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Iron in PDB 1aen: Specificity of Ligand Binding to A Buried Polar Cavity at the Active Site of Cytochrome C Peroxidase (2-Amino-5- Methylthiazole)

Enzymatic activity of Specificity of Ligand Binding to A Buried Polar Cavity at the Active Site of Cytochrome C Peroxidase (2-Amino-5- Methylthiazole)

All present enzymatic activity of Specificity of Ligand Binding to A Buried Polar Cavity at the Active Site of Cytochrome C Peroxidase (2-Amino-5- Methylthiazole):
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 (2-Amino-5- Methylthiazole), PDB code: 1aen was solved by R.A.Musah, G.M.Jensen, S.W.Bunte, R.Rosenfeld, 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 to A Buried Polar Cavity at the Active Site of Cytochrome C Peroxidase (2-Amino-5- Methylthiazole) (pdb code 1aen). 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 (2-Amino-5- Methylthiazole), PDB code: 1aen:

Iron binding site 1 out of 1 in 1aen

Go back to Iron Binding Sites List in 1aen
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 (2-Amino-5- Methylthiazole)


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 (2-Amino-5- Methylthiazole) 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:

R.A.Musah, G.M.Jensen, S.W.Bunte, R.J.Rosenfeld, D.B.Goodin. Artificial Protein Cavities As Specific Ligand-Binding Templates: Characterization of An Engineered Heterocyclic Cation-Binding Site That Preserves the Evolved Specificity of the Parent Protein. J.Mol.Biol. V. 315 845 2002.
ISSN: ISSN 0022-2836
PubMed: 11812152
DOI: 10.1006/JMBI.2001.5287
Page generated: Sat Aug 3 02:09:28 2024

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