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Potassium in PDB 6sss: Crystal Structure of Human Microsomal Glutathione S-Transferase 2

Enzymatic activity of Crystal Structure of Human Microsomal Glutathione S-Transferase 2

All present enzymatic activity of Crystal Structure of Human Microsomal Glutathione S-Transferase 2:
2.5.1.18;

Protein crystallography data

The structure of Crystal Structure of Human Microsomal Glutathione S-Transferase 2, PDB code: 6sss was solved by M.Thulasingam, E.Nji, J.Z.Haeggstrom, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 43.33 / 2.50
Space group P 1
Cell size a, b, c (Å), α, β, γ (°) 54.886, 72.162, 72.692, 67.93, 86.71, 86.86
R / Rfree (%) 21.8 / 26.7

Other elements in 6sss:

The structure of Crystal Structure of Human Microsomal Glutathione S-Transferase 2 also contains other interesting chemical elements:

Sodium (Na) 5 atoms

Potassium Binding Sites:

The binding sites of Potassium atom in the Crystal Structure of Human Microsomal Glutathione S-Transferase 2 (pdb code 6sss). 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 Microsomal Glutathione S-Transferase 2, PDB code: 6sss:

Potassium binding site 1 out of 1 in 6sss

Go back to Potassium Binding Sites List in 6sss
Potassium binding site 1 out of 1 in the Crystal Structure of Human Microsomal Glutathione S-Transferase 2


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 Microsomal Glutathione S-Transferase 2 within 5.0Å range:
probe atom residue distance (Å) B Occ
E:K205

b:66.9
occ:1.00
OH E:TYR86 2.7 34.1 1.0
O E:CYS56 2.9 39.8 1.0
HE2 E:TYR86 3.0 36.0 1.0
S E:SCN204 3.1 76.5 1.0
HA E:CYS56 3.1 50.0 1.0
HA E:TYR60 3.1 43.7 1.0
HB2 E:PHE59 3.2 50.6 1.0
N E:TYR60 3.5 36.4 1.0
HG3 E:ARG90 3.5 53.4 1.0
HB2 E:TYR60 3.5 46.3 1.0
HB3 E:PHE59 3.5 50.6 1.0
HD2 E:ARG90 3.5 56.3 1.0
CZ E:TYR86 3.6 31.6 1.0
C E:PHE59 3.6 40.2 1.0
HE E:ARG90 3.6 53.1 1.0
CE2 E:TYR86 3.6 30.0 1.0
CA E:TYR60 3.7 36.4 1.0
H E:TYR60 3.7 43.7 1.0
CB E:PHE59 3.7 42.2 1.0
HD1 E:TYR60 3.7 49.1 1.0
C E:CYS56 3.7 38.8 1.0
NE E:ARG90 3.8 44.3 1.0
CA E:CYS56 3.8 41.7 1.0
HB3 E:CYS56 3.9 55.3 1.0
O E:PHE59 3.9 43.3 1.0
HE21 E:GLN19 4.0 51.8 1.0
CD E:ARG90 4.0 46.9 1.0
CB E:TYR60 4.1 38.6 1.0
H E:PHE59 4.1 49.2 1.0
CA E:PHE59 4.1 41.0 1.0
CG E:ARG90 4.2 44.5 1.0
CZ E:ARG90 4.3 49.2 1.0
HE22 E:GLN19 4.3 51.8 1.0
CB E:CYS56 4.3 46.1 1.0
C E:SCN204 4.4 44.0 1.0
NE2 E:GLN19 4.4 43.1 1.0
CD1 E:TYR60 4.5 40.9 1.0
N E:PHE59 4.5 41.0 1.0
HH21 E:ARG90 4.6 73.8 1.0
NH2 E:ARG90 4.7 61.5 1.0
HB3 E:PHE63 4.7 37.6 1.0
HG2 E:ARG90 4.7 53.4 1.0
HB2 E:PHE63 4.7 37.6 1.0
O E:ASN55 4.7 39.1 0.4
CG E:TYR60 4.8 38.0 1.0
O E:ASN55 4.8 39.6 0.6
NH1 E:ARG90 4.9 44.8 1.0
HB3 E:TYR60 4.9 46.3 1.0
CE1 E:TYR86 4.9 35.3 1.0
HD3 E:ARG90 4.9 56.3 1.0
HH11 E:ARG90 4.9 53.8 1.0
CD2 E:TYR86 5.0 30.8 1.0

Reference:

M.Thulasingam, E.Nji, J.Z.Haeggstrom. Crystal Structure of Human Microsomal Glutathione S-Transferase 2 To Be Published.
Page generated: Mon Aug 12 17:35:52 2024

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