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Iron in PDB 1kxn: Crystal Structure of Cytochrome C Peroxidase with A Proposed Electron Transfer Pathway Excised to Form A Ligand Binding Channel.

Enzymatic activity of Crystal Structure of Cytochrome C Peroxidase with A Proposed Electron Transfer Pathway Excised to Form A Ligand Binding Channel.

All present enzymatic activity of Crystal Structure of Cytochrome C Peroxidase with A Proposed Electron Transfer Pathway Excised to Form A Ligand Binding Channel.:
1.11.1.5;

Protein crystallography data

The structure of Crystal Structure of Cytochrome C Peroxidase with A Proposed Electron Transfer Pathway Excised to Form A Ligand Binding Channel., PDB code: 1kxn was solved by R.J.Rosenfeld, A.M.A.Hayes, R.A.Musah, D.B.Goodin, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 10.00 / 1.80
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 106.800, 75.800, 51.100, 90.00, 90.00, 90.00
R / Rfree (%) n/a / 19.4

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of Cytochrome C Peroxidase with A Proposed Electron Transfer Pathway Excised to Form A Ligand Binding Channel. (pdb code 1kxn). 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 Cytochrome C Peroxidase with A Proposed Electron Transfer Pathway Excised to Form A Ligand Binding Channel., PDB code: 1kxn:

Iron binding site 1 out of 1 in 1kxn

Go back to Iron Binding Sites List in 1kxn
Iron binding site 1 out of 1 in the Crystal Structure of Cytochrome C Peroxidase with A Proposed Electron Transfer Pathway Excised to Form A Ligand Binding Channel.


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 Cytochrome C Peroxidase with A Proposed Electron Transfer Pathway Excised to Form A Ligand Binding Channel. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe1

b:15.0
occ:1.00
 FE A:HEM1 0.0 15.0 1.0
O A:HOH313 1.9 15.5 1.0
NE2 A:HIS175 2.0 16.3 1.0
NA A:HEM1 2.0 13.4 1.0
NC A:HEM1 2.0 12.1 1.0
ND A:HEM1 2.1 10.6 1.0
NB A:HEM1 2.1 12.0 1.0
CE1 A:HIS175 3.0 13.9 1.0
C1A A:HEM1 3.0 14.1 1.0
C1C A:HEM1 3.0 12.8 1.0
C4B A:HEM1 3.0 14.4 1.0
C4A A:HEM1 3.0 14.3 1.0
C1D A:HEM1 3.1 14.2 1.0
CD2 A:HIS175 3.1 12.6 1.0
C4C A:HEM1 3.1 16.2 1.0
C1B A:HEM1 3.1 12.6 1.0
C4D A:HEM1 3.1 15.3 1.0
CHC A:HEM1 3.3 11.3 1.0
CHD A:HEM1 3.4 13.4 1.0
CHA A:HEM1 3.4 12.1 1.0
CHB A:HEM1 3.4 13.2 1.0
NE A:ARG48 4.1 23.0 1.0
ND1 A:HIS175 4.1 14.9 1.0
NE1 A:TRP51 4.1 17.4 1.0
CG A:HIS175 4.2 18.1 1.0
C2A A:HEM1 4.2 16.3 1.0
C3A A:HEM1 4.2 15.8 1.0
C2D A:HEM1 4.2 19.6 1.0
C3C A:HEM1 4.3 16.2 1.0
C2C A:HEM1 4.3 17.9 1.0
C3B A:HEM1 4.3 11.0 1.0
C2B A:HEM1 4.3 13.7 1.0
C3D A:HEM1 4.3 15.7 1.0
O A:HOH344 4.3 19.7 1.0
NH1 A:ARG48 4.6 20.3 1.0
CD1 A:TRP51 4.6 15.3 1.0
O A:HOH403 4.6 21.5 1.0
CZ A:ARG48 4.9 23.6 1.0
CD A:ARG48 4.9 21.2 1.0
CG A:ARG48 4.9 14.7 1.0

Reference:

R.J.Rosenfeld, A.M.Hays, R.A.Musah, D.B.Goodin. Excision of A Proposed Electron Transfer Pathway in Cytochrome C Peroxidase and Its Replacement By A Ligand-Binding Channel. Protein Sci. V. 11 1251 2002.
ISSN: ISSN 0961-8368
PubMed: 11967381
DOI: 10.1110/PS.4870102
Page generated: Sat Aug 3 09:30:43 2024

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