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Iron in PDB 1cmq: Small Molecule Binding to An Artificially Created Cavity at the Active Site of Cytochrome C Peroxidase

Enzymatic activity of Small Molecule Binding to An Artificially Created Cavity at the Active Site of Cytochrome C Peroxidase

All present enzymatic activity of Small Molecule Binding to An Artificially Created Cavity at the Active Site of Cytochrome C Peroxidase:
1.11.1.5;

Protein crystallography data

The structure of Small Molecule Binding to An Artificially Created Cavity at the Active Site of Cytochrome C Peroxidase, PDB code: 1cmq was solved by M.M.Fitzgerald, D.E.Mcree, M.J.Churchill, 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 (%) 19 / n/a

Iron Binding Sites:

The binding sites of Iron atom in the Small Molecule Binding to An Artificially Created Cavity at the Active Site of Cytochrome C Peroxidase (pdb code 1cmq). 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 Small Molecule Binding to An Artificially Created Cavity at the Active Site of Cytochrome C Peroxidase, PDB code: 1cmq:

Iron binding site 1 out of 1 in 1cmq

Go back to Iron Binding Sites List in 1cmq
Iron binding site 1 out of 1 in the Small Molecule Binding to An Artificially Created Cavity at the Active Site 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 Small Molecule Binding to An Artificially Created Cavity at the Active Site of Cytochrome C Peroxidase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe295

b:10.2
occ:1.00
 FE A:HEM295 0.0 10.2 1.0
NE2 A:HIS175 2.0 16.4 1.0
NC A:HEM295 2.1 7.6 1.0
NA A:HEM295 2.1 7.0 1.0
ND A:HEM295 2.1 9.5 1.0
NB A:HEM295 2.1 6.1 1.0
O A:HOH313 2.1 11.3 1.0
CE1 A:HIS175 2.8 10.8 1.0
C4C A:HEM295 3.0 8.4 1.0
C4A A:HEM295 3.0 7.7 1.0
C1D A:HEM295 3.0 6.5 1.0
C1B A:HEM295 3.0 7.6 1.0
C1A A:HEM295 3.0 8.4 1.0
CD2 A:HIS175 3.1 13.9 1.0
C4D A:HEM295 3.1 8.7 1.0
C4B A:HEM295 3.1 4.4 1.0
C1C A:HEM295 3.1 8.6 1.0
CHD A:HEM295 3.3 3.4 1.0
CHB A:HEM295 3.3 5.0 1.0
CHA A:HEM295 3.4 5.6 1.0
CHC A:HEM295 3.4 5.2 1.0
HE1 A:TRP51 3.5 0.0 1.0
ND1 A:HIS175 3.9 12.6 1.0
CG A:HIS175 4.1 12.9 1.0
NE1 A:TRP51 4.2 16.3 1.0
C3A A:HEM295 4.2 3.6 1.0
C2D A:HEM295 4.2 9.4 1.0
C2A A:HEM295 4.2 8.0 1.0
C3C A:HEM295 4.2 7.5 1.0
C3D A:HEM295 4.3 8.7 1.0
C2B A:HEM295 4.3 5.4 1.0
C3B A:HEM295 4.3 5.4 1.0
C2C A:HEM295 4.3 7.3 1.0
HE A:ARG48 4.6 0.0 1.0
O A:HOH344 4.6 26.4 1.0
O A:HOH403 4.6 22.2 1.0
CD1 A:TRP51 4.7 15.3 1.0
O A:HOH300 4.7 24.7 1.0
HD1 A:HIS175 4.8 0.0 1.0

Reference:

M.M.Fitzgerald, M.J.Churchill, D.E.Mcree, D.B.Goodin. Small Molecule Binding to An Artificially Created Cavity at the Active Site of Cytochrome C Peroxidase. Biochemistry V. 33 3807 1994.
ISSN: ISSN 0006-2960
PubMed: 8142383
DOI: 10.1021/BI00179A004
Page generated: Sat Aug 3 03:23:23 2024

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