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Iron in PDB 1cyf: Identifying the Physiological Electron Transfer Site of Cytochrome C Peroxidase By Structure-Based Engineering

Enzymatic activity of Identifying the Physiological Electron Transfer Site of Cytochrome C Peroxidase By Structure-Based Engineering

All present enzymatic activity of Identifying the Physiological Electron Transfer Site of Cytochrome C Peroxidase By Structure-Based Engineering:
1.11.1.5;

Protein crystallography data

The structure of Identifying the Physiological Electron Transfer Site of Cytochrome C Peroxidase By Structure-Based Engineering, PDB code: 1cyf was solved by M.A.Miller, G.W.Han, J.Kraut, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 2.35
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 101.330, 73.880, 45.000, 90.00, 90.00, 90.00
R / Rfree (%) n/a / n/a

Iron Binding Sites:

The binding sites of Iron atom in the Identifying the Physiological Electron Transfer Site of Cytochrome C Peroxidase By Structure-Based Engineering (pdb code 1cyf). 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 Identifying the Physiological Electron Transfer Site of Cytochrome C Peroxidase By Structure-Based Engineering, PDB code: 1cyf:

Iron binding site 1 out of 1 in 1cyf

Go back to Iron Binding Sites List in 1cyf
Iron binding site 1 out of 1 in the Identifying the Physiological Electron Transfer Site of Cytochrome C Peroxidase By Structure-Based Engineering


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Identifying the Physiological Electron Transfer Site of Cytochrome C Peroxidase By Structure-Based Engineering within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe296

b:16.5
occ:1.00
 FE A:HEM296 0.0 16.5 1.0
O A:HOH295 1.8 14.7 1.0
NA A:HEM296 1.9 16.3 1.0
NC A:HEM296 2.0 13.7 1.0
ND A:HEM296 2.0 11.9 1.0
NB A:HEM296 2.0 20.5 1.0
NE2 A:HIS175 2.1 19.2 1.0
C1A A:HEM296 2.9 17.3 1.0
C1D A:HEM296 3.0 10.1 1.0
C4A A:HEM296 3.0 15.4 1.0
C4C A:HEM296 3.0 14.0 1.0
C4D A:HEM296 3.0 12.0 1.0
C4B A:HEM296 3.0 20.7 1.0
C1C A:HEM296 3.0 15.8 1.0
C1B A:HEM296 3.1 22.5 1.0
CE1 A:HIS175 3.1 16.4 1.0
CD2 A:HIS175 3.1 19.7 1.0
CHA A:HEM296 3.3 15.7 1.0
CHD A:HEM296 3.4 13.0 1.0
CHC A:HEM296 3.4 15.6 1.0
CHB A:HEM296 3.5 18.2 1.0
O A:HOH648 3.7 50.1 1.0
NE1 A:TRP51 4.1 19.4 1.0
C2A A:HEM296 4.1 17.4 1.0
C2D A:HEM296 4.2 6.9 1.0
C3A A:HEM296 4.2 14.3 1.0
C3C A:HEM296 4.2 17.4 1.0
C2C A:HEM296 4.2 14.2 1.0
C3D A:HEM296 4.2 10.7 1.0
ND1 A:HIS175 4.3 14.3 1.0
C3B A:HEM296 4.3 23.9 1.0
CG A:HIS175 4.3 14.9 1.0
C2B A:HEM296 4.3 25.3 1.0
CD1 A:TRP51 4.7 18.3 1.0
CH2 A:TRP191 5.0 14.3 1.0

Reference:

M.A.Miller, L.Geren, G.W.Han, A.Saunders, J.Beasley, G.J.Pielak, B.Durham, F.Millett, J.Kraut. Identifying the Physiological Electron Transfer Site of Cytochrome C Peroxidase By Structure-Based Engineering. Biochemistry V. 35 667 1996.
ISSN: ISSN 0006-2960
PubMed: 8547245
DOI: 10.1021/BI952557A
Page generated: Sat Aug 3 03:33:18 2024

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