Pyruvate Kinase Isozymes M1/m2

(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
 GLY-116   PRO-117  5.1 5.1 8.5 7.3 79.3 86.6 2.2
 PRO-117   GLU-118  1.4 1.4 -58.3 15.0 34.6 39.4 84.4
 GLU-118   ILE-119  2.8 2.5 27.5 -18.3 77.8 75.4 18.0

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
 VAL-216   ASP-217  8.2 7.1 1.9 18.7 143.7 144.0 -28.2
 ASP-217   LEU-218  8.5 7.4 -16.3 0.2 54.0 67.6 41.8
 LEU-218   PRO-219  4.8 3.6 1.8 -21.8 108.8 104.5 32.6
 PRO-219   ALA-220  4.9 3.9 12.1 -8.5 57.0 56.9 7.0
 ALA-220   VAL-221  6.8 6.0 -4.0 -8.9 78.2 69.3 9.9
 VAL-221   SER-222  6.0 6.0 -19.5 -6.4 64.5 47.4 42.1
 SER-222   GLU-223  3.6 3.4 12.5 -4.9 144.2 134.1 -8.3
 GLU-223   LYS-224  4.8 4.9 -7.9 8.0 101.1 113.3 1.1
 LYS-224   ASP-225  8.1 7.5 1.0 1.1 72.5 64.0 -0.1

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