Aspartate Carbamoyltransferase

(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-140   ASP-141  4.8 4.7 -5.4 -0.8 105.2 100.9 45.9
 ASP-141   LEU-142  4.6 4.6 -2.0 4.1 58.1 55.4 -37.1
 LEU-142   PHE-143  2.8 2.9 -0.7 -3.2 107.3 107.7 11.8
 PHE-143   THR-144  0.8 0.8 2.5 -6.2 39.6 39.0 -1.4

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-289   GLY-290  5.7 5.5 2.1 4.5 82.7 83.9 4.9
 GLY-290   ASN-291  5.9 5.5 0.0 3.3 19.0 17.5 24.0
 ASN-291   GLY-292  4.9 4.7 0.2 6.2 54.3 58.1 33.9

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