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
 THR-113   LYS-114  8.5 8.6 -14.7 15.8 54.7 60.1 0.1
 LYS-114   GLY-115  7.7 7.9 -12.0 -6.4 81.1 79.2 1.2
 GLY-115   PRO-116  4.0 4.2 9.9 8.9 80.3 97.4 -26.2
 PRO-116   GLU-117  4.1 3.8 -88.2 48.0 29.5 37.3 155.2
 GLU-117   ILE-118  7.0 6.6 -7.9 1.8 96.6 101.6 -17.8

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  6.6 6.5 -17.8 6.1 56.6 69.9 3.2
 PRO-218   ALA-219  4.3 3.8 -17.7 9.6 121.5 120.7 -4.6
 ALA-219   VAL-220  2.9 1.9 -9.6 6.3 84.7 64.1 -8.1
 VAL-220   SER-221  1.1 1.2 -11.5 -28.3 64.6 52.8 105.1
 SER-221   GLU-222  3.6 3.0 9.8 6.9 146.6 133.2 -61.3
 GLU-222   LYS-223  5.6 5.3 -22.6 17.3 98.8 112.1 12.5
 LYS-223   ASP-224  8.1 8.0 4.8 -4.0 79.1 70.9 12.6
 ASP-224   ILE-225  6.3 6.2 -2.5 -1.6 40.4 40.3 7.4

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