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Iron in PDB 2vo2: Crystal Structure of Soybean Ascorbate Peroxidase Mutant W41A Subjected to Low Dose X-Rays

Enzymatic activity of Crystal Structure of Soybean Ascorbate Peroxidase Mutant W41A Subjected to Low Dose X-Rays

All present enzymatic activity of Crystal Structure of Soybean Ascorbate Peroxidase Mutant W41A Subjected to Low Dose X-Rays:
1.11.11.1;

Protein crystallography data

The structure of Crystal Structure of Soybean Ascorbate Peroxidase Mutant W41A Subjected to Low Dose X-Rays, PDB code: 2vo2 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) 36.69 / 1.90
Space group P 42 21 2
Cell size a, b, c (Å), α, β, γ (°) 82.057, 82.057, 75.631, 90.00, 90.00, 90.00
R / Rfree (%) 17.4 / 23.6

Other elements in 2vo2:

The structure of Crystal Structure of Soybean Ascorbate Peroxidase Mutant W41A Subjected to Low Dose X-Rays also contains other interesting chemical elements:

Sodium (Na) 1 atom

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of Soybean Ascorbate Peroxidase Mutant W41A Subjected to Low Dose X-Rays (pdb code 2vo2). 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 Soybean Ascorbate Peroxidase Mutant W41A Subjected to Low Dose X-Rays, PDB code: 2vo2:

Iron binding site 1 out of 1 in 2vo2

Go back to Iron Binding Sites List in 2vo2
Iron binding site 1 out of 1 in the Crystal Structure of Soybean Ascorbate Peroxidase Mutant W41A Subjected to Low Dose X-Rays


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 Soybean Ascorbate Peroxidase Mutant W41A Subjected to Low Dose X-Rays within 5.0Å range:
probe atom residue distance (Å) B Occ
X:Fe1250

b:16.4
occ:1.00
 FE X:HEM1250 0.0 16.4 1.0
NB X:HEM1250 2.0 17.2 1.0
NC X:HEM1250 2.1 14.1 1.0
NA X:HEM1250 2.1 15.5 1.0
ND X:HEM1250 2.1 14.2 1.0
NE2 X:HIS163 2.2 14.8 1.0
NE2 X:HIS42 2.4 21.5 1.0
C4B X:HEM1250 3.0 15.1 1.0
C1C X:HEM1250 3.0 14.1 1.0
CD2 X:HIS163 3.1 11.6 1.0
C1B X:HEM1250 3.1 15.5 1.0
C1A X:HEM1250 3.1 15.8 1.0
C4D X:HEM1250 3.1 11.7 1.0
C4C X:HEM1250 3.1 13.8 1.0
C4A X:HEM1250 3.1 15.2 1.0
C1D X:HEM1250 3.2 13.4 1.0
CE1 X:HIS163 3.2 14.0 1.0
CE1 X:HIS42 3.3 21.9 1.0
CHC X:HEM1250 3.4 14.4 1.0
CD2 X:HIS42 3.4 22.6 1.0
CHA X:HEM1250 3.4 13.0 1.0
CHB X:HEM1250 3.5 13.6 1.0
CHD X:HEM1250 3.5 12.5 1.0
C3B X:HEM1250 4.2 16.2 1.0
CG X:HIS163 4.3 12.7 1.0
C2B X:HEM1250 4.3 15.7 1.0
C2C X:HEM1250 4.3 14.6 1.0
C3C X:HEM1250 4.3 14.6 1.0
C2A X:HEM1250 4.3 15.5 1.0
ND1 X:HIS163 4.3 15.1 1.0
C3A X:HEM1250 4.3 16.4 1.0
C3D X:HEM1250 4.3 11.4 1.0
C2D X:HEM1250 4.4 13.2 1.0
ND1 X:HIS42 4.4 23.4 1.0
CG X:HIS42 4.5 20.6 1.0
O X:HOH2049 4.9 39.5 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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