Magnesium in PDB 1ek6: Structure of Human Udp-Galactose 4-Epimerase Complexed with Nadh and Udp-Glucose

All present enzymatic activity of Structure of Human Udp-Galactose 4-Epimerase Complexed with Nadh and Udp-Glucose:
5.1.3.2;

The structure of Structure of Human Udp-Galactose 4-Epimerase Complexed with Nadh and Udp-Glucose, PDB code: 1ek6 was solved by J.B.Thoden, T.M.Wohlers, J.L.Fridovich-Keil, H.M.Holden, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.00 / 1.50
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	74.700, 86.900, 95.300, 90.00, 90.00, 90.00
R / Rfree (%)	n/a / n/a

The binding sites of Magnesium atom in the Structure of Human Udp-Galactose 4-Epimerase Complexed with Nadh and Udp-Glucose (pdb code 1ek6). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Structure of Human Udp-Galactose 4-Epimerase Complexed with Nadh and Udp-Glucose, PDB code: 1ek6:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Structure of Human Udp-Galactose 4-Epimerase Complexed with Nadh and Udp-Glucose


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of Human Udp-Galactose 4-Epimerase Complexed with Nadh and Udp-Glucose within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg961 b:19.1 occ:1.00 O A:HOH1943 1.9 25.5 1.0 O A:HOH1942 2.0 21.0 1.0 O A:HOH1945 2.0 18.9 1.0 O A:HOH1944 2.1 31.1 1.0 O A:HOH1143 2.2 19.8 1.0 O A:HOH1484 2.3 28.0 1.0 O A:HOH1674 4.0 23.1 1.0 O A:HOH1421 4.1 23.1 1.0 O A:HOH1372 4.1 20.2 1.0 OE1 A:GLU285 4.3 17.6 1.0 OE2 A:GLU285 4.4 14.2 1.0 CD A:LYS291 4.5 28.6 1.0 CG A:LYS291 4.7 23.9 1.0 CD A:GLU285 4.8 20.2 1.0

Magnesium binding site 2 out of 2 in the Structure of Human Udp-Galactose 4-Epimerase Complexed with Nadh and Udp-Glucose


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Structure of Human Udp-Galactose 4-Epimerase Complexed with Nadh and Udp-Glucose within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg960 b:34.1 occ:1.00 O B:HOH1286 2.0 17.7 1.0 O A:HOH1546 2.1 32.7 1.0 O B:HOH1795 2.1 26.3 1.0 O A:HOH1803 2.2 38.3 1.0 O A:HOH1635 2.3 29.6 1.0 O A:GLN173 4.0 18.8 1.0 OE2 B:GLU301 4.2 25.2 1.0 O A:HOH1412 4.2 29.9 1.0 OE1 B:GLU301 4.2 27.3 1.0 OE1 B:GLN99 4.2 23.9 1.0 O A:ALA174 4.2 24.9 1.0 OE1 A:GLN173 4.4 99.6 1.0 NE2 B:GLN99 4.5 27.7 1.0 CD B:GLU301 4.6 95.5 1.0 CD B:GLN99 4.8 18.2 1.0 C A:ALA174 5.0 19.8 1.0

J.B.Thoden, T.M.Wohlers, J.L.Fridovich-Keil, H.M.Holden. Crystallographic Evidence For Tyr 157 Functioning As the Active Site Base in Human Udp-Galactose 4-Epimerase. Biochemistry V. 39 5691 2000.
ISSN: ISSN 0006-2960
PubMed: 10801319
DOI: 10.1021/BI000215L