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

Enzymatic activity of Variation in the Strength of A Ch to O Hydrogen Bond in An Artificial Protein Cavity (1-Methylimidazole)

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

Iron binding site 1 out of 1 in 1aet

Go back to Iron Binding Sites List in 1aet
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 (1-Methylimidazole)


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 (1-Methylimidazole) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe295

b:16.9
occ:1.00
 FE A:HEM295 0.0 16.9 1.0
O A:HOH313 1.9 17.3 1.0
NE2 A:HIS175 2.0 16.2 1.0
NC A:HEM295 2.0 12.8 1.0
NA A:HEM295 2.1 15.6 1.0
ND A:HEM295 2.1 15.4 1.0
NB A:HEM295 2.1 14.0 1.0
CE1 A:HIS175 2.8 13.4 1.0
C4C A:HEM295 3.0 16.6 1.0
C4D A:HEM295 3.0 14.8 1.0
C1A A:HEM295 3.0 17.2 1.0
C4B A:HEM295 3.0 12.2 1.0
C1C A:HEM295 3.1 14.8 1.0
C1D A:HEM295 3.1 15.2 1.0
C1B A:HEM295 3.1 13.1 1.0
CD2 A:HIS175 3.1 16.8 1.0
C4A A:HEM295 3.1 14.9 1.0
CHA A:HEM295 3.3 13.8 1.0
CHC A:HEM295 3.4 11.9 1.0
CHD A:HEM295 3.4 10.7 1.0
CHB A:HEM295 3.4 13.1 1.0
HE1 A:TRP51 3.5 0.0 1.0
ND1 A:HIS175 4.0 10.8 1.0
NE1 A:TRP51 4.1 17.6 1.0
CG A:HIS175 4.2 14.4 1.0
C2A A:HEM295 4.2 16.2 1.0
C3C A:HEM295 4.2 16.7 1.0
C3D A:HEM295 4.2 15.0 1.0
C2D A:HEM295 4.2 13.0 1.0
C3A A:HEM295 4.3 15.2 1.0
C2C A:HEM295 4.3 13.9 1.0
C3B A:HEM295 4.3 14.0 1.0
C2B A:HEM295 4.3 12.0 1.0
O A:HOH300 4.4 33.8 1.0
O A:HOH344 4.5 38.2 1.0
CD1 A:TRP51 4.5 19.5 1.0
HE A:ARG48 4.6 0.0 1.0
HD1 A:HIS175 4.8 0.0 1.0

Reference:

M.M.Fitzgerald, R.A.Musah, D.E.Mcree, D.B.Goodin. 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 02:10:38 2024

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