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Iron in PDB 2vnz: Crystal Structure of Dithinonite Reduced Soybean Ascorbate Peroxidase Mutant W41A.

Enzymatic activity of Crystal Structure of Dithinonite Reduced Soybean Ascorbate Peroxidase Mutant W41A.

All present enzymatic activity of Crystal Structure of Dithinonite Reduced Soybean Ascorbate Peroxidase Mutant W41A.:
1.11.11.1;

Protein crystallography data

The structure of Crystal Structure of Dithinonite Reduced Soybean Ascorbate Peroxidase Mutant W41A., PDB code: 2vnz was solved by C.L.Metcalfe, S.K.Badyal, E.L.Raven, P.C.E.Moody, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 34.18 / 1.30
Space group P 42 21 2
Cell size a, b, c (Å), α, β, γ (°) 81.780, 81.780, 75.244, 90.00, 90.00, 90.00
R / Rfree (%) 18.1 / 19.9

Other elements in 2vnz:

The structure of Crystal Structure of Dithinonite Reduced Soybean Ascorbate Peroxidase Mutant W41A. also contains other interesting chemical elements:

Sodium (Na) 2 atoms

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of Dithinonite Reduced Soybean Ascorbate Peroxidase Mutant W41A. (pdb code 2vnz). 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 Dithinonite Reduced Soybean Ascorbate Peroxidase Mutant W41A., PDB code: 2vnz:

Iron binding site 1 out of 1 in 2vnz

Go back to Iron Binding Sites List in 2vnz
Iron binding site 1 out of 1 in the Crystal Structure of Dithinonite Reduced Soybean Ascorbate Peroxidase Mutant W41A.


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 Dithinonite Reduced Soybean Ascorbate Peroxidase Mutant W41A. within 5.0Å range:
probe atom residue distance (Å) B Occ
X:Fe251

b:9.2
occ:1.00
 FE X:HEM251 0.0 9.2 1.0
O X:HOH2237 2.0 12.2 1.0
NA X:HEM251 2.0 8.3 1.0
NC X:HEM251 2.0 8.2 1.0
NB X:HEM251 2.1 8.9 1.0
ND X:HEM251 2.1 7.7 1.0
NE2 X:HIS163 2.2 8.9 1.0
C4B X:HEM251 3.0 9.4 1.0
C1A X:HEM251 3.0 7.9 1.0
C4A X:HEM251 3.0 8.8 1.0
C1C X:HEM251 3.1 8.1 1.0
C1B X:HEM251 3.1 9.0 1.0
C4D X:HEM251 3.1 7.8 1.0
C1D X:HEM251 3.1 7.2 1.0
C4C X:HEM251 3.1 7.8 1.0
CD2 X:HIS163 3.1 8.5 1.0
CE1 X:HIS163 3.2 9.3 1.0
CHC X:HEM251 3.4 8.8 1.0
CHA X:HEM251 3.4 7.9 1.0
CHB X:HEM251 3.4 8.7 1.0
CHD X:HEM251 3.4 7.7 1.0
O X:HOH2236 4.0 34.0 1.0
C3B X:HEM251 4.2 9.2 1.0
C2B X:HEM251 4.2 9.5 1.0
C3A X:HEM251 4.3 8.6 1.0
C2A X:HEM251 4.3 8.3 1.0
C2D X:HEM251 4.3 7.4 1.0
CG X:HIS163 4.3 8.7 1.0
C3D X:HEM251 4.3 7.5 1.0
C2C X:HEM251 4.3 7.9 1.0
C3C X:HEM251 4.3 7.8 1.0
ND1 X:HIS163 4.3 9.6 1.0
O X:HOH2044 4.3 17.9 1.0

Reference:

S.K.Badyal, C.L.Metcalfe, J.Basran, I.Efimov, P.C.E.Moody, E.L.Raven. Iron Oxidation State Modulates Active Site Structure in A Heme Peroxidase. Biochemistry V. 47 4403 2008.
ISSN: ISSN 0006-2960
PubMed: 18351739
DOI: 10.1021/BI702337N
Page generated: Sun Aug 4 03:04:51 2024

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