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Iron in PDB 1zbz: High-Resolution Crystal Structure of Compound I Intermediate of Cytochrome C Peroxidase (Ccp)

Enzymatic activity of High-Resolution Crystal Structure of Compound I Intermediate of Cytochrome C Peroxidase (Ccp)

All present enzymatic activity of High-Resolution Crystal Structure of Compound I Intermediate of Cytochrome C Peroxidase (Ccp):
1.11.1.5;

Protein crystallography data

The structure of High-Resolution Crystal Structure of Compound I Intermediate of Cytochrome C Peroxidase (Ccp), PDB code: 1zbz was solved by C.A.Bonagura, B.Bhaskar, H.Shimizu, H.Li, M.Sundaramoorthy, D.E.Mcree, D.B.Goodin, T.L.Poulos, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 10.00 / 1.29
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 106.810, 74.810, 50.919, 90.00, 90.00, 90.00
R / Rfree (%) 11.6 / 15.5

Iron Binding Sites:

The binding sites of Iron atom in the High-Resolution Crystal Structure of Compound I Intermediate of Cytochrome C Peroxidase (Ccp) (pdb code 1zbz). 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 High-Resolution Crystal Structure of Compound I Intermediate of Cytochrome C Peroxidase (Ccp), PDB code: 1zbz:

Iron binding site 1 out of 1 in 1zbz

Go back to Iron Binding Sites List in 1zbz
Iron binding site 1 out of 1 in the High-Resolution Crystal Structure of Compound I Intermediate of Cytochrome C Peroxidase (Ccp)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of High-Resolution Crystal Structure of Compound I Intermediate of Cytochrome C Peroxidase (Ccp) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe296

b:11.0
occ:1.00
 FE A:HEM296 0.0 11.0 1.0
O A:HOH1040 1.9 15.5 1.0
NC A:HEM296 2.0 9.7 1.0
ND A:HEM296 2.0 10.9 1.0
NB A:HEM296 2.0 10.4 1.0
NA A:HEM296 2.0 10.7 1.0
NE2 A:HIS175 2.1 10.1 1.0
C4C A:HEM296 3.0 9.9 1.0
C1C A:HEM296 3.0 9.3 1.0
C4D A:HEM296 3.0 10.6 1.0
C1D A:HEM296 3.0 9.7 1.0
C4B A:HEM296 3.1 9.7 1.0
C4A A:HEM296 3.1 10.6 1.0
CE1 A:HIS175 3.1 11.7 1.0
C1A A:HEM296 3.1 11.0 1.0
C1B A:HEM296 3.1 11.1 1.0
CD2 A:HIS175 3.1 11.3 1.0
CHC A:HEM296 3.4 9.7 1.0
CHB A:HEM296 3.4 10.7 1.0
CHD A:HEM296 3.4 9.6 1.0
CHA A:HEM296 3.4 11.2 1.0
NE1 A:TRP51 3.9 11.6 1.0
NE A:ARG48 4.0 13.0 1.0
O A:HOH636 4.1 15.7 1.0
ND1 A:HIS175 4.2 10.7 1.0
CG A:HIS175 4.2 9.7 1.0
C3C A:HEM296 4.3 10.0 1.0
C2D A:HEM296 4.3 10.3 1.0
C3D A:HEM296 4.3 9.6 1.0
C2C A:HEM296 4.3 9.4 1.0
C2A A:HEM296 4.3 11.0 1.0
C3A A:HEM296 4.3 11.2 1.0
C2B A:HEM296 4.3 10.7 1.0
C3B A:HEM296 4.3 9.9 1.0
NH2 A:ARG48 4.5 14.2 1.0
CD1 A:TRP51 4.6 12.1 1.0
CZ A:ARG48 4.8 11.9 1.0
CD A:ARG48 4.9 13.6 1.0
CG A:ARG48 4.9 13.1 1.0
CE2 A:TRP51 5.0 10.5 1.0

Reference:

C.A.Bonagura, B.Bhaskar, H.Shimizu, H.Li, M.Sundaramoorthy, D.E.Mcree, D.B.Goodin, T.L.Poulos. High-Resolution Crystal Structures and Spectroscopy of Native and Compound I Cytochrome C Peroxidase Biochemistry V. 42 5600 2003.
ISSN: ISSN 0006-2960
PubMed: 12741816
DOI: 10.1021/BI034058C
Page generated: Sat Aug 3 18:17:08 2024

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