Cystathionine Beta-Synthase

(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
 SER-420   ALA-421  7.4 8.0 49.2 -8.2 47.9 37.1 103.4
 ALA-421   PRO-422  6.3 7.2 12.5 8.1 29.9 45.7 50.9
 PRO-422   LEU-423  5.5 5.2 4.2 -34.9 41.2 30.9 -76.2

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
 VAL-482   ILE-483  10.2 9.0 24.7 11.2 25.4 25.6 98.1
 ILE-483   TYR-484  8.2 7.7 -10.6 -18.6 122.2 117.9 -5.2
 TYR-484   LYS-485  10.2 10.3 2.1 -10.2 72.8 47.1 -7.6
 LYS-485   GLN-486  10.2 11.4 6.9 -10.1 28.6 36.5 -11.1
 GLN-486   PHE-487  12.3 13.8 -23.4 14.9 143.2 126.9 -13.7

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