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Iron in PDB 1dj5: Crystal Structure of R48A Mutant of Cytochrome C Peroxidase with N- Hydroxyguanidine Bound

Enzymatic activity of Crystal Structure of R48A Mutant of Cytochrome C Peroxidase with N- Hydroxyguanidine Bound

All present enzymatic activity of Crystal Structure of R48A Mutant of Cytochrome C Peroxidase with N- Hydroxyguanidine Bound:
1.11.1.5;

Protein crystallography data

The structure of Crystal Structure of R48A Mutant of Cytochrome C Peroxidase with N- Hydroxyguanidine Bound, PDB code: 1dj5 was solved by J.Hirst, D.B.Goodin, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 10.00 / 1.93
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 105.480, 74.320, 44.310, 90.00, 90.00, 90.00
R / Rfree (%) n/a / n/a

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of R48A Mutant of Cytochrome C Peroxidase with N- Hydroxyguanidine Bound (pdb code 1dj5). 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 R48A Mutant of Cytochrome C Peroxidase with N- Hydroxyguanidine Bound, PDB code: 1dj5:

Iron binding site 1 out of 1 in 1dj5

Go back to Iron Binding Sites List in 1dj5
Iron binding site 1 out of 1 in the Crystal Structure of R48A Mutant of Cytochrome C Peroxidase with N- Hydroxyguanidine Bound


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 R48A Mutant of Cytochrome C Peroxidase with N- Hydroxyguanidine Bound within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe1

b:8.8
occ:1.00
 FE A:HEM1 0.0 8.8 1.0
O A:HGU2 1.9 20.4 1.0
NC A:HEM1 2.0 9.0 1.0
NA A:HEM1 2.1 5.9 1.0
ND A:HEM1 2.1 8.7 1.0
NE2 A:HIS175 2.1 6.8 1.0
NB A:HEM1 2.1 5.7 1.0
N A:HGU2 2.7 28.9 1.0
CE1 A:HIS175 3.0 8.9 1.0
C1A A:HEM1 3.0 4.4 1.0
C4B A:HEM1 3.0 12.0 1.0
C1C A:HEM1 3.0 10.6 1.0
C4D A:HEM1 3.1 5.7 1.0
C4C A:HEM1 3.1 10.5 1.0
C4A A:HEM1 3.1 9.1 1.0
C1D A:HEM1 3.1 12.3 1.0
C1B A:HEM1 3.1 3.7 1.0
CD2 A:HIS175 3.1 6.4 1.0
CHC A:HEM1 3.4 1.0 1.0
CHA A:HEM1 3.4 1.2 1.0
CHD A:HEM1 3.4 7.4 1.0
CHB A:HEM1 3.4 4.2 1.0
C A:HGU2 3.7 23.0 1.0
NH2 A:HGU2 3.9 15.6 1.0
NE1 A:TRP51 4.0 9.0 1.0
ND1 A:HIS175 4.2 13.3 1.0
C2A A:HEM1 4.2 12.0 1.0
CG A:HIS175 4.2 11.6 1.0
C3B A:HEM1 4.2 7.2 1.0
C3A A:HEM1 4.2 9.6 1.0
C3C A:HEM1 4.2 10.0 1.0
C2C A:HEM1 4.3 8.2 1.0
C3D A:HEM1 4.3 5.7 1.0
C2D A:HEM1 4.3 8.3 1.0
C2B A:HEM1 4.3 3.4 1.0
O A:HOH344 4.4 8.1 1.0
CD1 A:TRP51 4.6 8.8 1.0
NH1 A:HGU2 4.7 11.8 1.0

Reference:

J.Hirst, D.B.Goodin. Unusual Oxidative Chemistry of N(Omega)-Hydroxyarginine and N-Hydroxyguanidine Catalyzed at An Engineered Cavity in A Heme Peroxidase. J.Biol.Chem. V. 275 8582 2000.
ISSN: ISSN 0021-9258
PubMed: 10722697
DOI: 10.1074/JBC.275.12.8582
Page generated: Sat Aug 3 03:46:01 2024

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