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  7.1 6.9 -7.5 -12.7 70.8 72.0 40.7
 GLY-115   PRO-116  4.2 4.4 26.5 -12.9 100.4 114.2 8.3
 PRO-116   GLU-117  6.0 6.5 -78.4 63.9 20.6 27.6 54.9
 GLU-117   ILE-118  8.3 7.8 -8.2 -2.8 85.3 85.0 -2.1

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
 LEU-217   PRO-218  10.2 10.6 -4.1 0.0 45.6 55.1 9.0
 PRO-218   ALA-219  8.6 8.8 -10.3 -12.1 107.2 107.8 0.6
 ALA-219   VAL-220  5.5 5.6 -0.2 0.3 83.2 54.1 19.2
 VAL-220   SER-221  3.8 4.3 -44.8 7.4 81.7 65.4 65.8
 SER-221   GLU-222  6.8 7.1 4.8 0.0 157.1 152.7 -16.7

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