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Magnesium in PDB 1l1r: Crystal Structure of Aprtase From Giardia Lamblia Complexed with 9- Deazaadenine, MG2+ and Prpp

Enzymatic activity of Crystal Structure of Aprtase From Giardia Lamblia Complexed with 9- Deazaadenine, MG2+ and Prpp

All present enzymatic activity of Crystal Structure of Aprtase From Giardia Lamblia Complexed with 9- Deazaadenine, MG2+ and Prpp:
2.4.2.7;

Protein crystallography data

The structure of Crystal Structure of Aprtase From Giardia Lamblia Complexed with 9- Deazaadenine, MG2+ and Prpp, PDB code: 1l1r was solved by W.Shi, A.E.Sarver, C.C.Wang, K.S.Tanaka, S.C.Almo, V.L.Schramm, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 25.00 / 1.95
Space group P 31 2 1
Cell size a, b, c (Å), α, β, γ (°) 54.325, 54.325, 108.744, 90.00, 90.00, 120.00
R / Rfree (%) 21.8 / 26.2

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Aprtase From Giardia Lamblia Complexed with 9- Deazaadenine, MG2+ and Prpp (pdb code 1l1r). 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 Aprtase From Giardia Lamblia Complexed with 9- Deazaadenine, MG2+ and Prpp, PDB code: 1l1r:

Magnesium binding site 1 out of 1 in 1l1r

Go back to Magnesium Binding Sites List in 1l1r
Magnesium binding site 1 out of 1 in the Crystal Structure of Aprtase From Giardia Lamblia Complexed with 9- Deazaadenine, MG2+ and Prpp


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 Aprtase From Giardia Lamblia Complexed with 9- Deazaadenine, MG2+ and Prpp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg400

b:25.6
occ:1.00
 O A:HOH463 2.1 22.8 1.0
O A:HOH464 2.1 26.3 1.0
O3B A:PRP301 2.2 36.7 1.0
O1 A:PRP301 2.3 35.3 1.0
O3 A:PRP301 2.5 29.9 1.0
O2 A:PRP301 2.5 32.1 1.0
O3A A:PRP301 3.0 36.9 1.0
PB A:PRP301 3.2 38.5 1.0
C2 A:PRP301 3.2 33.9 1.0
PA A:PRP301 3.3 39.4 1.0
C1 A:PRP301 3.3 34.2 1.0
C3 A:PRP301 3.4 33.4 1.0
O A:GLU61 3.5 26.6 1.0
N A:SER62 3.8 29.5 1.0
OD1 A:ASP124 3.9 24.3 1.0
O1A A:PRP301 4.0 37.0 1.0
C A:GLU61 4.0 26.9 1.0
O1B A:PRP301 4.1 38.2 1.0
O4 A:PRP301 4.2 36.4 1.0
OD2 A:ASP124 4.2 23.2 1.0
N A:ARG63 4.3 20.3 1.0
C4 A:PRP301 4.3 34.1 1.0
OD2 A:ASP125 4.3 25.6 1.0
O2B A:PRP301 4.3 35.4 1.0
O2A A:PRP301 4.5 39.7 1.0
O A:ILE60 4.5 21.1 1.0
CG A:ASP124 4.5 20.3 1.0
CB A:ARG63 4.6 22.5 1.0
CD A:ARG63 4.8 32.9 1.0
N A:GLY64 4.9 18.1 1.0
CA A:ARG63 5.0 21.5 1.0
NE A:ARG63 5.0 36.0 1.0

Reference:

W.Shi, A.E.Sarver, C.C.Wang, K.S.Tanaka, S.C.Almo, V.L.Schramm. Closed Site Complexes of Adenine Phosphoribosyltransferase From Giardia Lamblia Reveal A Mechanism of Ribosyl Migration. J.Biol.Chem. V. 277 39981 2002.
ISSN: ISSN 0021-9258
PubMed: 12171925
DOI: 10.1074/JBC.M205596200
Page generated: Tue Aug 13 08:12:40 2024

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