S-Adenosylhomocysteine Hydrolase

(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-385   PRO-386  10.5 10.7 16.0 2.0 74.5 75.6 4.5
 PRO-386   LYS-387  11.1 10.8 -4.2 -1.2 61.8 72.1 -5.8
 LYS-387   LYS-388  8.4 8.0 5.2 -1.6 145.6 144.1 -31.1
 LYS-388   LEU-389  11.0 10.4 -22.4 17.7 35.3 32.5 26.3
 LEU-389   ASP-390  10.5 10.1 0.0 5.2 74.1 79.2 9.4
 ASP-390   GLU-391  6.7 6.4 -19.0 4.3 119.9 120.6 -60.2
 ASP-390   GLU-391  6.7 6.4 -19.0 4.3 119.9 120.6 -60.2

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
 ASP-390   GLU-391  6.7 6.4 -19.0 4.3 119.9 120.6 -60.2
 ASP-390   GLU-391  6.7 6.4 -19.0 4.3 119.9 120.6 -60.2
 GLU-391   ALA-392  7.3 6.2 28.2 -17.8 20.4 24.4 57.6
 ALA-392   VAL-393  9.1 8.0 11.0 1.2 46.9 45.2 49.6
 VAL-393   ALA-394  6.6 5.2 -24.5 14.5 105.0 105.1 -23.0
 ALA-394   GLU-395  4.5 3.3 -9.5 9.5 135.1 128.3 -2.8
 GLU-395   ALA-396  7.6 6.8 -7.0 -13.6 156.8 160.7 -109.4

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