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Magnesium in PDB 1vst: Symmetric Sulfolobus Solfataricus Uracil Phosphoribosyltransferase with Bound Prpp and Gtp

Enzymatic activity of Symmetric Sulfolobus Solfataricus Uracil Phosphoribosyltransferase with Bound Prpp and Gtp

All present enzymatic activity of Symmetric Sulfolobus Solfataricus Uracil Phosphoribosyltransferase with Bound Prpp and Gtp:
2.4.2.9;

Protein crystallography data

The structure of Symmetric Sulfolobus Solfataricus Uracil Phosphoribosyltransferase with Bound Prpp and Gtp, PDB code: 1vst was solved by A.Kadziola, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 25.00 / 2.80
Space group P 64 2 2
Cell size a, b, c (Å), α, β, γ (°) 122.200, 122.200, 62.200, 90.00, 90.00, 120.00
R / Rfree (%) 22.6 / 27.7

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Symmetric Sulfolobus Solfataricus Uracil Phosphoribosyltransferase with Bound Prpp and Gtp (pdb code 1vst). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Symmetric Sulfolobus Solfataricus Uracil Phosphoribosyltransferase with Bound Prpp and Gtp, PDB code: 1vst:

Magnesium binding site 1 out of 1 in 1vst

Go back to Magnesium Binding Sites List in 1vst
Magnesium binding site 1 out of 1 in the Symmetric Sulfolobus Solfataricus Uracil Phosphoribosyltransferase with Bound Prpp and Gtp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Symmetric Sulfolobus Solfataricus Uracil Phosphoribosyltransferase with Bound Prpp and Gtp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg302

b:11.4
occ:0.50
O1A A:GTP301 2.1 22.4 1.0
O1B A:GTP301 2.1 21.1 1.0
PA A:GTP301 3.4 23.4 1.0
PB A:GTP301 3.4 21.1 1.0
O2G A:GTP301 3.6 24.7 1.0
O3A A:GTP301 3.7 22.7 1.0
O5' A:GTP301 4.0 25.5 1.0
C8 A:GTP301 4.1 25.8 1.0
N7 A:GTP301 4.2 26.0 1.0
CE A:LYS30 4.3 13.4 1.0
O2B A:GTP301 4.4 25.4 1.0
O3B A:GTP301 4.4 23.1 1.0
NZ A:LYS30 4.5 11.9 1.0
O2A A:GTP301 4.6 24.6 1.0
PG A:GTP301 4.6 21.5 1.0

Reference:

S.Christoffersen, A.Kadziola, E.Johansson, M.Rasmussen, M.Willemoes, K.F.Jensen. Structural and Kinetic Studies of the Allosteric Transition in Sulfolobus Solfataricus Uracil Phosphoribosyltransferase: Permanent Activation By Engineering of the C-Terminus J.Mol.Biol. V. 393 464 2009.
ISSN: ISSN 0022-2836
PubMed: 19683539
DOI: 10.1016/J.JMB.2009.08.019
Page generated: Tue Aug 13 16:27:02 2024

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