA A:HEM1374 4.5 12.9 1.0
HB2 A:ARG177 4.5 12.5 1.0
CG A:GLU35 4.5 11.2 1.0
HG3 A:GLU35 4.6 13.4 1.0
O A:HOH2071 4.6 34.7 1.0
H A:ASP179 4.6 14.3 1.0
HH11 A:ARG42 4.8 19.8 1.0
HG2 A:GLU35 4.9 13.4 1.0
N A:ASP179 4.9 12.0 1.0
C A:ARG177 5.0 10.5 1.0
HA A:ALA187 5.0 15.1 1.0
HB3 A:ASP179 5.0 15.6 1.0

Manganese binding site 2 out of 2 in 4czo

Go back to Manganese Binding Sites List in 4czo
Manganese binding site 2 out of 2 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 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 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn1373

b:29.4
occ:1.00
 O A:HOH2161 2.0 26.4 1.0
O A:HOH2160 2.1 33.5 1.0
OD2 A:ASP85 2.2 19.5 1.0
O A:HOH2488 2.3 39.2 1.0
O A:HOH2157 2.5 24.9 1.0
O A:HOH2079 2.7 32.7 1.0
CG A:ASP85 3.2 18.7 1.0
OD1 A:ASP85 3.6 20.3 1.0
HE2 A:LYS180 3.9 26.4 1.0
O A:HOH2072 4.0 15.4 1.0
O A:HOH2298 4.0 32.3 1.0
HA2 A:GLY82 4.2 16.1 1.0
HB2 A:ASP85 4.4 17.6 1.0
CB A:ASP85 4.4 14.7 1.0
OD2 A:ASP179 4.4 13.3 1.0
O A:HOH2080 4.4 24.7 1.0
HB3 A:ASP179 4.4 15.6 1.0
HB2 A:ASP179 4.5 15.6 1.0
O A:GLY82 4.5 13.2 1.0
CB A:ASP179 4.8 13.0 1.0
OD1 A:ASP84 4.8 17.2 1.0
HA3 A:GLY82 4.8 16.1 1.0
HB3 A:ASP85 4.9 17.6 1.0
CE A:LYS180 4.9 22.0 1.0
CA A:GLY82 4.9 13.4 1.0
CG A:ASP179 5.0 12.7 1.0
H A:ASP85 5.0 15.6 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: Tue Dec 15 04:18:58 2020

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