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Iron in PDB 1mkr: Crystal Structure of A Mutant Variant of Cytochrome C Peroxidase (Plate Like Crystals)

Enzymatic activity of Crystal Structure of A Mutant Variant of Cytochrome C Peroxidase (Plate Like Crystals)

All present enzymatic activity of Crystal Structure of A Mutant Variant of Cytochrome C Peroxidase (Plate Like Crystals):
1.11.1.5;

Protein crystallography data

The structure of Crystal Structure of A Mutant Variant of Cytochrome C Peroxidase (Plate Like Crystals), PDB code: 1mkr 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 / 1.58
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 50.480, 50.957, 118.884, 90.00, 90.00, 90.00
R / Rfree (%) 19.4 / 21.9

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of A Mutant Variant of Cytochrome C Peroxidase (Plate Like Crystals) (pdb code 1mkr). 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 A Mutant Variant of Cytochrome C Peroxidase (Plate Like Crystals), PDB code: 1mkr:

Iron binding site 1 out of 1 in 1mkr

Go back to Iron Binding Sites List in 1mkr
Iron binding site 1 out of 1 in the Crystal Structure of A Mutant Variant of Cytochrome C Peroxidase (Plate Like Crystals)


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 A Mutant Variant of Cytochrome C Peroxidase (Plate Like Crystals) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe296

b:13.9
occ:1.00
FE A:HEM296 0.0 13.9 1.0
NC A:HEM296 2.0 12.8 1.0
NB A:HEM296 2.0 13.7 1.0
ND A:HEM296 2.0 13.3 1.0
NA A:HEM296 2.0 13.6 1.0
NE2 A:HIS175 2.1 13.1 1.0
C1C A:HEM296 3.0 13.1 1.0
C4B A:HEM296 3.1 13.9 1.0
C1D A:HEM296 3.1 12.9 1.0
C4C A:HEM296 3.1 12.9 1.0
C4D A:HEM296 3.1 13.2 1.0
C1A A:HEM296 3.1 13.8 1.0
C1B A:HEM296 3.1 13.9 1.0
C4A A:HEM296 3.1 14.1 1.0
CD2 A:HIS175 3.1 13.0 1.0
CE1 A:HIS175 3.1 13.3 1.0
CHC A:HEM296 3.4 13.3 1.0
CHD A:HEM296 3.4 12.8 1.0
CHA A:HEM296 3.4 13.4 1.0
CHB A:HEM296 3.5 13.8 1.0
O A:HOH378 4.0 25.9 1.0
O A:HOH512 4.1 29.0 1.0
ND1 A:HIS175 4.2 12.8 1.0
CG A:HIS175 4.2 13.3 1.0
C2D A:HEM296 4.3 12.8 1.0
C3D A:HEM296 4.3 12.8 1.0
C2C A:HEM296 4.3 12.8 1.0
C3B A:HEM296 4.3 13.9 1.0
C2B A:HEM296 4.3 13.7 1.0
C3C A:HEM296 4.3 12.9 1.0
C2A A:HEM296 4.3 14.0 1.0
C3A A:HEM296 4.3 14.2 1.0
NE1 A:TRP51 4.4 17.0 1.0
CD1 A:TRP51 4.7 16.6 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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