Magnesium in PDB 6had: Human Transketolase Variant E160Q

All present enzymatic activity of Human Transketolase Variant E160Q:
2.2.1.1;

The structure of Human Transketolase Variant E160Q, PDB code: 6had was solved by S.Dai, V.Sautner, K.Tittmann, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	42.75 / 1.04
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	115.710, 85.490, 73.610, 90.00, 127.85, 90.00
R / Rfree (%)	11.1 / 13

The structure of Human Transketolase Variant E160Q also contains other interesting chemical elements:

Calcium	(Ca)	1 atom
Sodium	(Na)	1 atom

The binding sites of Magnesium atom in the Human Transketolase Variant E160Q (pdb code 6had). 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 Variant E160Q, PDB code: 6had:

Magnesium binding site 1 out of 1 in the Human Transketolase Variant E160Q


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Human Transketolase Variant E160Q within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg703 b:11.3 occ:0.24 CA A:CA702 0.1 9.0 0.8 OD1 A:ASP155 2.1 10.8 1.0 O12 A:TDP704 2.1 10.1 1.0 O A:LEU187 2.2 11.4 1.0 O23 A:TDP704 2.3 9.0 1.0 OD1 A:ASN185 2.3 9.7 1.0 O A:HOH926 2.4 10.0 1.0 H A:GLY156 3.2 11.8 1.0 CG A:ASN185 3.3 8.9 1.0 H A:ASP155 3.3 11.1 1.0 CG A:ASP155 3.3 10.2 1.0 HD21 A:ASN185 3.3 11.7 1.0 C A:LEU187 3.3 10.7 1.0 P1 A:TDP704 3.3 9.6 1.0 P2 A:TDP704 3.4 9.0 1.0 HZ2 A:LYS244 3.5 11.7 1.0 H A:LEU187 3.5 12.2 1.0 O11 A:TDP704 3.6 9.3 1.0 HA2 A:GLY188 3.6 12.8 1.0 ND2 A:ASN185 3.7 9.7 1.0 H A:ASN185 3.9 11.4 1.0 O21 A:TDP704 3.9 10.8 1.0 HD2 A:LYS244 3.9 11.7 1.0 OD2 A:ASP155 3.9 11.7 1.0 N A:LEU187 4.0 10.2 1.0 N A:ASP155 4.0 9.2 1.0 N A:GLY156 4.1 9.8 1.0 O5G A:TDP704 4.1 11.5 1.0 N A:GLY188 4.2 10.7 1.0 CA A:LEU187 4.2 10.0 1.0 CA A:GLY188 4.3 10.6 1.0 HB2 A:ALA193 4.4 15.1 1.0 NZ A:LYS244 4.4 9.8 1.0 CB A:ASP155 4.4 9.6 1.0 O13 A:TDP704 4.5 10.3 1.0 HD22 A:ASN185 4.5 11.7 1.0 O A:ASP183 4.5 10.0 1.0 H A:ARG186 4.5 11.4 1.0 CA A:ASP155 4.5 9.6 1.0 CB A:ASN185 4.6 9.7 1.0 N A:ASN185 4.6 9.5 1.0 HB2 A:LEU187 4.6 13.3 1.0 HZ3 A:LYS244 4.6 11.7 1.0 N A:ARG186 4.6 9.5 1.0 C A:ASN185 4.6 9.6 1.0 O22 A:TDP704 4.7 10.5 1.0 HA3 A:GLY154 4.7 11.7 1.0 HA3 A:GLY156 4.7 11.6 1.0 C A:ASP155 4.8 9.2 1.0 CA A:ASN185 4.8 9.4 1.0 CD A:LYS244 4.8 9.7 1.0 C A:ARG186 4.8 9.8 1.0 HA2 A:GLY154 4.9 11.7 1.0 HZ1 A:LYS244 4.9 11.7 1.0 HB3 A:ASP155 4.9 11.6 1.0 HA3 A:GLY188 5.0 12.8 1.0 HA A:LEU187 5.0 12.0 1.0 H A:GLY188 5.0 12.8 1.0 CA A:GLY156 5.0 9.6 1.0

S.Dai, L.M.Funk, F.R.Von Pappenheim, V.Sautner, M.Paulikat, B.Schroder, J.Uranga, R.A.Mata, K.Tittmann. Low-Barrier Hydrogen Bonds in Enzyme Cooperativity. Nature V. 573 609 2019.
ISSN: ESSN 1476-4687
PubMed: 31534226
DOI: 10.1038/S41586-019-1581-9