Manganese in PDB 5jsx: Crystal Structure of Glucosyl-3-Phosphoglycerate Synthase From Mycobacterium Tuberculosis in Complex with MN2+ and Uridine- Diphosphate-Glucose (Udp-Glc)

The structure of Crystal Structure of Glucosyl-3-Phosphoglycerate Synthase From Mycobacterium Tuberculosis in Complex with MN2+ and Uridine- Diphosphate-Glucose (Udp-Glc), PDB code: 5jsx was solved by D.Albesa-Jove, E.Sancho-Vaello, A.Rodrigo-Unzueta, N.Comino, A.Carreras-Gonzalez, P.Arrasate, S.Urresti, M.E.Guerin, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	41.76 / 2.81
Space group	I 41
Cell size a, b, c (Å), α, β, γ (°)	98.780, 98.780, 127.920, 90.00, 90.00, 90.00
R / Rfree (%)	19 / 21.7

The binding sites of Manganese atom in the Crystal Structure of Glucosyl-3-Phosphoglycerate Synthase From Mycobacterium Tuberculosis in Complex with MN2+ and Uridine- Diphosphate-Glucose (Udp-Glc) (pdb code 5jsx). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total only one binding site of Manganese was determined in the Crystal Structure of Glucosyl-3-Phosphoglycerate Synthase From Mycobacterium Tuberculosis in Complex with MN2+ and Uridine- Diphosphate-Glucose (Udp-Glc), PDB code: 5jsx:

Manganese binding site 1 out of 1 in the Crystal Structure of Glucosyl-3-Phosphoglycerate Synthase From Mycobacterium Tuberculosis in Complex with MN2+ and Uridine- Diphosphate-Glucose (Udp-Glc)


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Crystal Structure of Glucosyl-3-Phosphoglycerate Synthase From Mycobacterium Tuberculosis in Complex with MN2+ and Uridine- Diphosphate-Glucose (Udp-Glc) within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn401 b:61.6 occ:1.00 O2B A:UPG402 2.1 64.2 1.0 O A:HOH501 2.1 54.2 1.0 O A:HOH509 2.2 73.2 1.0 O1A A:UPG402 2.2 63.4 1.0 OD2 A:ASP136 2.2 58.9 1.0 ND1 A:HIS258 2.4 70.2 1.0 CE1 A:HIS258 3.1 68.9 1.0 CG A:ASP136 3.2 57.0 1.0 PB A:UPG402 3.3 62.3 1.0 CG A:HIS258 3.3 70.5 1.0 PA A:UPG402 3.4 57.6 1.0 OD1 A:ASP136 3.4 55.4 1.0 O2' A:UPG402 3.6 62.1 1.0 O3A A:UPG402 3.6 64.7 1.0 CB A:HIS258 3.7 66.6 1.0 O1B A:UPG402 4.1 62.9 1.0 NE2 A:HIS258 4.2 71.6 1.0 O A:ARG259 4.3 69.3 1.0 CD2 A:HIS258 4.3 73.2 1.0 O2A A:UPG402 4.4 54.7 1.0 N A:ARG259 4.4 62.6 1.0 C5C A:UPG402 4.4 56.0 1.0 O5C A:UPG402 4.5 55.2 1.0 O3B A:UPG402 4.5 61.0 1.0 CB A:ASP136 4.6 57.8 1.0 NH2 A:ARG259 4.6 54.0 0.5 OD2 A:ASP134 4.7 64.6 1.0 NH1 A:ARG259 4.7 60.7 0.5 C2' A:UPG402 4.8 63.1 1.0 CB A:ARG259 4.8 61.7 0.5 CB A:ARG259 4.8 61.6 0.5 CZ A:ARG259 4.8 58.9 0.5 NH2 A:ARG256 4.9 81.1 1.0 C1' A:UPG402 4.9 63.8 1.0 O A:HOH523 4.9 82.3 1.0 CA A:ARG259 5.0 62.1 0.5 CA A:HIS258 5.0 65.8 1.0 CA A:ARG259 5.0 62.1 0.5

D.Albesa-Jove, J.Romero-Garcia, E.Sancho-Vaello, F.X.Contreras, A.Rodrigo-Unzueta, N.Comino, A.Carreras-Gonzalez, P.Arrasate, S.Urresti, X.Biarnes, A.Planas, M.E.Guerin. Structural Snapshots and Loop Dynamics Along the Catalytic Cycle of Glycosyltransferase Gpgs. Structure V. 25 1034 2017.
ISSN: ISSN 1878-4186
PubMed: 28625787
DOI: 10.1016/J.STR.2017.05.009