Iron in PDB 3zcy: Ascorbate Peroxidase W41A-H42Y Mutant

All present enzymatic activity of Ascorbate Peroxidase W41A-H42Y Mutant:
1.11.1.11;

The structure of Ascorbate Peroxidase W41A-H42Y Mutant, PDB code: 3zcy 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)	36.797 / 2.00
Space group	P 42 21 2
Cell size a, b, c (Å), α, β, γ (°)	82.280, 82.280, 75.170, 90.00, 90.00, 90.00
R / Rfree (%)	15.97 / 21.32

The structure of Ascorbate Peroxidase W41A-H42Y Mutant also contains other interesting chemical elements:

Potassium

(K)

1 atom

The binding sites of Iron atom in the Ascorbate Peroxidase W41A-H42Y Mutant (pdb code 3zcy). 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-H42Y Mutant, PDB code: 3zcy:

Iron binding site 1 out of 1 in the Ascorbate Peroxidase W41A-H42Y 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-H42Y Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe251 b:9.6 occ:1.00 FE A:HEM251 0.0 9.6 1.0 NC A:HEM251 2.0 7.5 1.0 NB A:HEM251 2.1 10.4 1.0 NA A:HEM251 2.1 9.4 1.0 ND A:HEM251 2.1 5.4 1.0 NE2 A:HIS163 2.3 11.5 1.0 O8 A:EPE1251 2.3 16.7 1.0 C1C A:HEM251 3.0 10.7 1.0 C4C A:HEM251 3.0 10.5 1.0 C4B A:HEM251 3.0 15.4 1.0 C1D A:HEM251 3.1 7.5 1.0 C1A A:HEM251 3.1 12.2 1.0 C1B A:HEM251 3.1 11.1 1.0 C4D A:HEM251 3.1 8.0 1.0 C4A A:HEM251 3.1 12.9 1.0 CD2 A:HIS163 3.1 7.3 1.0 CE1 A:HIS163 3.4 9.4 1.0 CHC A:HEM251 3.4 10.7 1.0 C8 A:EPE1251 3.4 20.4 1.0 CHD A:HEM251 3.4 7.3 1.0 CHA A:HEM251 3.5 8.6 1.0 CHB A:HEM251 3.5 12.0 1.0 C3C A:HEM251 4.3 8.8 1.0 C2C A:HEM251 4.3 8.8 1.0 C3B A:HEM251 4.3 14.8 1.0 C2D A:HEM251 4.3 6.4 1.0 C7 A:EPE1251 4.3 34.4 1.0 C2B A:HEM251 4.3 14.4 1.0 C2A A:HEM251 4.3 9.8 1.0 C3A A:HEM251 4.3 12.9 1.0 C3D A:HEM251 4.3 8.6 1.0 CG A:HIS163 4.3 7.5 1.0 NE A:ARG38 4.4 21.3 1.0 N4 A:EPE1251 4.4 29.4 1.0 ND1 A:HIS163 4.4 9.2 1.0 CG A:ARG38 4.9 10.9 1.0 CD A:ARG38 5.0 16.9 1.0

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