Uridylmonophosphate/cytidylmonophosphate 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
 VAL-123   MET-124  2.6 2.4 -5.6 2.9 112.8 114.3 17.1
 MET-124   THR-125  0.7 0.9 -6.1 4.5 144.6 145.6 -12.0
 THR-125   GLN-126  1.6 1.2 6.5 -6.1 103.8 100.6 -14.5
 GLN-126   ARG-127  4.9 4.6 0.2 -0.5 107.9 108.0 40.0

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
 SER-144   ILE-145  4.5 5.0 4.0 -0.3 30.8 30.0 39.1
 ILE-145   LYS-146  3.1 3.4 0.4 -5.0 97.5 91.8 14.8
 LYS-146   LYS-147  3.6 3.8 2.2 0.2 111.3 109.7 18.8
 LYS-147   ARG-148  6.4 6.7 3.8 3.8 42.0 39.2 38.0

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