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Iron in PDB 1ac8: Variation in the Strength of A Ch to O Hydrogen Bond in An Artificial Protein Cavity (3,4,5-Trimethylthiazole)

Enzymatic activity of Variation in the Strength of A Ch to O Hydrogen Bond in An Artificial Protein Cavity (3,4,5-Trimethylthiazole)

All present enzymatic activity of Variation in the Strength of A Ch to O Hydrogen Bond in An Artificial Protein Cavity (3,4,5-Trimethylthiazole):
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 (3,4,5-Trimethylthiazole), PDB code: 1ac8 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 (3,4,5-Trimethylthiazole) (pdb code 1ac8). 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 (3,4,5-Trimethylthiazole), PDB code: 1ac8:

Iron binding site 1 out of 1 in 1ac8

Go back to Iron Binding Sites List in 1ac8
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 (3,4,5-Trimethylthiazole)


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 (3,4,5-Trimethylthiazole) 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
O A:HOH313 1.9 18.6 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
CE1 A:HIS175 2.8 8.8 1.0
C4C A:HEM295 3.0 10.1 1.0
C1B A:HEM295 3.0 8.8 1.0
C4A A:HEM295 3.1 11.9 1.0
C1D A:HEM295 3.1 9.0 1.0
C4D A:HEM295 3.1 7.2 1.0
C1A A:HEM295 3.1 11.3 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
C3C A:HEM295 4.2 9.5 1.0
C2A A:HEM295 4.2 10.2 1.0
C3D A:HEM295 4.2 7.0 1.0
C2D A:HEM295 4.2 7.7 1.0
C2B A:HEM295 4.3 11.3 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 4.5 0.0 1.0
CD1 A:TRP51 4.5 8.7 1.0
S1 A:TMZ296 4.7 15.0 1.0
HD1 A:HIS175 4.8 0.0 1.0

Reference:

M.M.Fitzgerald, R.A.Musah, D.E.Mcree, D.B.Goodin. Variation in Strength of An Unconventional C-H to O Hydrogen Bond in An Engineered Protein Cavity J.Am.Chem.Soc. V. 119 626 1997.
ISSN: ISSN 0002-7863
Page generated: Wed Jul 16 12:06:47 2025

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