Magnesium in PDB 9fe6: Short-Chain Dehydrogenase/Reductase (Sdr) From Thermus Caliditerrae

The structure of Short-Chain Dehydrogenase/Reductase (Sdr) From Thermus Caliditerrae, PDB code: 9fe6 was solved by B.Kapur, H.Nar, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	98.25 / 1.88
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	56.673, 122.989, 163.347, 90, 90, 90
R / Rfree (%)	21.7 / 24.5

The binding sites of Magnesium atom in the Short-Chain Dehydrogenase/Reductase (Sdr) From Thermus Caliditerrae (pdb code 9fe6). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Short-Chain Dehydrogenase/Reductase (Sdr) From Thermus Caliditerrae, PDB code: 9fe6:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Short-Chain Dehydrogenase/Reductase (Sdr) From Thermus Caliditerrae


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Short-Chain Dehydrogenase/Reductase (Sdr) From Thermus Caliditerrae within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg301 b:54.9 occ:1.00 O A:HOH432 2.1 36.9 1.0 O C:HOH333 2.1 39.9 1.0 O B:HOH409 2.4 46.7 1.0 O A:HOH440 2.8 50.0 1.0 O D:HOH337 2.8 40.2 1.0 O C:HOH312 3.1 68.0 1.0 O D:HOH334 3.6 43.4 1.0 O D:MET259 3.9 29.9 1.0 OXT A:GLY261 4.0 28.6 1.0 O B:HOH435 4.1 32.9 1.0 O B:HOH445 4.3 30.6 1.0 HA D:VAL260 4.3 29.1 1.0 HG13 D:VAL258 4.4 30.8 1.0 O A:GLY261 4.4 30.6 1.0 H D:MET259 4.6 30.6 1.0 O C:GLY261 4.6 29.1 1.0 C A:GLY261 4.7 29.6 1.0 O C:HOH309 4.7 62.5 1.0 OXT C:GLY261 4.8 34.2 1.0 C D:MET259 4.8 29.9 1.0 HG13 B:VAL258 4.9 25.7 1.0 O B:MET259 4.9 22.9 1.0 O A:HOH450 5.0 68.2 1.0

Magnesium binding site 2 out of 2 in the Short-Chain Dehydrogenase/Reductase (Sdr) From Thermus Caliditerrae


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Short-Chain Dehydrogenase/Reductase (Sdr) From Thermus Caliditerrae within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg301 b:50.7 occ:1.00 O C:HOH354 1.9 62.9 1.0 O A:HOH451 1.9 79.7 1.0 O B:HOH414 2.1 40.8 1.0 O D:HOH304 2.6 38.9 1.0 O D:HOH345 2.9 54.1 1.0 O B:HOH467 3.2 52.2 1.0 OXT D:GLY261 3.8 35.5 1.0 O B:GLY261 3.8 28.7 1.0 O A:HOH411 3.9 49.9 1.0 OXT B:GLY261 4.1 31.4 1.0 O D:GLY261 4.2 34.0 1.0 O A:HOH427 4.3 38.0 1.0 C B:GLY261 4.4 28.4 1.0 C D:GLY261 4.4 33.7 1.0 O A:HOH439 4.4 30.8 1.0 O A:MET259 4.5 20.8 1.0 O C:HOH345 4.5 41.0 1.0 HA A:VAL260 4.6 24.8 1.0 O C:MET259 4.6 28.0 1.0 O C:HOH379 4.6 48.3 1.0 O A:HOH450 4.6 68.2 1.0 HA C:VAL260 4.7 27.0 1.0 HG13 A:VAL258 4.8 27.0 1.0 O B:HOH411 4.9 27.6 1.0 HG13 C:VAL258 5.0 29.1 1.0

Y.Sosa, B.Kapur, J.Hurtak, L.Kingsley, H.Wu, S.Gruber, H.Nar, S.Khattabi, J.Moral, M.Lucas, C.Martin, N.Loncar, F.Buono, N.Pefaur, A.E.Nixon, J.Song. In Silico Enzyme Screening Identifies An Sdr Ketoreductase From Thermus Caliditerrae As An Attractive Biocatalyst and Promising Candidate For Protein Engineering Front Chem Biol 2024.