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Iron in PDB 1v0h: Ascobate Peroxidase From Soybean Cytosol in Complex with Salicylhydroxamic Acid

Enzymatic activity of Ascobate Peroxidase From Soybean Cytosol in Complex with Salicylhydroxamic Acid

All present enzymatic activity of Ascobate Peroxidase From Soybean Cytosol in Complex with Salicylhydroxamic Acid:
1.11.1.11;

Protein crystallography data

The structure of Ascobate Peroxidase From Soybean Cytosol in Complex with Salicylhydroxamic Acid, PDB code: 1v0h was solved by K.H.Sharp, 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) 55.90 / 1.46
Space group P 42 21 2
Cell size a, b, c (Å), α, β, γ (°) 82.770, 82.770, 74.991, 90.00, 90.00, 90.00
R / Rfree (%) 15 / 18.2

Other elements in 1v0h:

The structure of Ascobate Peroxidase From Soybean Cytosol in Complex with Salicylhydroxamic Acid also contains other interesting chemical elements:

Sodium (Na) 1 atom

Iron Binding Sites:

The binding sites of Iron atom in the Ascobate Peroxidase From Soybean Cytosol in Complex with Salicylhydroxamic Acid (pdb code 1v0h). 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 Ascobate Peroxidase From Soybean Cytosol in Complex with Salicylhydroxamic Acid, PDB code: 1v0h:

Iron binding site 1 out of 1 in 1v0h

Go back to Iron Binding Sites List in 1v0h
Iron binding site 1 out of 1 in the Ascobate Peroxidase From Soybean Cytosol in Complex with Salicylhydroxamic Acid


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Ascobate Peroxidase From Soybean Cytosol in Complex with Salicylhydroxamic Acid within 5.0Å range:
probe atom residue distance (Å) B Occ
X:Fe251

b:9.4
occ:1.00
 FE X:HEM251 0.0 9.4 1.0
NA X:HEM251 2.0 9.4 1.0
NC X:HEM251 2.0 8.7 1.0
ND X:HEM251 2.0 8.3 1.0
NB X:HEM251 2.0 9.2 1.0
O9 X:SHA253 2.1 11.7 1.0
NE2 X:HIS163 2.2 9.9 1.0
N8 X:SHA253 2.9 13.3 1.0
C4B X:HEM251 3.0 9.0 1.0
C1C X:HEM251 3.0 9.2 1.0
C1A X:HEM251 3.0 8.9 1.0
C4A X:HEM251 3.0 9.5 1.0
C4D X:HEM251 3.0 8.5 1.0
C1D X:HEM251 3.0 7.0 1.0
C4C X:HEM251 3.1 8.3 1.0
C1B X:HEM251 3.1 9.2 1.0
CD2 X:HIS163 3.1 13.0 1.0
CE1 X:HIS163 3.1 12.0 1.0
CHC X:HEM251 3.4 9.6 1.0
CHB X:HEM251 3.4 10.8 1.0
CHA X:HEM251 3.4 9.3 1.0
CHD X:HEM251 3.4 7.7 1.0
C7 X:SHA253 3.8 13.9 1.0
NE1 X:TRP41 4.0 10.4 1.0
O7 X:SHA253 4.1 14.0 1.0
ND1 X:HIS163 4.2 12.6 1.0
CG X:HIS163 4.2 10.1 1.0
C2A X:HEM251 4.2 10.4 1.0
C3A X:HEM251 4.3 10.0 1.0
C2D X:HEM251 4.3 8.4 1.0
C3C X:HEM251 4.3 9.2 1.0
C2C X:HEM251 4.3 9.1 1.0
C3B X:HEM251 4.3 9.9 1.0
C2B X:HEM251 4.3 10.6 1.0
C3D X:HEM251 4.3 9.2 1.0
CD1 X:TRP41 4.7 9.7 1.0
C1 X:SHA253 4.9 14.8 1.0

Reference:

K.H.Sharp, P.C.E.Moody, K.A.Brown, E.L.Raven. Crystal Structure of the Ascorbate Peroxidase-Salicylhydroxamic Acid Complex Biochemistry V. 43 8644 2004.
ISSN: ISSN 0006-2960
PubMed: 15236572
DOI: 10.1021/BI049343Q
Page generated: Sun Dec 13 14:33:59 2020

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