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Magnesium in PDB 4kxu: Human Transketolase in Covalent Complex with Donor Ketose D-Fructose- 6-Phosphate

Enzymatic activity of Human Transketolase in Covalent Complex with Donor Ketose D-Fructose- 6-Phosphate

All present enzymatic activity of Human Transketolase in Covalent Complex with Donor Ketose D-Fructose- 6-Phosphate:
2.2.1.1;

Protein crystallography data

The structure of Human Transketolase in Covalent Complex with Donor Ketose D-Fructose- 6-Phosphate, PDB code: 4kxu was solved by P.Neumann, S.Luedtke, R.Ficner, K.Tittmann, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 0.98
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 113.760, 85.880, 72.990, 90.00, 125.31, 90.00
R / Rfree (%) 10.2 / 12.2

Other elements in 4kxu:

The structure of Human Transketolase in Covalent Complex with Donor Ketose D-Fructose- 6-Phosphate also contains other interesting chemical elements:

Sodium (Na) 1 atom

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Human Transketolase in Covalent Complex with Donor Ketose D-Fructose- 6-Phosphate (pdb code 4kxu). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Human Transketolase in Covalent Complex with Donor Ketose D-Fructose- 6-Phosphate, PDB code: 4kxu:

Magnesium binding site 1 out of 1 in 4kxu

Go back to Magnesium Binding Sites List in 4kxu
Magnesium binding site 1 out of 1 in the Human Transketolase in Covalent Complex with Donor Ketose D-Fructose- 6-Phosphate


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Human Transketolase in Covalent Complex with Donor Ketose D-Fructose- 6-Phosphate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1006

b:3.8
occ:1.00
 OD1 A:ASP155 2.0 4.6 1.0
O13 A:TDP1015 2.0 4.1 1.0
O21 A:TDP1015 2.1 4.1 1.0
O A:LEU187 2.1 4.6 1.0
OD1 A:ASN185 2.1 4.1 1.0
O A:HOH7009 2.2 4.4 1.0
CG A:ASN185 3.1 4.0 1.0
CG A:ASP155 3.2 4.3 1.0
P2 A:TDP1015 3.2 4.2 1.0
C A:LEU187 3.2 4.3 1.0
P1 A:TDP1015 3.3 4.0 1.0
ND2 A:ASN185 3.4 4.8 1.0
O11 A:TDP1015 3.4 4.1 1.0
O22 A:TDP1015 3.7 5.2 1.0
OD2 A:ASP155 3.9 5.8 1.0
N A:ASP155 4.0 4.3 1.0
N A:LEU187 4.0 4.7 1.0
O5G A:TDP1015 4.1 4.5 1.0
N A:GLY156 4.1 4.1 1.0
N A:GLY188 4.2 4.6 1.0
CA A:LEU187 4.2 4.6 1.0
NZ A:LYS244 4.3 5.2 1.0
CB A:ASP155 4.3 4.7 1.0
O A:ASP183 4.3 4.7 1.0
CA A:GLY188 4.3 4.7 1.0
O12 A:TDP1015 4.4 4.2 1.0
CB A:ASN185 4.4 4.3 1.0
O23 A:TDP1015 4.5 5.1 1.0
CA A:ASP155 4.5 4.0 1.0
N A:ASN185 4.5 4.2 1.0
C A:ASN185 4.7 4.5 1.0
N A:ARG186 4.7 4.4 1.0
CA A:ASN185 4.7 4.6 1.0
CD A:LYS244 4.8 4.6 1.0
C A:ASP155 4.8 4.1 1.0
CB A:LEU187 4.9 4.9 1.0
C A:ARG186 4.9 4.3 1.0
CE A:LYS244 5.0 4.8 1.0
C A:GLY154 5.0 4.7 1.0
CA A:GLY154 5.0 4.8 1.0

Reference:

S.Ludtke, P.Neumann, K.M.Erixon, F.Leeper, R.Kluger, R.Ficner, K.Tittmann. Sub-Angstrom-Resolution Crystallography Reveals Physical Distortions That Enhance Reactivity of A Covalent Enzymatic Intermediate. Nat Chem V. 5 762 2013.
PubMed: 23965678
DOI: 10.1038/NCHEM.1728
Page generated: Mon Aug 11 18:10:43 2025

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