Atomistry » Iron » PDB 4ccx-4cun » 4ccx
Atomistry »
  Iron »
    PDB 4ccx-4cun »
      4ccx »

Iron in PDB 4ccx: Altering Substrate Specificity at the Heme Edge of Cytochrome C Peroxidase

Enzymatic activity of Altering Substrate Specificity at the Heme Edge of Cytochrome C Peroxidase

All present enzymatic activity of Altering Substrate Specificity at the Heme Edge of Cytochrome C Peroxidase:
1.11.1.5;

Protein crystallography data

The structure of Altering Substrate Specificity at the Heme Edge of Cytochrome C Peroxidase, PDB code: 4ccx was solved by S.K.Wilcox, G.M.Jensen, M.M.Fitzgerald, D.E.Mcree, D.B.Goodin, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 5.00 / 1.90
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 105.200, 74.300, 45.400, 90.00, 90.00, 90.00
R / Rfree (%) 20 / n/a

Iron Binding Sites:

The binding sites of Iron atom in the Altering Substrate Specificity at the Heme Edge of Cytochrome C Peroxidase (pdb code 4ccx). 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 Altering Substrate Specificity at the Heme Edge of Cytochrome C Peroxidase, PDB code: 4ccx:

Iron binding site 1 out of 1 in 4ccx

Go back to Iron Binding Sites List in 4ccx
Iron binding site 1 out of 1 in the Altering Substrate Specificity at the Heme Edge of Cytochrome C Peroxidase


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Altering Substrate Specificity at the Heme Edge of Cytochrome C Peroxidase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe295

b:16.8
occ:1.00
FE A:HEM295 0.0 16.8 1.0
NE2 A:HIS175 2.0 17.3 1.0
NC A:HEM295 2.0 13.5 1.0
NA A:HEM295 2.1 15.5 1.0
O A:HOH313 2.1 33.8 1.0
NB A:HEM295 2.1 15.2 1.0
ND A:HEM295 2.1 14.7 1.0
CE1 A:HIS175 2.9 14.6 1.0
C1C A:HEM295 3.0 18.0 1.0
C4B A:HEM295 3.0 14.9 1.0
C1A A:HEM295 3.0 17.0 1.0
C4D A:HEM295 3.0 13.4 1.0
CD2 A:HIS175 3.0 16.7 1.0
C4C A:HEM295 3.1 16.4 1.0
C4A A:HEM295 3.1 15.7 1.0
C1D A:HEM295 3.1 13.9 1.0
C1B A:HEM295 3.1 14.3 1.0
CHC A:HEM295 3.3 10.9 1.0
CHA A:HEM295 3.3 11.6 1.0
CHD A:HEM295 3.4 15.7 1.0
CHB A:HEM295 3.4 13.1 1.0
ND1 A:HIS175 4.0 13.4 1.0
CG A:HIS175 4.2 15.0 1.0
C3D A:HEM295 4.2 15.1 1.0
C2A A:HEM295 4.2 17.4 1.0
C3C A:HEM295 4.2 17.4 1.0
C2C A:HEM295 4.2 15.9 1.0
C2D A:HEM295 4.2 13.4 1.0
C3A A:HEM295 4.3 14.1 1.0
C3B A:HEM295 4.3 15.0 1.0
NE1 A:TRP51 4.3 21.1 1.0
C2B A:HEM295 4.3 15.6 1.0
O A:HOH344 4.5 34.3 1.0
CD1 A:TRP51 4.6 20.2 1.0
O A:HOH300 4.7 47.0 1.0
CH2 A:TRP191 5.0 19.5 1.0

Reference:

S.K.Wilcox, G.M.Jensen, M.M.Fitzgerald, D.E.Mcree, D.B.Goodin. Altering Substrate Specificity at the Heme Edge of Cytochrome C Peroxidase. Biochemistry V. 35 4858 1996.
ISSN: ISSN 0006-2960
PubMed: 8664277
DOI: 10.1021/BI952929F
Page generated: Sun Dec 13 15:30:02 2020

Last articles

Zn in 8WB0
Zn in 8WAX
Zn in 8WAU
Zn in 8WAZ
Zn in 8WAY
Zn in 8WAV
Zn in 8WAW
Zn in 8WAT
Zn in 8W7M
Zn in 8WD3
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy