Atomistry » Iron » PDB 1a9w-1aop » 1aeq
Atomistry »
  Iron »
    PDB 1a9w-1aop »
      1aeq »

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: Sat Aug 3 02:10:16 2024

Last articles

Zn in 9JYW
Zn in 9IR4
Zn in 9IR3
Zn in 9GMX
Zn in 9GMW
Zn in 9JEJ
Zn in 9ERF
Zn in 9ERE
Zn in 9EGV
Zn in 9EGW
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy