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
 PRO-100   GLU-101  3.5 3.3 2.0 -8.3 30.6 26.5 -68.3
 GLU-101   ARG-102  4.5 4.6 25.5 7.5 42.4 51.9 165.9
 ARG-102   ILE-103  1.4 1.7 -12.5 -12.3 59.9 64.1 130.1

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
 ASN-148   VAL-149  13.6 13.6 1.8 9.5 124.7 127.4 19.0
 VAL-149   VAL-150  12.7 12.5 5.7 -31.2 71.8 63.2 -51.5
 VAL-150   LEU-151  10.1 10.3 38.5 -49.3 61.2 46.3 -57.9
 LEU-151   ALA-152  12.7 13.0 -121.2 4.8 45.5 69.2 672.1

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