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Iron in PDB 3zch: Ascorbate Peroxidase W41A-H42M Mutant

Enzymatic activity of Ascorbate Peroxidase W41A-H42M Mutant

All present enzymatic activity of Ascorbate Peroxidase W41A-H42M Mutant:
1.11.1.11;

Protein crystallography data

The structure of Ascorbate Peroxidase W41A-H42M Mutant, PDB code: 3zch was solved by A.Gumiero, 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) 46.080 / 2.00
Space group P 42 21 2
Cell size a, b, c (Å), α, β, γ (°) 82.629, 82.629, 74.950, 90.00, 90.00, 90.00
R / Rfree (%) 15.29 / 19.85

Other elements in 3zch:

The structure of Ascorbate Peroxidase W41A-H42M Mutant also contains other interesting chemical elements:

Potassium (K) 1 atom

Iron Binding Sites:

The binding sites of Iron atom in the Ascorbate Peroxidase W41A-H42M Mutant (pdb code 3zch). 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 Ascorbate Peroxidase W41A-H42M Mutant, PDB code: 3zch:

Iron binding site 1 out of 1 in 3zch

Go back to Iron Binding Sites List in 3zch
Iron binding site 1 out of 1 in the Ascorbate Peroxidase W41A-H42M Mutant


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Ascorbate Peroxidase W41A-H42M Mutant within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe251

b:8.7
occ:1.00
FE A:HEM251 0.0 8.7 1.0
NB A:HEM251 2.0 5.6 1.0
NC A:HEM251 2.0 5.8 1.0
NA A:HEM251 2.1 7.8 1.0
ND A:HEM251 2.1 6.7 1.0
NE2 A:HIS163 2.3 9.3 1.0
C4B A:HEM251 3.0 14.4 1.0
C1B A:HEM251 3.1 9.8 1.0
C1C A:HEM251 3.1 9.5 1.0
C4C A:HEM251 3.1 10.8 1.0
C1D A:HEM251 3.1 9.2 1.0
C4A A:HEM251 3.1 12.6 1.0
C4D A:HEM251 3.1 6.7 1.0
C1A A:HEM251 3.1 11.1 1.0
CD2 A:HIS163 3.1 8.7 1.0
C7 A:EPE1251 3.2 16.6 1.0
CE1 A:HIS163 3.4 8.5 1.0
CHC A:HEM251 3.4 8.9 1.0
CHD A:HEM251 3.4 7.5 1.0
CHB A:HEM251 3.5 9.4 1.0
CHA A:HEM251 3.5 8.8 1.0
O8 A:EPE1251 3.8 43.2 1.0
C8 A:EPE1251 3.8 6.9 1.0
N4 A:EPE1251 4.1 20.2 1.0
C3B A:HEM251 4.2 11.2 1.0
C2B A:HEM251 4.3 12.1 1.0
C2C A:HEM251 4.3 6.7 1.0
C3C A:HEM251 4.3 7.5 1.0
C2D A:HEM251 4.3 6.9 1.0
NE A:ARG38 4.3 12.6 1.0
C3D A:HEM251 4.3 6.3 1.0
C2A A:HEM251 4.3 8.2 1.0
C3A A:HEM251 4.3 10.0 1.0
CG A:HIS163 4.3 7.4 1.0
ND1 A:HIS163 4.4 8.7 1.0
C5 A:EPE1251 4.6 15.6 1.0
CG A:ARG38 4.8 10.9 1.0
CD A:ARG38 4.9 12.1 1.0

Reference:

A.Guimero, S.K.Badyal, T.Leeks, P.C.E.Moody, E.L.Raven. Probing the Conformational Mobility of the Active Site of Ascorbate Peroxidase Dalton Trans V. 42 3170 2013.
ISSN: ISSN 1477-9226
PubMed: 23202589
DOI: 10.1039/C2DT32455E
Page generated: Sun Aug 4 23:00:00 2024

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