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Magnesium in PDB 5dis: Crystal Structure of A CRM1-Rangtp-SPN1 Export Complex Bound to A 113 Amino Acid Fg-Repeat Containing Fragment of NUP214

Protein crystallography data

The structure of Crystal Structure of A CRM1-Rangtp-SPN1 Export Complex Bound to A 113 Amino Acid Fg-Repeat Containing Fragment of NUP214, PDB code: 5dis was solved by T.Monecke, S.A.Port, A.Dickmanns, R.H.Kehlenbach, R.Ficner, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 48.49 / 2.85
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 112.330, 248.970, 210.570, 90.00, 90.00, 90.00
R / Rfree (%) 20.6 / 24.9

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of A CRM1-Rangtp-SPN1 Export Complex Bound to A 113 Amino Acid Fg-Repeat Containing Fragment of NUP214 (pdb code 5dis). 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 A CRM1-Rangtp-SPN1 Export Complex Bound to A 113 Amino Acid Fg-Repeat Containing Fragment of NUP214, PDB code: 5dis:

Magnesium binding site 1 out of 1 in 5dis

Go back to Magnesium Binding Sites List in 5dis
Magnesium binding site 1 out of 1 in the Crystal Structure of A CRM1-Rangtp-SPN1 Export Complex Bound to A 113 Amino Acid Fg-Repeat Containing Fragment of NUP214


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 A CRM1-Rangtp-SPN1 Export Complex Bound to A 113 Amino Acid Fg-Repeat Containing Fragment of NUP214 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg202

b:94.1
occ:1.00
O1B B:GTP201 2.0 78.9 1.0
O B:HOH303 2.0 0.7 1.0
OG1 B:THR42 2.0 92.6 1.0
O1G B:GTP201 2.0 0.5 1.0
OG1 B:THR24 2.1 74.4 1.0
O B:HOH302 2.2 66.9 1.0
CB B:THR42 2.9 77.5 1.0
PG B:GTP201 2.9 0.5 1.0
O2G B:GTP201 3.1 0.6 1.0
PB B:GTP201 3.2 69.9 1.0
O3B B:GTP201 3.5 66.0 1.0
N B:THR42 3.5 67.5 1.0
CB B:THR24 3.5 68.2 1.0
CA B:THR42 3.7 72.2 1.0
OD1 B:ASP65 3.8 0.9 1.0
OD2 B:ASP65 3.9 93.7 1.0
O2A B:GTP201 4.0 99.9 1.0
CG2 B:THR42 4.1 82.3 1.0
N B:THR24 4.2 55.2 1.0
CG B:ASP65 4.3 0.4 1.0
O3A B:GTP201 4.3 0.9 1.0
O2B B:GTP201 4.3 70.9 1.0
O3G B:GTP201 4.3 0.1 1.0
CG2 B:THR24 4.4 85.8 1.0
CA B:THR24 4.4 64.7 1.0
O B:THR66 4.4 73.0 1.0
NZ B:LYS23 4.5 84.5 1.0
C B:ALA41 4.6 71.3 1.0
PA B:GTP201 4.6 84.7 1.0
CB B:LYS23 4.9 46.3 1.0
CA B:ALA41 4.9 69.9 1.0
C B:THR42 5.0 78.6 1.0
O B:VAL40 5.0 84.8 1.0

Reference:

S.A.Port, T.Monecke, A.Dickmanns, C.Spillner, R.Hofele, H.Urlaub, R.Ficner, R.H.Kehlenbach. Structural and Functional Characterization of CRM1-NUP214 Interactions Reveals Multiple Fg-Binding Sites Involved in Nuclear Export. Cell Rep V. 13 690 2015.
ISSN: ESSN 2211-1247
PubMed: 26489467
DOI: 10.1016/J.CELREP.2015.09.042
Page generated: Sun Sep 29 02:49:09 2024

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