Atomistry » Iron » PDB 2c2c-2ciy » 2cep
Atomistry »
  Iron »
    PDB 2c2c-2ciy »
      2cep »

Iron in PDB 2cep: Role of Met-230 in Intramolecular Electron Transfer Between the Oxyferryl Heme and Trp 191 in Cytochrome C Peroxidase Compound II

Enzymatic activity of Role of Met-230 in Intramolecular Electron Transfer Between the Oxyferryl Heme and Trp 191 in Cytochrome C Peroxidase Compound II

All present enzymatic activity of Role of Met-230 in Intramolecular Electron Transfer Between the Oxyferryl Heme and Trp 191 in Cytochrome C Peroxidase Compound II:
1.11.1.5;

Protein crystallography data

The structure of Role of Met-230 in Intramolecular Electron Transfer Between the Oxyferryl Heme and Trp 191 in Cytochrome C Peroxidase Compound II, PDB code: 2cep was solved by G.W.Han, M.A.Miller, J.Kraut, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 2.20
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 105.000, 74.200, 45.400, 90.00, 90.00, 90.00
R / Rfree (%) n/a / n/a

Iron Binding Sites:

The binding sites of Iron atom in the Role of Met-230 in Intramolecular Electron Transfer Between the Oxyferryl Heme and Trp 191 in Cytochrome C Peroxidase Compound II (pdb code 2cep). 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 Role of Met-230 in Intramolecular Electron Transfer Between the Oxyferryl Heme and Trp 191 in Cytochrome C Peroxidase Compound II, PDB code: 2cep:

Iron binding site 1 out of 1 in 2cep

Go back to Iron Binding Sites List in 2cep
Iron binding site 1 out of 1 in the Role of Met-230 in Intramolecular Electron Transfer Between the Oxyferryl Heme and Trp 191 in Cytochrome C Peroxidase Compound II


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Role of Met-230 in Intramolecular Electron Transfer Between the Oxyferryl Heme and Trp 191 in Cytochrome C Peroxidase Compound II within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe296

b:17.0
occ:1.00
 FE A:HEM296 0.0 17.0 1.0
NA A:HEM296 1.9 11.3 1.0
NC A:HEM296 2.0 13.6 1.0
NB A:HEM296 2.0 15.0 1.0
ND A:HEM296 2.1 13.6 1.0
NE2 A:HIS175 2.2 19.1 1.0
O A:HOH595 2.6 27.1 1.0
CE1 A:HIS175 3.0 16.8 1.0
C1A A:HEM296 3.0 16.6 1.0
C4B A:HEM296 3.0 13.0 1.0
C4D A:HEM296 3.0 8.6 1.0
C4C A:HEM296 3.0 16.8 1.0
C4A A:HEM296 3.0 16.2 1.0
C1C A:HEM296 3.0 17.1 1.0
C1D A:HEM296 3.1 10.4 1.0
C1B A:HEM296 3.1 13.4 1.0
CD2 A:HIS175 3.3 17.0 1.0
CHA A:HEM296 3.3 10.7 1.0
CHC A:HEM296 3.4 15.9 1.0
CHD A:HEM296 3.5 11.9 1.0
CHB A:HEM296 3.5 14.0 1.0
ND1 A:HIS175 4.1 17.5 1.0
C3D A:HEM296 4.2 12.2 1.0
C2A A:HEM296 4.2 18.8 1.0
C3A A:HEM296 4.2 15.9 1.0
C3C A:HEM296 4.2 14.8 1.0
C2D A:HEM296 4.3 9.0 1.0
C3B A:HEM296 4.3 17.3 1.0
C2C A:HEM296 4.3 13.8 1.0
C2B A:HEM296 4.3 17.2 1.0
NE1 A:TRP51 4.3 19.1 1.0
CG A:HIS175 4.4 15.9 1.0
O A:HOH596 4.5 48.6 1.0
CD1 A:TRP51 4.7 20.3 1.0
CH2 A:TRP191 4.9 22.6 1.0

Reference:

R.Q.Liu, M.A.Miller, G.W.Han, S.Hahm, L.Geren, S.Hibdon, J.Kraut, B.Durham, F.Millett. Role of Methionine 230 in Intramolecular Electron Transfer Between the Oxyferryl Heme and Tryptophan 191 in Cytochrome C Peroxidase Compound II. Biochemistry V. 33 8678 1994.
ISSN: ISSN 0006-2960
PubMed: 8038157
DOI: 10.1021/BI00195A008
Page generated: Sat Aug 3 20:14:41 2024

Last articles

Zn in 9J0N
Zn in 9J0O
Zn in 9J0P
Zn in 9FJX
Zn in 9EKB
Zn in 9C0F
Zn in 9CAH
Zn in 9CH0
Zn in 9CH3
Zn in 9CH1
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy