Atomistry » Potassium » PDB 6u9t-6v7h » 6v76
Atomistry »
  Potassium »
    PDB 6u9t-6v7h »
      6v76 »

Potassium in PDB 6v76: Crystal Structure of Human PKM2 in Complex with L-Valine

Enzymatic activity of Crystal Structure of Human PKM2 in Complex with L-Valine

All present enzymatic activity of Crystal Structure of Human PKM2 in Complex with L-Valine:
2.7.1.40;

Protein crystallography data

The structure of Crystal Structure of Human PKM2 in Complex with L-Valine, PDB code: 6v76 was solved by S.Nandi, M.Dey, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 61.44 / 2.75
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 81.040, 154.980, 91.960, 90.00, 102.36, 90.00
R / Rfree (%) 22.3 / 26.5

Other elements in 6v76:

The structure of Crystal Structure of Human PKM2 in Complex with L-Valine also contains other interesting chemical elements:

Magnesium (Mg) 2 atoms
Chlorine (Cl) 2 atoms

Potassium Binding Sites:

The binding sites of Potassium atom in the Crystal Structure of Human PKM2 in Complex with L-Valine (pdb code 6v76). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total only one binding site of Potassium was determined in the Crystal Structure of Human PKM2 in Complex with L-Valine, PDB code: 6v76:

Potassium binding site 1 out of 1 in 6v76

Go back to Potassium Binding Sites List in 6v76
Potassium binding site 1 out of 1 in the Crystal Structure of Human PKM2 in Complex with L-Valine


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Crystal Structure of Human PKM2 in Complex with L-Valine within 5.0Å range:
probe atom residue distance (Å) B Occ
C:K602

b:50.5
occ:1.00
OD1 C:ASN75 2.7 35.1 1.0
O C:THR114 2.7 39.6 1.0
OD1 C:ASP113 2.8 41.1 1.0
OG C:SER77 3.1 48.2 1.0
CG C:ASP113 3.5 40.6 1.0
OG C:SER243 3.6 42.0 1.0
C C:THR114 3.6 40.0 1.0
CG C:ASN75 3.7 36.9 1.0
CB C:SER77 3.9 39.2 1.0
O C:ASP113 3.9 36.3 1.0
CA C:LYS115 4.0 38.2 1.0
NZ C:LYS270 4.1 35.6 1.0
CB C:ASP113 4.1 37.7 1.0
N C:SER77 4.1 44.8 1.0
C C:ASP113 4.1 39.0 1.0
N C:LYS115 4.2 39.5 1.0
OD2 C:ASP113 4.2 37.2 1.0
ND2 C:ASN75 4.3 36.4 1.0
NH2 C:ARG73 4.4 40.1 1.0
N C:THR114 4.5 34.1 1.0
CA C:SER77 4.5 45.9 1.0
CA C:THR114 4.7 35.4 1.0
N C:PHE76 4.7 34.8 1.0
O C:LYS115 4.7 41.8 1.0
CB C:SER243 4.7 33.7 1.0
C C:LYS115 4.7 41.2 1.0
CA C:ASP113 4.7 36.9 1.0
CA C:ASN75 4.8 35.2 1.0
CB C:ASN75 4.8 36.1 1.0
C C:ASN75 5.0 34.9 1.0
C C:PHE76 5.0 39.8 1.0

Reference:

S.Nandi, M.Dey. Biochemical and Structural Investigation of Pyurvate Kinase Muscle Isoform 2 Regulation By Amino Acids To Be Published.
Page generated: Mon Aug 12 17:57:05 2024

Last articles

Zn in 9JYW
Zn in 9IR4
Zn in 9IR3
Zn in 9GMX
Zn in 9GMW
Zn in 9JEJ
Zn in 9ERF
Zn in 9ERE
Zn in 9EGV
Zn in 9EGW
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy