Acetylglutamate Kinase

(All numbering and residues are taken from first PDB file)

Bending Residue Dihedral Analysis

Residue
i
Residue
i+1
Distance of hinge axis to residue i in conformer 1
(A)
Distance of hinge axis to residue i in conformer 2
(A)
Change in psi (i)
(deg)
Change in phi (i+1)
(deg)
Angle of psi(i) axis to hinge axis conformer 1
(deg)
Angle of psi(i) axis to hinge axis conformer 2
(deg)
Percentage Progress
 ARG-31   GLU-32  10.3 8.8 -21.0 -5.2 55.8 67.6 27.4
 GLU-32   SER-33  12.8 11.6 15.2 -3.0 53.3 56.1 30.3
 SER-33   HIS-34  14.7 13.1 21.4 -3.1 30.4 18.5 64.1
 HIS-34   GLN-35  13.6 12.4 -3.8 22.2 83.8 87.7 -20.9
 GLN-35   ARG-36  14.0 14.1 -40.1 -0.3 136.0 117.0 -118.7
 ARG-36   PRO-37  11.8 11.4 -3.0 -16.2 70.6 48.3 56.0
 PRO-37   LEU-38  11.2 10.6 10.0 22.2 80.7 79.2 12.7
 LEU-38   VAL-39  7.7 7.3 0.4 3.2 99.8 96.7 -19.1

Downloading Image

Graph shows rotational transition at bending residues and can be used to identify hinge bending residues.
Probably only informative for interdomain rotations greater than 20 degrees


Residue
i
Residue
i+1
Distance of hinge axis to residue i in conformer 1
(A)
Distance of hinge axis to residue i in conformer 2
(A)
Change in psi (i)
(deg)
Change in phi (i+1)
(deg)
Angle of psi(i) axis to hinge axis conformer 1
(deg)
Angle of psi(i) axis to hinge axis conformer 2
(deg)
Percentage Progress
 ILE-177   LEU-178  1.1 1.6 -9.1 1.2 74.3 70.0 28.7
 LEU-178   LEU-179  4.8 5.5 4.3 4.4 126.9 124.0 -0.4
 LEU-179   SER-180  5.6 6.9 2.0 18.2 112.6 101.6 -28.1
 SER-180   ASP-181  9.2 10.7 -33.3 8.3 72.5 60.2 48.6

Downloading Image

Graph shows rotational transition at bending residues and can be used to identify hinge bending residues.
Probably only informative for interdomain rotations greater than 20 degrees