Magnesium in PDB 1syl: Crystal Structure of Inactive Mutant Dutpase Complexed with Substrate Dutp

All present enzymatic activity of Crystal Structure of Inactive Mutant Dutpase Complexed with Substrate Dutp:
3.6.1.23;

The structure of Crystal Structure of Inactive Mutant Dutpase Complexed with Substrate Dutp, PDB code: 1syl was solved by O.Barabas, J.Kovari, V.Pongracz, M.Wilmanns, B.G.Vertessy, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 1.95
Space group	P 63 2 2
Cell size a, b, c (Å), α, β, γ (°)	76.421, 76.421, 100.259, 90.00, 90.00, 120.00
R / Rfree (%)	15.8 / 18.9

The binding sites of Magnesium atom in the Crystal Structure of Inactive Mutant Dutpase Complexed with Substrate Dutp (pdb code 1syl). 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 Crystal Structure of Inactive Mutant Dutpase Complexed with Substrate Dutp, PDB code: 1syl:

Magnesium binding site 1 out of 1 in the Crystal Structure of Inactive Mutant Dutpase Complexed with Substrate Dutp


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 Inactive Mutant Dutpase Complexed with Substrate Dutp within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg997 b:32.5 occ:1.00 O A:HOH1010 2.0 26.4 1.0 O1A A:DUT777 2.1 34.5 1.0 O1B A:DUT777 2.1 31.0 1.0 O A:HOH1083 2.1 32.4 1.0 O A:HOH1033 2.2 31.9 1.0 O2G A:DUT777 2.2 33.2 1.0 PB A:DUT777 3.3 31.2 1.0 PA A:DUT777 3.3 29.8 1.0 PG A:DUT777 3.4 37.6 1.0 O3A A:DUT777 3.6 31.9 1.0 O3B A:DUT777 3.7 39.7 1.0 O1G A:DUT777 3.9 38.8 1.0 O A:HOH1012 4.2 35.1 1.0 O A:HOH1025 4.2 32.9 1.0 O2A A:DUT777 4.3 34.0 1.0 O5' A:DUT777 4.4 25.9 1.0 C5' A:DUT777 4.5 28.2 1.0 O3G A:DUT777 4.6 37.4 1.0 O2B A:DUT777 4.6 25.8 1.0 ND2 A:ASN90 4.7 32.8 1.0 O A:HOH1095 4.7 55.3 1.0

O.Barabas, V.Pongracz, J.Kovari, M.Wilmanns, B.G.Vertessy. Structural Insights Into the Catalytic Mechanism of Phosphate Ester Hydrolysis By Dutpase J.Biol.Chem. V. 279 42907 2004.
ISSN: ISSN 0021-9258
PubMed: 15208312
DOI: 10.1074/JBC.M406135200