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  8.1 8.0 2.3 -4.5 122.5 118.8 -4.8
 LYS-114   GLY-115  7.4 7.3 -1.8 -16.8 75.4 76.3 8.7
 GLY-115   PRO-116  3.6 3.6 23.8 -0.2 78.8 95.1 6.8
 PRO-116   GLU-117  3.7 3.8 -80.5 64.3 32.1 43.8 53.9
 GLU-117   ILE-118  6.7 6.7 -10.2 -5.6 99.5 101.7 32.3

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


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
 PRO-218   ALA-219  4.9 4.5 -8.7 -1.3 122.4 117.6 -13.3
 ALA-219   VAL-220  4.0 3.1 -11.7 7.9 79.8 67.0 -8.6
 VAL-220   SER-221  1.3 1.2 -34.2 7.4 61.8 54.1 69.4
 SER-221   GLU-222  2.4 2.4 7.7 -7.0 150.2 144.6 -13.1
 GLU-222   LYS-223  3.8 4.2 -7.5 5.1 97.3 104.8 17.9
 LYS-223   ASP-224  6.6 6.9 -4.2 0.9 105.8 104.9 -2.5
 ASP-224   ILE-225  5.3 5.3 3.5 -13.7 140.6 141.6 46.9

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