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
 ASP-112   THR-113  12.5 12.5 0.7 12.1 63.8 61.2 -16.3
 THR-113   LYS-114  9.3 9.2 2.2 -13.7 123.6 112.6 17.8
 LYS-114   GLY-115  7.5 6.7 -15.7 -13.0 79.4 70.6 26.4
 GLY-115   PRO-116  4.2 3.5 17.9 -8.8 82.9 94.9 -2.3
 PRO-116   GLU-117  0.6 0.3 -74.5 38.6 33.7 35.8 69.0
 GLU-117   ILE-118  3.2 3.2 0.7 -3.0 77.3 79.2 4.4

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


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
 ASP-216   LEU-217  9.4 8.3 68.5 -55.2 129.5 124.5 -11.6
 LEU-217   PRO-218  6.0 4.8 -21.6 5.7 61.9 64.1 18.6
 PRO-218   ALA-219  5.0 3.9 -7.9 -8.9 124.3 119.1 -6.7
 ALA-219   VAL-220  5.8 4.5 6.0 1.9 90.4 118.1 -18.7
 VAL-220   SER-221  3.8 3.4 -64.7 51.3 67.5 59.7 -3.8
 SER-221   GLU-222  1.8 1.7 -13.3 0.8 32.0 23.6 44.8

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