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Iron in PDB 1mkq: Crystal Structure of the Mutant Variant of Cytochrome C Peroxidase in the 'Open' Uncross-Linked Form

Enzymatic activity of Crystal Structure of the Mutant Variant of Cytochrome C Peroxidase in the 'Open' Uncross-Linked Form

All present enzymatic activity of Crystal Structure of the Mutant Variant of Cytochrome C Peroxidase in the 'Open' Uncross-Linked Form:
1.11.1.5;

Protein crystallography data

The structure of Crystal Structure of the Mutant Variant of Cytochrome C Peroxidase in the 'Open' Uncross-Linked Form, PDB code: 1mkq was solved by B.Bhaskar, C.E.Immoos, H.Shimizu, P.J.Farmer, T.L.Poulos, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.00 / 1.64
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 106.598, 74.943, 50.987, 90.00, 90.00, 90.00
R / Rfree (%) 18.4 / 20.8

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of the Mutant Variant of Cytochrome C Peroxidase in the 'Open' Uncross-Linked Form (pdb code 1mkq). 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 the Mutant Variant of Cytochrome C Peroxidase in the 'Open' Uncross-Linked Form, PDB code: 1mkq:

Iron binding site 1 out of 1 in 1mkq

Go back to Iron Binding Sites List in 1mkq
Iron binding site 1 out of 1 in the Crystal Structure of the Mutant Variant of Cytochrome C Peroxidase in the 'Open' Uncross-Linked Form


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 the Mutant Variant of Cytochrome C Peroxidase in the 'Open' Uncross-Linked Form within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe296

b:13.5
occ:1.00
 FE A:HEM296 0.0 13.5 1.0
ND A:HEM296 2.0 12.8 1.0
NC A:HEM296 2.0 12.4 1.0
NB A:HEM296 2.0 13.0 1.0
NA A:HEM296 2.0 13.0 1.0
NE2 A:HIS175 2.1 13.0 1.0
C1C A:HEM296 3.0 12.5 1.0
C4D A:HEM296 3.1 12.8 1.0
C4B A:HEM296 3.1 13.0 1.0
C1D A:HEM296 3.1 12.8 1.0
C1A A:HEM296 3.1 13.5 1.0
C4C A:HEM296 3.1 12.6 1.0
C4A A:HEM296 3.1 13.4 1.0
C1B A:HEM296 3.1 13.1 1.0
CD2 A:HIS175 3.1 12.9 1.0
CE1 A:HIS175 3.1 13.3 1.0
CHC A:HEM296 3.4 12.4 1.0
CHA A:HEM296 3.4 13.1 1.0
CHD A:HEM296 3.4 12.6 1.0
CHB A:HEM296 3.5 13.3 1.0
O A:HOH797 3.9 25.2 1.0
O A:HOH857 4.1 27.7 1.0
ND1 A:HIS175 4.2 12.6 1.0
CG A:HIS175 4.2 13.1 1.0
C3D A:HEM296 4.3 12.8 1.0
C2D A:HEM296 4.3 12.6 1.0
C3B A:HEM296 4.3 13.0 1.0
C2C A:HEM296 4.3 12.3 1.0
C2A A:HEM296 4.3 13.7 1.0
C2B A:HEM296 4.3 13.2 1.0
C3C A:HEM296 4.3 12.4 1.0
C3A A:HEM296 4.3 13.3 1.0
NE1 A:TRP51 4.4 16.1 1.0
CD1 A:TRP51 4.7 16.3 1.0
CH2 A:TRP191 5.0 12.5 1.0

Reference:

B.Bhaskar, C.E.Immoos, H.Shimizu, F.Sulc, P.J.Farmer, T.L.Poulos. A Novel Heme and Peroxide-Dependent Tryptophan-Tyrosine Cross-Link in A Mutant of Cytochrome C Peroxidase J.Mol.Biol. V. 328 157 2003.
ISSN: ISSN 0022-2836
PubMed: 12684005
DOI: 10.1016/S0022-2836(03)00179-7
Page generated: Sat Aug 3 11:00:38 2024

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