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Magnesium in PDB 2ps1: S. Cerevisiae Orotate Phosphoribosyltransferase Complexed with Orotic Acid and Prpp

Enzymatic activity of S. Cerevisiae Orotate Phosphoribosyltransferase Complexed with Orotic Acid and Prpp

All present enzymatic activity of S. Cerevisiae Orotate Phosphoribosyltransferase Complexed with Orotic Acid and Prpp:
2.4.2.10;

Protein crystallography data

The structure of S. Cerevisiae Orotate Phosphoribosyltransferase Complexed with Orotic Acid and Prpp, PDB code: 2ps1 was solved by L.Gonzalez-Segura, T.D.Hurley, R.W.Mcclard, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 49.94 / 1.75
Space group P 1
Cell size a, b, c (Å), α, β, γ (°) 41.788, 50.051, 50.078, 90.59, 105.88, 92.99
R / Rfree (%) 19.4 / 21.7

Magnesium Binding Sites:

The binding sites of Magnesium atom in the S. Cerevisiae Orotate Phosphoribosyltransferase Complexed with Orotic Acid and Prpp (pdb code 2ps1). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the S. Cerevisiae Orotate Phosphoribosyltransferase Complexed with Orotic Acid and Prpp, PDB code: 2ps1:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 2ps1

Go back to Magnesium Binding Sites List in 2ps1
Magnesium binding site 1 out of 2 in the S. Cerevisiae Orotate Phosphoribosyltransferase Complexed with Orotic Acid and Prpp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of S. Cerevisiae Orotate Phosphoribosyltransferase Complexed with Orotic Acid and Prpp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg401

b:19.4
occ:1.00
O A:HOH834 2.2 20.1 1.0
O A:HOH721 2.2 21.8 1.0
O3B A:PRP700 2.3 17.3 1.0
O2 A:PRP700 2.5 16.9 1.0
O1 A:PRP700 2.5 17.1 1.0
O3 A:PRP700 2.6 17.2 1.0
C2 A:PRP700 3.3 16.7 1.0
PA A:PRP700 3.4 16.9 1.0
C1 A:PRP700 3.5 16.5 1.0
C3 A:PRP700 3.5 16.6 1.0
PB A:PRP700 3.5 17.6 1.0
O1A A:PRP700 3.6 16.8 1.0
O3A A:PRP700 3.6 17.4 1.0
O A:ALA74 3.8 14.6 1.0
OD1 A:ASP131 4.0 18.9 1.0
N A:TYR75 4.0 14.1 1.0
CB A:LYS76 4.2 15.3 1.0
N A:LYS76 4.2 14.4 1.0
C A:ALA74 4.3 14.1 1.0
OD2 A:ASP131 4.3 19.2 1.0
C4 A:PRP700 4.3 16.1 1.0
O4 A:PRP700 4.4 16.9 1.0
O A:HOH789 4.4 26.7 1.0
OD1 A:ASP132 4.4 17.4 1.0
O2B A:PRP700 4.5 17.7 1.0
O1B A:PRP700 4.6 16.5 1.0
CG A:ASP131 4.6 17.5 1.0
O A:HOH702 4.6 21.2 1.0
O A:PRO73 4.8 13.9 1.0
CA A:LYS76 4.8 15.0 1.0
O2A A:PRP700 4.8 16.5 1.0

Magnesium binding site 2 out of 2 in 2ps1

Go back to Magnesium Binding Sites List in 2ps1
Magnesium binding site 2 out of 2 in the S. Cerevisiae Orotate Phosphoribosyltransferase Complexed with Orotic Acid and Prpp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of S. Cerevisiae Orotate Phosphoribosyltransferase Complexed with Orotic Acid and Prpp within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg402

b:20.1
occ:1.00
O B:HOH877 2.3 15.0 1.0
O3B B:PRP800 2.3 17.4 1.0
O B:HOH833 2.4 20.7 1.0
O2 B:PRP800 2.5 15.2 1.0
O1 B:PRP800 2.5 17.1 1.0
O3 B:PRP800 2.6 16.1 1.0
C2 B:PRP800 3.2 15.9 1.0
PA B:PRP800 3.4 17.6 1.0
C1 B:PRP800 3.5 16.2 1.0
C3 B:PRP800 3.5 15.9 1.0
PB B:PRP800 3.5 16.1 1.0
O3A B:PRP800 3.5 17.2 1.0
O1A B:PRP800 3.6 16.5 1.0
O B:ALA74 3.9 14.6 1.0
OD1 B:ASP131 4.0 18.2 1.0
N B:TYR75 4.0 14.1 1.0
N B:LYS76 4.2 14.0 1.0
CB B:LYS76 4.2 14.5 1.0
C B:ALA74 4.3 14.3 1.0
C4 B:PRP800 4.3 15.7 1.0
OD1 B:ASP132 4.4 17.6 1.0
OD2 B:ASP131 4.4 19.0 1.0
CG B:LYS76 4.4 15.0 1.0
O4 B:PRP800 4.4 16.8 1.0
O2B B:PRP800 4.5 17.4 1.0
O1B B:PRP800 4.5 17.3 1.0
O A:HOH713 4.5 17.8 1.0
O B:HOH914 4.6 28.8 1.0
CG B:ASP131 4.6 16.8 1.0
O2A B:PRP800 4.8 17.1 1.0
CA B:LYS76 4.8 14.3 1.0
O B:PRO73 4.8 13.4 1.0
O B:HOH834 4.8 30.0 1.0
OD2 B:ASP132 4.9 18.0 1.0

Reference:

L.Gonzalez-Segura, J.F.Witte, R.W.Mcclard, T.D.Hurley. Ternary Complex Formation and Induced Asymmetry in Orotate Phosphoribosyltransferase. Biochemistry V. 46 14075 2007.
ISSN: ISSN 0006-2960
PubMed: 18020427
DOI: 10.1021/BI701023Z
Page generated: Mon Dec 14 07:35:04 2020

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