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Magnesium in PDB 1xtj: Structure of Human UAP56 in Complex with Adp

Protein crystallography data

The structure of Structure of Human UAP56 in Complex with Adp, PDB code: 1xtj was solved by H.Shi, O.Cordin, C.M.Minder, P.Linder, R.-M.Xu, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 32.70 / 2.70
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 36.988, 78.201, 63.192, 90.00, 103.42, 90.00
R / Rfree (%) 21 / 30

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Structure of Human UAP56 in Complex with Adp (pdb code 1xtj). 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 Structure of Human UAP56 in Complex with Adp, PDB code: 1xtj:

Magnesium binding site 1 out of 1 in 1xtj

Go back to Magnesium Binding Sites List in 1xtj
Magnesium binding site 1 out of 1 in the Structure of Human UAP56 in Complex with Adp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of Human UAP56 in Complex with Adp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg501

b:36.0
occ:1.00
O3B A:ADP550 2.1 46.2 1.0
OE2 A:GLU197 3.0 42.9 1.0
OD1 A:ASP196 3.4 31.6 1.0
OD2 A:ASP196 3.4 32.4 1.0
CG2 A:THR96 3.4 28.8 1.0
PB A:ADP550 3.5 44.8 1.0
CG A:ASP196 3.8 31.1 1.0
O1B A:ADP550 3.9 47.1 1.0
CE A:LYS95 4.0 23.4 1.0
CD A:GLU197 4.1 42.2 1.0
O2B A:ADP550 4.1 43.0 1.0
CB A:LYS95 4.3 25.9 1.0
N A:THR96 4.4 27.4 1.0
CG A:GLU197 4.4 40.8 1.0
NZ A:LYS95 4.5 24.7 1.0
O3A A:ADP550 4.7 43.2 1.0
CB A:THR96 4.8 30.8 1.0
O2A A:ADP550 5.0 44.6 1.0
CA A:THR96 5.0 29.6 1.0
O1A A:ADP550 5.0 41.6 1.0

Reference:

H.Shi, O.Cordin, C.M.Minder, P.Linder, R.-M.Xu. Crystal Structure of the Human Atp-Dependent Splicing and Export Factor UAP56 Proc.Natl.Acad.Sci.Usa V. 101 17628 2004.
ISSN: ISSN 0027-8424
PubMed: 15585580
DOI: 10.1073/PNAS.0408172101
Page generated: Sun Aug 10 07:36:55 2025

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