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
 ILE-224   LEU-225  11.8 11.7 -1.8 0.8 105.8 102.6 1.6
 LEU-225   TYR-226  8.6 8.5 1.5 -0.5 141.3 141.5 3.1
 TYR-226   MET-227  6.3 6.2 -14.6 13.9 93.5 86.9 10.1
 MET-227   THR-228  3.2 3.0 -2.5 1.7 55.5 55.7 7.0

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  8.7 8.8 -10.1 4.7 123.2 74.6 -13.2
 PHE-247   VAL-248  6.3 7.0 89.0 11.9 24.7 32.1 273.7
 VAL-248   LEU-249  8.2 8.9 -34.2 32.3 78.0 79.8 -9.0
 LEU-249   ARG-250  9.9 9.5 -10.5 4.5 127.4 127.3 -26.9
 ARG-250   ALA-251  13.5 13.1 1.5 4.8 102.0 99.3 -10.1
 ALA-251   SER-252  15.9 15.7 8.1 -13.9 148.8 147.3 15.7

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