Aspartate Carbamoyltransferase Catalytic Chain

(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
 LEU-225   TYR-226  8.9 8.9 11.9 -13.8 40.4 35.4 -9.7
 TYR-226   MET-227  7.0 6.8 1.6 2.2 87.9 89.2 -1.6
 MET-227   THR-228  3.8 3.7 -28.1 47.7 126.1 121.4 50.0
 THR-228   ARG-229  1.8 1.9 38.1 -31.0 74.5 64.1 26.0

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
 GLN-246   PHE-247  8.0 8.4 69.0 -32.9 69.2 107.0 25.0
 PHE-247   VAL-248  6.1 5.7 -60.7 -35.4 36.5 22.9 282.6
 VAL-248   LEU-249  7.9 7.3 29.2 -27.5 76.4 81.0 18.6
 LEU-249   ARG-250  9.3 9.1 28.9 -42.0 123.6 115.7 17.4
 ARG-250   ALA-251  13.1 12.8 -5.6 -4.0 101.5 103.3 -2.8
 ALA-251   SER-252  15.8 15.7 -2.8 -0.6 160.3 156.2 -11.5

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