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Magnesium in PDB 1opr: The Crystal Structure of the Orotate Phosphoribosyltransferase Complexed with Orotate and Alpha-D-5-Phosphoribosyl-1-Pyrophosphate

Enzymatic activity of The Crystal Structure of the Orotate Phosphoribosyltransferase Complexed with Orotate and Alpha-D-5-Phosphoribosyl-1-Pyrophosphate

All present enzymatic activity of The Crystal Structure of the Orotate Phosphoribosyltransferase Complexed with Orotate and Alpha-D-5-Phosphoribosyl-1-Pyrophosphate:
2.4.2.10;

Protein crystallography data

The structure of The Crystal Structure of the Orotate Phosphoribosyltransferase Complexed with Orotate and Alpha-D-5-Phosphoribosyl-1-Pyrophosphate, PDB code: 1opr was solved by G.Scapin, J.C.Sacchettini, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 15.00 / 2.30
Space group P 41 21 2
Cell size a, b, c (Å), α, β, γ (°) 47.300, 47.300, 216.600, 90.00, 90.00, 90.00
R / Rfree (%) n/a / n/a

Magnesium Binding Sites:

The binding sites of Magnesium atom in the The Crystal Structure of the Orotate Phosphoribosyltransferase Complexed with Orotate and Alpha-D-5-Phosphoribosyl-1-Pyrophosphate (pdb code 1opr). 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 The Crystal Structure of the Orotate Phosphoribosyltransferase Complexed with Orotate and Alpha-D-5-Phosphoribosyl-1-Pyrophosphate, PDB code: 1opr:

Magnesium binding site 1 out of 1 in 1opr

Go back to Magnesium Binding Sites List in 1opr
Magnesium binding site 1 out of 1 in the The Crystal Structure of the Orotate Phosphoribosyltransferase Complexed with Orotate and Alpha-D-5-Phosphoribosyl-1-Pyrophosphate


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of The Crystal Structure of the Orotate Phosphoribosyltransferase Complexed with Orotate and Alpha-D-5-Phosphoribosyl-1-Pyrophosphate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg300

b:28.2
occ:1.00
 O2 A:PRP221 2.5 34.2 1.0
O A:HOH561 2.6 30.8 0.7
O3A A:PRP221 2.6 40.3 1.0
O3 A:PRP221 2.8 38.0 1.0
O1 A:PRP221 2.9 39.9 1.0
O3B A:PRP221 2.9 36.2 1.0
PA A:PRP221 3.1 41.3 1.0
PB A:PRP221 3.3 38.6 1.0
C2 A:PRP221 3.5 36.2 1.0
O1A A:PRP221 3.6 42.4 1.0
C3 A:PRP221 3.6 37.0 1.0
C1 A:PRP221 3.7 37.8 1.0
CB A:ALA71 3.8 40.2 1.0
N A:LYS73 3.8 33.6 1.0
CB A:LYS73 4.1 37.1 1.0
O2B A:PRP221 4.2 40.0 1.0
C4 A:PRP221 4.2 36.5 1.0
CA A:LYS73 4.3 34.0 1.0
OD1 A:ASP124 4.3 42.7 1.0
N A:TYR72 4.4 32.2 1.0
O1B A:PRP221 4.5 37.4 1.0
O2A A:PRP221 4.5 41.6 1.0
O4 A:PRP221 4.6 37.6 1.0
OD2 A:ASP124 4.7 42.5 1.0
O A:PRO70 4.8 33.3 1.0
CA A:ALA71 4.9 38.7 1.0
C A:TYR72 4.9 33.0 1.0
NZ A:LYS73 4.9 43.2 1.0
CG A:ASP124 5.0 41.4 1.0
N A:GLY74 5.0 28.9 1.0

Reference:

G.Scapin, D.H.Ozturk, C.Grubmeyer, J.C.Sacchettini. The Crystal Structure of the Orotate Phosphoribosyltransferase Complexed with Orotate and Alpha-D-5-Phosphoribosyl-1-Pyrophosphate. Biochemistry V. 34 10744 1995.
ISSN: ISSN 0006-2960
PubMed: 7545004
DOI: 10.1021/BI00034A006
Page generated: Tue Aug 13 10:41:45 2024

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