Aspartate Carbamoyltransferase (Aspartate Transcarbamylase) 3 (T State) (E.C.2.1.3.2)

(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  8.5 8.7 -3.5 -2.7 142.4 141.8 -10.1
 TYR-226   MET-227  6.4 6.5 9.0 -7.7 85.3 92.4 3.3
 MET-227   THR-228  3.3 3.3 4.3 -3.5 54.6 55.2 10.7

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


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  8.9 8.6 25.1 -17.7 78.7 122.3 4.3
 PHE-247   VAL-248  7.1 6.1 -86.8 -10.7 27.1 25.1 287.8
 VAL-248   LEU-249  8.7 8.0 25.8 -30.4 80.2 77.3 -28.0
 LEU-249   ARG-250  9.5 9.8 14.0 -9.2 126.9 127.6 -29.4

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