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Sodium in PDB 4czn: Crystal Structure of the Extralong Fungal Manganese Peroxidase From Ceriporiopsis Subvermispora

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

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

Protein crystallography data

The structure of Crystal Structure of the Extralong Fungal Manganese Peroxidase From Ceriporiopsis Subvermispora, PDB code: 4czn 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) 42.626 / 1.20
Space group P 43 21 2
Cell size a, b, c (Å), α, β, γ (°) 108.560, 108.560, 68.850, 90.00, 90.00, 90.00
R / Rfree (%) 13.44 / 15.11

Other elements in 4czn:

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

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

Sodium Binding Sites:

The binding sites of Sodium atom in the Crystal Structure of the Extralong Fungal Manganese Peroxidase From Ceriporiopsis Subvermispora (pdb code 4czn). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total only one binding site of Sodium was determined in the Crystal Structure of the Extralong Fungal Manganese Peroxidase From Ceriporiopsis Subvermispora, PDB code: 4czn:

Sodium binding site 1 out of 1 in 4czn

Go back to Sodium Binding Sites List in 4czn
Sodium binding site 1 out of 1 in the Crystal Structure of the Extralong Fungal Manganese Peroxidase From Ceriporiopsis Subvermispora


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Crystal Structure of the Extralong Fungal Manganese Peroxidase From Ceriporiopsis Subvermispora within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na1371

b:12.3
occ:1.00
 O1D A:HEM1372 2.2 16.7 1.0
O A:HOH2097 2.3 21.7 1.0
O A:HOH2352 2.4 19.6 1.0
OE2 A:GLU35 2.4 18.8 1.0
OD2 A:ASP179 2.4 19.6 1.0
CGD A:HEM1372 2.9 12.1 1.0
O2D A:HEM1372 3.3 12.3 1.0
CD A:GLU35 3.3 15.8 1.0
CG A:ASP179 3.4 16.6 1.0
OE1 A:GLU35 3.6 14.8 1.0
HG2 A:GLU39 3.6 15.6 1.0
HG3 A:GLU39 3.7 15.6 1.0
OD1 A:ASP179 3.8 15.2 1.0
O A:HOH2096 3.9 13.1 1.0
O A:HOH2595 3.9 24.7 1.0
HBD A:HEM1372 4.1 11.4 1.0
CBD A:HEM1372 4.1 9.5 1.0
CG A:GLU39 4.1 13.0 1.0
O A:ARG177 4.3 9.5 1.0
HB2 A:ARG177 4.3 10.2 1.0
O A:HOH2095 4.5 34.4 1.0
HB2 A:ASP179 4.6 16.9 1.0
O2A A:HEM1372 4.6 10.8 1.0
HBDA A:HEM1372 4.6 11.4 1.0
OE2 A:GLU39 4.6 16.1 1.0
CB A:ASP179 4.7 14.1 1.0
O A:HOH2594 4.7 19.9 1.0
H A:ASP179 4.7 11.9 1.0
CG A:GLU35 4.7 12.3 1.0
HG3 A:GLU35 4.8 14.8 1.0
C A:ARG177 4.8 8.7 1.0
HB2 A:HIS38 4.9 10.6 1.0
HA A:GLU39 4.9 9.7 1.0
CD A:GLU39 4.9 15.1 1.0
HA A:ALA187 5.0 11.8 1.0
H A:ARG177 5.0 10.0 1.0
HE A:ARG177 5.0 11.1 1.0
N A:ASP179 5.0 9.9 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 Oct 7 14:48:52 2024

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