Magnesium in PDB 7dld: Crystal Structures of (S)-Carbonyl Reductases From Candida Parapsilosis in Different Oligomerization States

The structure of Crystal Structures of (S)-Carbonyl Reductases From Candida Parapsilosis in Different Oligomerization States, PDB code: 7dld was solved by Y.H.Li, R.Z.Zhang, F.Forouhar, C.Wang, G.T.Montelione, T.Szyperski, Y.Xu, J.F.Hunt, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	43.22 / 1.75
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	69.262, 114.38, 126.371, 90, 90, 90
R / Rfree (%)	18.8 / 22.9

The binding sites of Magnesium atom in the Crystal Structures of (S)-Carbonyl Reductases From Candida Parapsilosis in Different Oligomerization States (pdb code 7dld). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Crystal Structures of (S)-Carbonyl Reductases From Candida Parapsilosis in Different Oligomerization States, PDB code: 7dld:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Crystal Structures of (S)-Carbonyl Reductases From Candida Parapsilosis in Different Oligomerization States


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structures of (S)-Carbonyl Reductases From Candida Parapsilosis in Different Oligomerization States within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg301 b:29.0 occ:0.50 O A:HOH448 1.9 36.3 0.5 OXT A:PRO279 2.1 31.8 1.0 O A:HOH452 2.2 28.2 1.0 O A:HOH490 2.2 40.1 0.5 C A:PRO279 3.0 35.5 1.0 O A:PRO279 3.2 34.5 1.0 O A:HOH514 3.8 42.9 1.0 CA A:PRO279 4.3 23.6 1.0 CG2 A:ILE177 4.5 24.4 1.0 O A:THR277 4.5 27.9 1.0 O A:HOH447 4.6 16.6 1.0 O A:TYR276 4.7 17.7 1.0 N A:PRO279 4.7 26.9 1.0 C A:THR277 4.9 29.0 1.0 CB A:PRO279 4.9 24.6 1.0

Magnesium binding site 2 out of 2 in the Crystal Structures of (S)-Carbonyl Reductases From Candida Parapsilosis in Different Oligomerization States


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Crystal Structures of (S)-Carbonyl Reductases From Candida Parapsilosis in Different Oligomerization States within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg301 b:33.6 occ:0.50 OXT B:PRO279 2.1 41.6 1.0 O B:HOH492 2.1 38.1 0.5 O B:HOH485 2.2 26.0 1.0 C B:PRO279 3.1 43.0 1.0 O B:PRO279 3.3 45.1 1.0 O B:HOH476 3.9 44.6 1.0 CA B:PRO279 4.5 26.3 1.0 O B:HOH455 4.5 21.4 1.0 CG2 B:ILE177 4.6 21.4 1.0 O B:THR277 4.6 28.3 1.0 O B:TYR276 4.7 21.5 1.0 N B:PRO279 4.8 22.9 1.0 C B:THR277 4.9 26.4 1.0

Y.Li, R.Zhang, C.Wang, F.Forouhar, O.B.Clarke, S.Vorobiev, S.Singh, G.T.Montelione, T.Szyperski, Y.Xu, J.F.Hunt. Oligomeric Interactions Maintain Active-Site Structure in A Noncooperative Enzyme Family. Embo J. V. 41 08368 2022.
ISSN: ESSN 1460-2075
PubMed: 35801308
DOI: 10.15252/EMBJ.2021108368