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Iron in PDB 1mk8: Crystal Structure of A Mutant Cytochrome C Peroxidase Showing A Novel Trp-Tyr Covalent Cross-Link

Enzymatic activity of Crystal Structure of A Mutant Cytochrome C Peroxidase Showing A Novel Trp-Tyr Covalent Cross-Link

All present enzymatic activity of Crystal Structure of A Mutant Cytochrome C Peroxidase Showing A Novel Trp-Tyr Covalent Cross-Link:
1.11.1.5;

Protein crystallography data

The structure of Crystal Structure of A Mutant Cytochrome C Peroxidase Showing A Novel Trp-Tyr Covalent Cross-Link, PDB code: 1mk8 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 / 1.65
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 106.773, 75.527, 51.033, 90.00, 90.00, 90.00
R / Rfree (%) 18 / 19.8

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of A Mutant Cytochrome C Peroxidase Showing A Novel Trp-Tyr Covalent Cross-Link (pdb code 1mk8). 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 Cytochrome C Peroxidase Showing A Novel Trp-Tyr Covalent Cross-Link, PDB code: 1mk8:

Iron binding site 1 out of 1 in 1mk8

Go back to Iron Binding Sites List in 1mk8
Iron binding site 1 out of 1 in the Crystal Structure of A Mutant Cytochrome C Peroxidase Showing A Novel Trp-Tyr Covalent Cross-Link


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 Cytochrome C Peroxidase Showing A Novel Trp-Tyr Covalent Cross-Link within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe296

b:12.3
occ:1.00
 FE A:HEM296 0.0 12.3 1.0
O A:HOH899 1.9 23.8 1.0
ND A:HEM296 2.0 11.9 1.0
NA A:HEM296 2.0 12.3 1.0
NB A:HEM296 2.0 11.9 1.0
NC A:HEM296 2.0 11.3 1.0
NE2 A:HIS175 2.0 10.6 1.0
CD2 A:HIS175 3.0 11.3 1.0
C4D A:HEM296 3.0 12.1 1.0
C1A A:HEM296 3.0 12.4 1.0
CE1 A:HIS175 3.0 11.0 1.0
C1D A:HEM296 3.1 11.6 1.0
C4B A:HEM296 3.1 11.8 1.0
C1C A:HEM296 3.1 11.2 1.0
C4A A:HEM296 3.1 12.4 1.0
C1B A:HEM296 3.1 12.1 1.0
C4C A:HEM296 3.1 11.5 1.0
CHA A:HEM296 3.4 12.2 1.0
CHC A:HEM296 3.4 10.9 1.0
CHD A:HEM296 3.5 11.6 1.0
CHB A:HEM296 3.5 12.1 1.0
ND1 A:HIS175 4.2 10.9 1.0
OH A:TYR52 4.2 17.7 1.0
CG A:HIS175 4.2 10.9 1.0
NE1 A:TRP51 4.2 13.1 1.0
C3D A:HEM296 4.2 11.8 1.0
C2D A:HEM296 4.3 11.6 1.0
C2A A:HEM296 4.3 12.4 1.0
C3A A:HEM296 4.3 12.4 1.0
C3B A:HEM296 4.3 11.9 1.0
C2B A:HEM296 4.3 12.0 1.0
C2C A:HEM296 4.3 11.1 1.0
C3C A:HEM296 4.3 11.2 1.0
O A:HOH461 4.5 27.6 1.0
CD1 A:TRP51 4.7 13.1 1.0
CE1 A:TYR52 4.8 15.2 1.0
CZ A:TYR52 4.8 16.9 1.0
CH2 A:TRP191 5.0 12.0 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 10:43:20 2024

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