Aspartate Carbamoyltransferase (Aspartate Transcarbamylase) 3 (R 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
 ASP-223   ILE-224  7.4 7.4 -12.1 11.1 145.8 144.8 4.4
 ILE-224   LEU-225  4.7 4.9 4.6 -3.0 99.3 97.5 13.4
 LEU-225   TYR-226  1.2 1.4 -2.5 2.1 130.8 129.1 17.3
 TYR-226   MET-227  2.7 2.8 1.9 -4.1 82.9 86.1 -18.4

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


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
 ALA-251   SER-252  11.7 11.7 7.8 -10.0 33.9 40.3 -8.3
 SER-252   ASP-253  14.3 14.6 3.2 5.9 27.8 25.2 8.2
 ASP-253   LEU-254  11.9 12.2 -18.7 8.9 98.8 94.1 21.9

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