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Iron in PDB 1dse: Cytochrome C Peroxidase H175G Mutant, Imidazole Complex, with Phosphate Bound, pH 6, 100K

Enzymatic activity of Cytochrome C Peroxidase H175G Mutant, Imidazole Complex, with Phosphate Bound, pH 6, 100K

All present enzymatic activity of Cytochrome C Peroxidase H175G Mutant, Imidazole Complex, with Phosphate Bound, pH 6, 100K:
1.11.1.5;

Protein crystallography data

The structure of Cytochrome C Peroxidase H175G Mutant, Imidazole Complex, with Phosphate Bound, pH 6, 100K, PDB code: 1dse was solved by J.Hirst, S.K.Wilcox, P.A.Williams, D.E.Mcree, D.B.Goodin, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.00 / 2.00
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 107.258, 73.768, 51.041, 90.00, 90.00, 90.00
R / Rfree (%) 19.6 / n/a

Iron Binding Sites:

The binding sites of Iron atom in the Cytochrome C Peroxidase H175G Mutant, Imidazole Complex, with Phosphate Bound, pH 6, 100K (pdb code 1dse). 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 Cytochrome C Peroxidase H175G Mutant, Imidazole Complex, with Phosphate Bound, pH 6, 100K, PDB code: 1dse:

Iron binding site 1 out of 1 in 1dse

Go back to Iron Binding Sites List in 1dse
Iron binding site 1 out of 1 in the Cytochrome C Peroxidase H175G Mutant, Imidazole Complex, with Phosphate Bound, pH 6, 100K


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Cytochrome C Peroxidase H175G Mutant, Imidazole Complex, with Phosphate Bound, pH 6, 100K within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe1001

b:17.5
occ:1.00
 FE A:HEM1001 0.0 17.5 1.0
O4 A:PO41501 2.0 15.3 1.0
NC A:HEM1001 2.0 13.8 1.0
NA A:HEM1001 2.0 18.0 1.0
NB A:HEM1001 2.1 13.0 1.0
ND A:HEM1001 2.1 16.4 1.0
C1C A:HEM1001 3.0 18.8 1.0
C4A A:HEM1001 3.0 18.6 1.0
C1A A:HEM1001 3.0 16.8 1.0
C4B A:HEM1001 3.1 10.0 1.0
C1B A:HEM1001 3.1 12.7 1.0
C4C A:HEM1001 3.1 10.6 1.0
C1D A:HEM1001 3.1 16.3 1.0
C4D A:HEM1001 3.1 12.6 1.0
P A:PO41501 3.3 47.5 1.0
N1 A:IMD1500 3.3 20.3 1.0
CHC A:HEM1001 3.4 11.4 1.0
CHD A:HEM1001 3.4 13.3 1.0
CHB A:HEM1001 3.4 12.1 1.0
CHA A:HEM1001 3.4 11.3 1.0
O1 A:PO41501 3.6 52.6 1.0
C2 A:IMD1500 3.7 25.6 1.0
NE1 A:TRP51 3.8 17.6 1.0
O3 A:PO41501 3.9 41.1 1.0
C3A A:HEM1001 4.2 16.7 1.0
C2A A:HEM1001 4.2 18.0 1.0
C3C A:HEM1001 4.2 15.4 1.0
C2C A:HEM1001 4.3 13.2 1.0
C3B A:HEM1001 4.3 14.7 1.0
C2B A:HEM1001 4.3 16.9 1.0
C2D A:HEM1001 4.3 13.2 1.0
C3D A:HEM1001 4.3 9.3 1.0
CD1 A:TRP51 4.4 18.8 1.0
C5 A:IMD1500 4.4 19.9 1.0
O2 A:PO41501 4.5 32.9 1.0
CE2 A:TRP51 4.7 13.5 1.0
CG A:ARG48 4.8 17.2 1.0

Reference:

J.Hirst, S.K.Wilcox, P.A.Williams, J.Blankenship, D.E.Mcree, D.B.Goodin. Replacement of the Axial Histidine Ligand with Imidazole in Cytochrome C Peroxidase. 1. Effects on Structure. Biochemistry V. 40 1265 2001.
ISSN: ISSN 0006-2960
PubMed: 11170452
DOI: 10.1021/BI002089R
Page generated: Wed Jul 16 13:24:52 2025

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