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Iron in PDB 1aeq: Variation in the Strength of A Ch to O Hydrogen Bond in An Artificial Protein Cavity (2-Ethylimidazole)

Enzymatic activity of Variation in the Strength of A Ch to O Hydrogen Bond in An Artificial Protein Cavity (2-Ethylimidazole)

All present enzymatic activity of Variation in the Strength of A Ch to O Hydrogen Bond in An Artificial Protein Cavity (2-Ethylimidazole):
1.11.1.5;

Protein crystallography data

The structure of Variation in the Strength of A Ch to O Hydrogen Bond in An Artificial Protein Cavity (2-Ethylimidazole), PDB code: 1aeq 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 (°) 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 Variation in the Strength of A Ch to O Hydrogen Bond in An Artificial Protein Cavity (2-Ethylimidazole) (pdb code 1aeq). 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 Variation in the Strength of A Ch to O Hydrogen Bond in An Artificial Protein Cavity (2-Ethylimidazole), PDB code: 1aeq:

Iron binding site 1 out of 1 in 1aeq

Go back to Iron Binding Sites List in 1aeq
Iron binding site 1 out of 1 in the Variation in the Strength of A Ch to O Hydrogen Bond in An Artificial Protein Cavity (2-Ethylimidazole)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Variation in the Strength of A Ch to O Hydrogen Bond in An Artificial Protein Cavity (2-Ethylimidazole) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe295

b:10.8
occ:1.00
 FE A:HEM295 0.0 10.8 1.0
NE2 A:HIS175 2.0 7.4 1.0
NC A:HEM295 2.1 8.9 1.0
ND A:HEM295 2.1 8.0 1.0
NB A:HEM295 2.1 8.8 1.0
NA A:HEM295 2.1 10.1 1.0
O A:HOH313 2.4 18.6 1.0
CE1 A:HIS175 2.8 8.8 1.0
C1B A:HEM295 3.0 8.8 1.0
C4C A:HEM295 3.0 10.1 1.0
C4A A:HEM295 3.0 11.9 1.0
C1A A:HEM295 3.0 11.3 1.0
C4D A:HEM295 3.1 7.2 1.0
C1D A:HEM295 3.1 9.0 1.0
C1C A:HEM295 3.1 8.9 1.0
CD2 A:HIS175 3.1 12.6 1.0
C4B A:HEM295 3.1 9.0 1.0
CHB A:HEM295 3.4 11.2 1.0
CHD A:HEM295 3.4 3.3 1.0
CHA A:HEM295 3.4 9.4 1.0
CHC A:HEM295 3.4 6.1 1.0
HE1 A:TRP51 3.5 0.0 1.0
ND1 A:HIS175 4.0 12.6 1.0
NE1 A:TRP51 4.1 12.6 1.0
CG A:HIS175 4.2 5.8 1.0
C3A A:HEM295 4.2 10.1 1.0
C2A A:HEM295 4.2 10.2 1.0
C3C A:HEM295 4.2 9.5 1.0
C3D A:HEM295 4.3 7.0 1.0
C2B A:HEM295 4.3 11.3 1.0
C2D A:HEM295 4.3 7.7 1.0
C3B A:HEM295 4.3 12.4 1.0
C2C A:HEM295 4.3 10.4 1.0
O A:HOH344 4.3 22.1 1.0
O A:HOH300 4.4 24.4 1.0
HE A:ARG48 4.4 0.0 1.0
CD1 A:TRP51 4.5 8.7 1.0
C5 A:2EZ296 4.7 15.0 1.0
HD1 A:HIS175 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: Sun Dec 13 14:03:48 2020

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