Pyruvate Kinase, M2 Isozyme

(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
 LYS-114   GLY-115  8.3 8.1 -10.0 -10.7 72.1 71.5 50.9
 GLY-115   PRO-116  6.1 6.2 23.1 -6.9 108.2 121.7 -20.4
 PRO-116   GLU-117  8.0 8.3 -79.6 79.6 12.2 26.9 -11.1
 GLU-117   ILE-118  9.8 9.4 -20.4 2.2 76.9 71.5 108.0

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
 LEU-217   PRO-218  11.9 12.4 -4.0 -6.6 36.3 46.3 28.6
 PRO-218   ALA-219  10.6 10.8 -8.9 -3.4 100.2 99.7 23.4
 ALA-219   VAL-220  7.0 7.3 -5.6 5.1 85.4 55.3 11.2
 VAL-220   SER-221  6.5 7.0 -47.5 8.9 91.2 76.4 37.6
 SER-221   GLU-222  9.6 10.2 -0.6 14.0 27.4 29.8 -31.0

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