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Iron in PDB 1aes: Specificity of Ligand Binding to A Buried Polar Cavity at the Active Site of Cytochrome C Peroxidase (Imidazole)

Enzymatic activity of Specificity of Ligand Binding to A Buried Polar Cavity at the Active Site of Cytochrome C Peroxidase (Imidazole)

All present enzymatic activity of Specificity of Ligand Binding to A Buried Polar Cavity at the Active Site of Cytochrome C Peroxidase (Imidazole):
1.11.1.5;

Protein crystallography data

The structure of Specificity of Ligand Binding to A Buried Polar Cavity at the Active Site of Cytochrome C Peroxidase (Imidazole), PDB code: 1aes 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 (°) 108.000, 77.300, 51.800, 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 to A Buried Polar Cavity at the Active Site of Cytochrome C Peroxidase (Imidazole) (pdb code 1aes). 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 to A Buried Polar Cavity at the Active Site of Cytochrome C Peroxidase (Imidazole), PDB code: 1aes:

Iron binding site 1 out of 1 in 1aes

Go back to Iron Binding Sites List in 1aes
Iron binding site 1 out of 1 in the Specificity of Ligand Binding to A Buried Polar Cavity at the Active Site of Cytochrome C Peroxidase (Imidazole)


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 to A Buried Polar Cavity at the Active Site of Cytochrome C Peroxidase (Imidazole) 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
NA A:HEM295 2.1 8.8 1.0
NB A:HEM295 2.1 8.7 1.0
NC A:HEM295 2.1 9.9 1.0
ND A:HEM295 2.1 11.1 1.0
CE1 A:HIS175 2.6 12.5 1.0
C4A A:HEM295 3.0 7.9 1.0
C4C A:HEM295 3.0 10.9 1.0
C1B A:HEM295 3.0 8.0 1.0
C4B A:HEM295 3.0 5.5 1.0
C1A A:HEM295 3.1 9.4 1.0
C1D A:HEM295 3.1 8.0 1.0
C1C A:HEM295 3.1 11.1 1.0
C4D A:HEM295 3.1 7.7 1.0
CD2 A:HIS175 3.1 14.5 1.0
CHB A:HEM295 3.3 6.2 1.0
CHD A:HEM295 3.4 4.5 1.0
CHC A:HEM295 3.4 6.2 1.0
CHA A:HEM295 3.4 5.9 1.0
HE1 A:TRP51 3.5 0.0 1.0
ND1 A:HIS175 3.8 14.5 1.0
CG A:HIS175 4.1 13.7 1.0
NE1 A:TRP51 4.1 17.0 1.0
C3A A:HEM295 4.2 5.6 1.0
C3C A:HEM295 4.2 9.0 1.0
C2A A:HEM295 4.2 9.1 1.0
O A:HOH344 4.2 31.5 1.0
C3B A:HEM295 4.2 5.8 1.0
C2C A:HEM295 4.3 10.9 1.0
C2B A:HEM295 4.3 5.9 1.0
C2D A:HEM295 4.3 8.8 1.0
C3D A:HEM295 4.3 7.1 1.0
O A:HOH300 4.4 30.1 1.0
HD1 A:HIS175 4.6 0.0 1.0
CD1 A:TRP51 4.6 15.6 1.0
HE A:ARG48 4.8 0.0 1.0
CD A:ARG48 5.0 17.2 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: Sat Aug 3 02:10:27 2024

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