Magnesium in PDB 5nd5: Crystal Structure of Transketolase From Chlamydomonas Reinhardtii in Complex with Tpp and MG2+

All present enzymatic activity of Crystal Structure of Transketolase From Chlamydomonas Reinhardtii in Complex with Tpp and MG2+:
2.2.1.1;

The structure of Crystal Structure of Transketolase From Chlamydomonas Reinhardtii in Complex with Tpp and MG2+, PDB code: 5nd5 was solved by S.Fermani, M.Zaffagnini, F.Francia, M.Pasquini, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	97.51 / 1.74
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	201.489, 75.930, 103.759, 90.00, 109.99, 90.00
R / Rfree (%)	14.5 / 18.6

The binding sites of Magnesium atom in the Crystal Structure of Transketolase From Chlamydomonas Reinhardtii in Complex with Tpp and MG2+ (pdb code 5nd5). 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 Structure of Transketolase From Chlamydomonas Reinhardtii in Complex with Tpp and MG2+, PDB code: 5nd5:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Crystal Structure of Transketolase From Chlamydomonas Reinhardtii in Complex with Tpp and MG2+


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of Transketolase From Chlamydomonas Reinhardtii in Complex with Tpp and MG2+ within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg800 b:14.6 occ:1.00 O3B A:TPP801 2.0 11.2 1.0 O2A A:TPP801 2.1 12.0 1.0 O A:ILE240 2.1 12.5 1.0 OD2 A:ASP208 2.1 12.8 1.0 O A:HOH1042 2.1 11.4 1.0 OD1 A:ASN238 2.2 11.0 1.0 CG A:ASN238 3.2 13.0 1.0 CG A:ASP208 3.2 12.6 1.0 C A:ILE240 3.3 14.1 1.0 PA A:TPP801 3.3 14.1 1.0 PB A:TPP801 3.3 13.9 1.0 ND2 A:ASN238 3.5 12.4 1.0 O3A A:TPP801 3.6 14.2 1.0 CB A:ASP208 3.7 11.7 1.0 N A:ILE240 3.9 13.5 1.0 N A:ASP208 4.0 10.9 1.0 O1B A:TPP801 4.0 15.2 1.0 CA A:ILE240 4.1 14.1 1.0 O A:HOH1032 4.2 13.7 1.0 O7 A:TPP801 4.2 17.0 1.0 N A:SER241 4.3 13.6 1.0 OD1 A:ASP208 4.3 12.5 1.0 O A:ASP236 4.4 13.4 1.0 O1A A:TPP801 4.4 15.2 1.0 CA A:ASP208 4.5 10.7 1.0 O2B A:TPP801 4.5 17.0 1.0 CB A:ILE240 4.5 15.8 1.0 CA A:SER241 4.5 14.3 1.0 CB A:ASN238 4.5 13.4 1.0 N A:ASN238 4.7 11.9 1.0 N A:LYS239 4.8 14.2 1.0 C A:ASN238 4.9 13.6 1.0 CA A:ASN238 4.9 13.6 1.0 CB A:SER241 4.9 13.8 1.0 CG2 A:ILE240 5.0 16.5 1.0

Magnesium binding site 2 out of 2 in the Crystal Structure of Transketolase From Chlamydomonas Reinhardtii in Complex with Tpp and MG2+


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Crystal Structure of Transketolase From Chlamydomonas Reinhardtii in Complex with Tpp and MG2+ within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg800 b:13.5 occ:1.00 OD2 B:ASP208 2.0 11.0 1.0 O2B B:TPP801 2.0 13.3 1.0 O2A B:TPP801 2.1 14.8 1.0 O B:ILE240 2.1 14.1 1.0 O B:HOH1074 2.2 12.9 1.0 OD1 B:ASN238 2.2 12.8 1.0 CG B:ASP208 3.1 12.5 1.0 CG B:ASN238 3.1 13.6 1.0 PA B:TPP801 3.3 16.1 1.0 C B:ILE240 3.3 14.3 1.0 PB B:TPP801 3.3 15.9 1.0 ND2 B:ASN238 3.4 14.4 1.0 O3A B:TPP801 3.6 15.7 1.0 CB B:ASP208 3.6 11.9 1.0 N B:ILE240 3.9 14.2 1.0 N B:ASP208 3.9 10.9 1.0 O3B B:TPP801 4.1 17.6 1.0 CA B:ILE240 4.1 14.7 1.0 OD1 B:ASP208 4.2 13.3 1.0 O B:HOH1018 4.2 15.8 1.0 O7 B:TPP801 4.3 18.1 1.0 N B:SER241 4.3 14.1 1.0 O1A B:TPP801 4.4 18.2 1.0 O B:ASP236 4.4 12.3 1.0 CA B:ASP208 4.4 11.2 1.0 O1B B:TPP801 4.5 16.5 1.0 CB B:ASN238 4.5 12.3 1.0 CA B:SER241 4.5 14.2 1.0 CB B:ILE240 4.6 17.4 1.0 N B:ASN238 4.8 12.2 1.0 N B:LYS239 4.8 15.4 1.0 C B:ASN238 4.9 14.3 1.0 CA B:ASN238 4.9 12.4 1.0 CB B:SER241 4.9 14.2 1.0 CG2 B:ILE240 5.0 17.1 1.0

M.Pasquini, S.Fermani, D.Tedesco, C.Sciabolini, P.Crozet, M.Naldi, J.Henri, U.Vothknecht, C.Bertucci, S.D.Lemaire, M.Zaffagnini, F.Francia. Structural Basis For the Magnesium-Dependent Activation of Transketolase From Chlamydomonas Reinhardtii. Biochim. Biophys. Acta V.1861 2132 2017.
ISSN: ISSN 0006-3002
PubMed: 28552632
DOI: 10.1016/J.BBAGEN.2017.05.021