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Iron in PDB 1aeu: Specificity of Ligand Binding in A Polar Cavity of Cytochrome C Peroxidase (2-Methylimidazole)

Enzymatic activity of Specificity of Ligand Binding in A Polar Cavity of Cytochrome C Peroxidase (2-Methylimidazole)

All present enzymatic activity of Specificity of Ligand Binding in A Polar Cavity of Cytochrome C Peroxidase (2-Methylimidazole):
1.11.1.5;

Protein crystallography data

The structure of Specificity of Ligand Binding in A Polar Cavity of Cytochrome C Peroxidase (2-Methylimidazole), PDB code: 1aeu was solved by R.A.Musah, 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) 7.00 / 2.10
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 (%) n/a / n/a

Iron Binding Sites:

The binding sites of Iron atom in the Specificity of Ligand Binding in A Polar Cavity of Cytochrome C Peroxidase (2-Methylimidazole) (pdb code 1aeu). 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 Specificity of Ligand Binding in A Polar Cavity of Cytochrome C Peroxidase (2-Methylimidazole), PDB code: 1aeu:

Iron binding site 1 out of 1 in 1aeu

Go back to Iron Binding Sites List in 1aeu
Iron binding site 1 out of 1 in the Specificity of Ligand Binding in A Polar Cavity of Cytochrome C Peroxidase (2-Methylimidazole)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Specificity of Ligand Binding in A Polar Cavity of Cytochrome C Peroxidase (2-Methylimidazole) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe295

b:11.8
occ:1.00
 FE A:HEM295 0.0 11.8 1.0
NE2 A:HIS175 2.0 16.6 1.0
O A:HOH313 2.0 15.6 1.0
NC A:HEM295 2.0 9.9 1.0
NB A:HEM295 2.1 8.7 1.0
ND A:HEM295 2.1 11.1 1.0
NA A:HEM295 2.1 8.8 1.0
CE1 A:HIS175 2.8 12.5 1.0
C4C A:HEM295 3.0 10.9 1.0
C1D A:HEM295 3.0 8.0 1.0
C1A A:HEM295 3.0 9.4 1.0
C1B A:HEM295 3.1 8.0 1.0
CD2 A:HIS175 3.1 14.5 1.0
C4A A:HEM295 3.1 7.9 1.0
C4B A:HEM295 3.1 5.5 1.0
C1C A:HEM295 3.1 11.1 1.0
C4D A:HEM295 3.1 7.7 1.0
CHD A:HEM295 3.3 4.5 1.0
CHB A:HEM295 3.4 6.2 1.0
CHA A:HEM295 3.4 5.9 1.0
CHC A:HEM295 3.4 6.2 1.0
HE1 A:TRP51 3.5 0.0 1.0
ND1 A:HIS175 4.0 14.5 1.0
CG A:HIS175 4.1 13.7 1.0
NE1 A:TRP51 4.2 17.0 1.0
C3C A:HEM295 4.2 9.0 1.0
C2D A:HEM295 4.2 8.8 1.0
C2A A:HEM295 4.2 9.1 1.0
C3A A:HEM295 4.2 5.6 1.0
C3D A:HEM295 4.2 7.1 1.0
C3B A:HEM295 4.3 5.8 1.0
C2C A:HEM295 4.3 10.9 1.0
C2B A:HEM295 4.3 5.9 1.0
O A:HOH344 4.5 31.5 1.0
O A:HOH300 4.6 30.1 1.0
CD1 A:TRP51 4.7 15.6 1.0
HD1 A:HIS175 4.8 0.0 1.0
HE A:ARG48 4.8 0.0 1.0

Reference:

M.M.Fitzgerald, R.A.Musah, D.E.Mcree, D.B.Goodin. A Ligand-Gated, Hinged Loop Rearrangement Opens A Channel to A Buried Artificial Protein Cavity. Nat.Struct.Biol. V. 3 626 1996.
ISSN: ISSN 1072-8368
PubMed: 8673607
DOI: 10.1038/NSB0796-626
Page generated: Wed Jul 16 12:08:19 2025

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