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Magnesium in PDB 3rce: Bacterial Oligosaccharyltransferase Pglb

Protein crystallography data

The structure of Bacterial Oligosaccharyltransferase Pglb, PDB code: 3rce was solved by C.Lizak, S.Gerber, S.Numao, M.Aebi, K.P.Locher, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 29.98 / 3.40
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 85.060, 116.100, 175.040, 90.00, 90.00, 90.00
R / Rfree (%) 23.8 / 27.1

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Bacterial Oligosaccharyltransferase Pglb (pdb code 3rce). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Bacterial Oligosaccharyltransferase Pglb, PDB code: 3rce:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 3rce

Go back to Magnesium Binding Sites List in 3rce
Magnesium binding site 1 out of 2 in the Bacterial Oligosaccharyltransferase Pglb


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Bacterial Oligosaccharyltransferase Pglb within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg725

b:78.1
occ:1.00
OD2 A:ASP56 2.4 0.1 1.0
OD2 A:ASP154 2.8 71.9 1.0
OE2 A:GLU319 2.9 0.8 1.0
OD1 A:ASP154 2.9 70.7 1.0
CG A:ASP154 3.1 70.5 1.0
CG A:ASP56 3.5 0.4 1.0
CD A:GLU319 4.1 0.4 1.0
NH1 A:ARG147 4.1 96.3 1.0
CB A:ASP56 4.2 0.9 1.0
OD1 A:ASP156 4.2 0.0 1.0
NH2 A:ARG147 4.4 98.0 1.0
CB A:ASP154 4.4 70.0 1.0
OD1 A:ASP56 4.5 0.1 1.0
OE1 A:GLU319 4.6 0.7 1.0
OH A:TYR152 4.6 0.4 1.0
CZ A:ARG147 4.7 97.0 1.0
CE2 A:TYR152 4.9 0.6 1.0
CG A:ASP156 4.9 0.7 1.0

Magnesium binding site 2 out of 2 in 3rce

Go back to Magnesium Binding Sites List in 3rce
Magnesium binding site 2 out of 2 in the Bacterial Oligosaccharyltransferase Pglb


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Bacterial Oligosaccharyltransferase Pglb within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg726

b:65.5
occ:1.00
OE1 A:GLN73 2.6 0.4 1.0
OD1 A:ASP475 2.7 0.4 1.0
OD2 A:ASP76 2.8 0.2 1.0
O A:ASP475 3.2 0.9 1.0
CD A:GLN73 3.6 0.2 1.0
CG A:ASP475 3.8 0.8 1.0
CG A:ASP76 3.9 0.5 1.0
C A:ASP475 3.9 0.6 1.0
NE2 A:GLN73 4.1 0.4 1.0
CA A:ASP475 4.2 0.9 1.0
OD2 A:ASP66 4.3 0.0 1.0
O A:VAL476 4.4 0.9 1.0
OE2 A:GLU62 4.5 0.7 1.0
CB A:ASP475 4.6 0.7 1.0
OD1 A:ASP76 4.6 0.5 1.0
NH2 A:ARG65 4.6 0.3 1.0
OD2 A:ASP475 4.7 1.0 1.0
CB A:ASP76 4.7 0.9 1.0
O A:ARG456 4.8 1.0 1.0
N A:GLN73 4.8 0.3 1.0
OD1 A:ASP66 4.9 0.5 1.0
CG A:GLN73 4.9 0.8 1.0
CB A:GLN73 4.9 0.7 1.0
N A:VAL476 5.0 0.5 1.0

Reference:

C.Lizak, S.Gerber, S.Numao, M.Aebi, K.P.Locher. X-Ray Structure of A Bacterial Oligosaccharyltransferase. Nature V. 474 350 2011.
ISSN: ISSN 0028-0836
PubMed: 21677752
DOI: 10.1038/NATURE10151
Page generated: Mon Dec 14 08:44:29 2020

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