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Iron in PDB 1jci: Stabilization of the Engineered Cation-Binding Loop in Cytochrome C Peroxidase (Ccp)

Enzymatic activity of Stabilization of the Engineered Cation-Binding Loop in Cytochrome C Peroxidase (Ccp)

All present enzymatic activity of Stabilization of the Engineered Cation-Binding Loop in Cytochrome C Peroxidase (Ccp):
1.11.1.5;

Protein crystallography data

The structure of Stabilization of the Engineered Cation-Binding Loop in Cytochrome C Peroxidase (Ccp), PDB code: 1jci was solved by B.Bhaskar, C.A.Bonagura, H.Li, T.L.Poulos, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.00 / 1.90
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 106.680, 75.340, 51.300, 90.00, 90.00, 90.00
R / Rfree (%) 15.8 / 19.9

Other elements in 1jci:

The structure of Stabilization of the Engineered Cation-Binding Loop in Cytochrome C Peroxidase (Ccp) also contains other interesting chemical elements:

Potassium (K) 1 atom

Iron Binding Sites:

The binding sites of Iron atom in the Stabilization of the Engineered Cation-Binding Loop in Cytochrome C Peroxidase (Ccp) (pdb code 1jci). 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 Stabilization of the Engineered Cation-Binding Loop in Cytochrome C Peroxidase (Ccp), PDB code: 1jci:

Iron binding site 1 out of 1 in 1jci

Go back to Iron Binding Sites List in 1jci
Iron binding site 1 out of 1 in the Stabilization of the Engineered Cation-Binding Loop in Cytochrome C Peroxidase (Ccp)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Stabilization of the Engineered Cation-Binding Loop in Cytochrome C Peroxidase (Ccp) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe296

b:13.2
occ:1.00
 FE A:HEM296 0.0 13.2 1.0
O A:HOH1191 2.0 23.8 1.0
NB A:HEM296 2.0 12.2 1.0
NC A:HEM296 2.0 12.1 1.0
ND A:HEM296 2.0 12.1 1.0
NA A:HEM296 2.0 12.3 1.0
NE2 A:HIS175 2.1 11.5 1.0
CD2 A:HIS175 3.0 11.6 1.0
C1C A:HEM296 3.1 12.4 1.0
C4B A:HEM296 3.1 12.5 1.0
C4D A:HEM296 3.1 12.1 1.0
C1A A:HEM296 3.1 12.4 1.0
C1B A:HEM296 3.1 12.5 1.0
CE1 A:HIS175 3.1 11.7 1.0
C4A A:HEM296 3.1 12.5 1.0
C1D A:HEM296 3.1 11.9 1.0
C4C A:HEM296 3.1 12.2 1.0
CHC A:HEM296 3.4 12.2 1.0
CHA A:HEM296 3.4 12.1 1.0
CHB A:HEM296 3.4 12.3 1.0
CHD A:HEM296 3.5 11.9 1.0
NE1 A:TRP51 4.1 10.1 1.0
ND1 A:HIS175 4.2 11.3 1.0
CG A:HIS175 4.2 11.1 1.0
O A:HOH1205 4.2 27.2 0.5
NE A:ARG48 4.2 9.1 0.6
O A:HOH874 4.2 17.3 1.0
C3D A:HEM296 4.3 11.8 1.0
C3B A:HEM296 4.3 12.5 1.0
C2D A:HEM296 4.3 11.7 1.0
C2C A:HEM296 4.3 12.2 1.0
C2B A:HEM296 4.3 12.4 1.0
C2A A:HEM296 4.3 12.3 1.0
C3C A:HEM296 4.3 12.3 1.0
C3A A:HEM296 4.3 12.3 1.0
CD1 A:TRP51 4.7 10.2 1.0
NH2 A:ARG48 4.8 9.2 0.6
CG A:ARG48 4.8 9.7 0.6
CD A:ARG48 4.9 9.4 0.6
CZ A:ARG48 5.0 9.0 0.6

Reference:

B.Bhaskar, C.A.Bonagura, H.Li, T.L.Poulos. Cation-Induced Stabilization of the Engineered Cation-Binding Loop in Cytochrome C Peroxidase (Ccp). Biochemistry V. 41 2684 2002.
ISSN: ISSN 0006-2960
PubMed: 11851415
DOI: 10.1021/BI011599Y
Page generated: Sat Aug 3 08:26:52 2024

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