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 6.7 -7.9 -11.9 75.7 77.0 38.6
 GLY-115   PRO-116  3.6 3.3 21.5 -0.5 88.0 100.9 12.6
 PRO-116   GLU-117  4.5 5.0 -77.7 72.1 30.2 37.8 15.8
 GLU-117   ILE-118  7.4 7.3 -9.8 -9.6 97.8 95.3 27.8

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  8.6 8.7 6.5 -9.8 122.4 116.7 2.8
 PRO-218   ALA-219  6.5 6.5 -11.3 0.3 119.1 112.2 -11.2
 ALA-219   VAL-220  4.2 4.1 -12.9 7.4 86.5 66.9 11.1
 VAL-220   SER-221  1.2 1.5 -48.3 17.9 70.8 60.8 65.1
 SER-221   GLU-222  4.4 4.3 1.4 6.3 152.4 145.3 -14.3

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