Atomistry » Iron » PDB 3c25-3crb » 3ccx
Atomistry »
  Iron »
    PDB 3c25-3crb »
      3ccx »

Iron in PDB 3ccx: 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: 3ccx 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 / 2.30
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 (%) 17 / 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 3ccx). 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: 3ccx:

Iron binding site 1 out of 1 in 3ccx

Go back to Iron Binding Sites List in 3ccx
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
NA A:HEM295 2.0 11.1 1.0
NC A:HEM295 2.1 16.9 1.0
NB A:HEM295 2.1 17.3 1.0
ND A:HEM295 2.1 19.3 1.0
CE1 A:HIS175 2.9 10.4 1.0
C4A A:HEM295 3.0 18.6 1.0
C1A A:HEM295 3.0 17.5 1.0
C4B A:HEM295 3.1 15.7 1.0
C1C A:HEM295 3.1 19.9 1.0
C4C A:HEM295 3.1 17.7 1.0
C1B A:HEM295 3.1 17.0 1.0
C4D A:HEM295 3.1 13.5 1.0
CD2 A:HIS175 3.1 19.6 1.0
C1D A:HEM295 3.1 15.6 1.0
O A:HOH313 3.3 44.7 1.0
CHC A:HEM295 3.4 15.8 1.0
CHB A:HEM295 3.4 16.3 1.0
CHA A:HEM295 3.4 13.2 1.0
CHD A:HEM295 3.4 15.8 1.0
ND1 A:HIS175 4.1 11.8 1.0
CG A:HIS175 4.2 12.2 1.0
C3A A:HEM295 4.2 9.7 1.0
C2A A:HEM295 4.2 15.8 1.0
C3D A:HEM295 4.3 19.0 1.0
C3B A:HEM295 4.3 19.9 1.0
C3C A:HEM295 4.3 17.2 1.0
C2D A:HEM295 4.3 14.9 1.0
C2C A:HEM295 4.3 16.5 1.0
C2B A:HEM295 4.3 13.8 1.0
NE1 A:TRP51 4.4 25.1 1.0
CD1 A:TRP51 4.6 22.5 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 Aug 4 08:19:58 2024

Last articles

Cl in 3RCO
Cl in 3RF7
Cl in 3RGF
Cl in 3RF4
Cl in 3REW
Cl in 3RE0
Cl in 3RE3
Cl in 3RDK
Cl in 3RD7
Cl in 3RDR
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy