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Manganese in PDB 4dec: Crystal Structure of Glucosyl-3-Phosphoglycerate Synthase From Mycobacterium Tuberculosis in Complex with MN2+, Uridine-Diphosphate (Udp) and Phosphoglyceric Acid (Pga)

Protein crystallography data

The structure of Crystal Structure of Glucosyl-3-Phosphoglycerate Synthase From Mycobacterium Tuberculosis in Complex with MN2+, Uridine-Diphosphate (Udp) and Phosphoglyceric Acid (Pga), PDB code: 4dec was solved by D.Albesa-Jove, S.Urresti, M.Van Der Woerd, M.E.Guerin, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 39.36 / 1.98
Space group I 41
Cell size a, b, c (Å), α, β, γ (°) 100.316, 100.316, 127.026, 90.00, 90.00, 90.00
R / Rfree (%) 17.7 / 20.5

Manganese Binding Sites:

The binding sites of Manganese atom in the Crystal Structure of Glucosyl-3-Phosphoglycerate Synthase From Mycobacterium Tuberculosis in Complex with MN2+, Uridine-Diphosphate (Udp) and Phosphoglyceric Acid (Pga) (pdb code 4dec). 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+, Uridine-Diphosphate (Udp) and Phosphoglyceric Acid (Pga), PDB code: 4dec:

Manganese binding site 1 out of 1 in 4dec

Go back to Manganese Binding Sites List in 4dec
Manganese binding site 1 out of 1 in the Crystal Structure of Glucosyl-3-Phosphoglycerate Synthase From Mycobacterium Tuberculosis in Complex with MN2+, Uridine-Diphosphate (Udp) and Phosphoglyceric Acid (Pga)


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+, Uridine-Diphosphate (Udp) and Phosphoglyceric Acid (Pga) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn402

b:53.9
occ:1.00
OD2 A:ASP136 2.4 51.3 1.0
O A:HOH501 2.7 44.8 1.0
ND1 A:HIS258 2.8 68.5 1.0
O A:HOH713 3.0 63.1 1.0
CE1 A:HIS258 3.2 64.3 1.0
O A:HOH697 3.3 65.8 1.0
CG A:ASP136 3.3 40.3 1.0
O1A A:UDP401 3.4 58.0 1.0
O3A A:UDP401 3.4 76.7 1.0
CG A:HIS258 3.5 60.9 1.0
OD1 A:ASP136 3.5 36.9 1.0
NE2 A:HIS258 3.9 74.9 1.0
PA A:UDP401 4.0 53.6 1.0
CD2 A:HIS258 4.0 66.8 1.0
CB A:HIS258 4.1 59.5 1.0
O A:ARG259 4.3 66.3 1.0
O3B A:UDP401 4.5 74.5 1.0
PB A:UDP401 4.5 72.0 1.0
C5' A:UDP401 4.6 32.2 1.0
OD2 A:ASP134 4.6 35.6 1.0
CB A:ASP136 4.7 34.6 1.0
O5' A:UDP401 4.8 49.6 1.0
NH2 A:ARG256 4.9 75.1 1.0

Reference:

S.Urresti, D.Albesa-Jove, F.Schaeffer, H.T.Pham, D.Kaur, P.Gest, M.J.Van Der Woerd, A.Carreras-Gonzalez, S.Lopez-Fernandez, P.M.Alzari, P.J.Brennan, M.Jackson, M.E.Guerin. Mechanistic Insights Into the Retaining Glucosyl-3-Phosphoglycerate Synthase From Mycobacteria. J.Biol.Chem. V. 287 24649 2012.
ISSN: ISSN 0021-9258
PubMed: 22637481
DOI: 10.1074/JBC.M112.368191
Page generated: Tue Dec 15 04:19:12 2020

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