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Magnesium in PDB 5ifs: Quantitative Interaction Mapping Reveals An Extended Ubiquitin Regulatory Domain in Aspl That Disrupts Functional P97 Hexamers and Induces Cell Death

Enzymatic activity of Quantitative Interaction Mapping Reveals An Extended Ubiquitin Regulatory Domain in Aspl That Disrupts Functional P97 Hexamers and Induces Cell Death

All present enzymatic activity of Quantitative Interaction Mapping Reveals An Extended Ubiquitin Regulatory Domain in Aspl That Disrupts Functional P97 Hexamers and Induces Cell Death:
3.6.4.6;

Protein crystallography data

The structure of Quantitative Interaction Mapping Reveals An Extended Ubiquitin Regulatory Domain in Aspl That Disrupts Functional P97 Hexamers and Induces Cell Death, PDB code: 5ifs was solved by Y.Roske, A.Arumughan, U.Heinemann, E.Wanker, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 33.77 / 2.46
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 69.844, 132.914, 96.121, 90.00, 110.15, 90.00
R / Rfree (%) 20.1 / 25.1

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Quantitative Interaction Mapping Reveals An Extended Ubiquitin Regulatory Domain in Aspl That Disrupts Functional P97 Hexamers and Induces Cell Death (pdb code 5ifs). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Quantitative Interaction Mapping Reveals An Extended Ubiquitin Regulatory Domain in Aspl That Disrupts Functional P97 Hexamers and Induces Cell Death, PDB code: 5ifs:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 5ifs

Go back to Magnesium Binding Sites List in 5ifs
Magnesium binding site 1 out of 2 in the Quantitative Interaction Mapping Reveals An Extended Ubiquitin Regulatory Domain in Aspl That Disrupts Functional P97 Hexamers and Induces Cell Death


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Quantitative Interaction Mapping Reveals An Extended Ubiquitin Regulatory Domain in Aspl That Disrupts Functional P97 Hexamers and Induces Cell Death within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg502

b:57.2
occ:1.00
O2B B:ADP501 2.6 28.0 1.0
O B:HOH635 3.8 38.2 1.0
PB B:ADP501 3.9 26.4 1.0
OD1 B:ASP304 4.0 41.2 1.0
OD2 B:ASP304 4.0 42.4 1.0
O3B B:ADP501 4.3 28.3 1.0
O2A B:ADP501 4.4 32.0 1.0
CG B:ASP304 4.5 40.5 1.0
O B:HOH742 4.5 40.2 1.0
N B:GLY248 4.5 30.9 1.0
CA B:PRO247 4.6 33.4 1.0
NZ B:LYS251 4.7 31.6 1.0
CB B:PRO247 4.7 32.6 1.0
O1B B:ADP501 4.8 27.3 1.0
O B:HOH607 4.8 27.4 1.0
O3A B:ADP501 4.9 28.4 1.0

Magnesium binding site 2 out of 2 in 5ifs

Go back to Magnesium Binding Sites List in 5ifs
Magnesium binding site 2 out of 2 in the Quantitative Interaction Mapping Reveals An Extended Ubiquitin Regulatory Domain in Aspl That Disrupts Functional P97 Hexamers and Induces Cell Death


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Quantitative Interaction Mapping Reveals An Extended Ubiquitin Regulatory Domain in Aspl That Disrupts Functional P97 Hexamers and Induces Cell Death within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Mg502

b:63.5
occ:1.00
O3B D:ADP501 2.4 29.0 1.0
O D:HOH608 3.3 45.6 1.0
PB D:ADP501 3.5 29.5 1.0
O1B D:ADP501 3.8 29.9 1.0
OD1 D:ASP304 4.0 45.8 1.0
CA D:PRO247 4.1 32.0 1.0
CB D:PRO247 4.2 32.9 1.0
N D:GLY248 4.3 31.1 1.0
O2B D:ADP501 4.4 30.3 1.0
NZ D:LYS251 4.5 39.0 1.0
O3A D:ADP501 4.7 30.9 1.0
C D:PRO247 4.8 32.1 1.0
O1A D:ADP501 4.8 31.7 1.0
CG D:ASP304 4.9 47.0 1.0
OD2 D:ASP304 5.0 48.3 1.0
O D:HOH609 5.0 35.5 1.0

Reference:

A.Arumughan, Y.Roske, C.Barth, L.L.Forero, K.Bravo-Rodriguez, A.Redel, S.Kostova, E.Mcshane, R.Opitz, K.Faelber, K.Rau, T.Mielke, O.Daumke, M.Selbach, E.Sanchez-Garcia, O.Rocks, D.Panakova, U.Heinemann, E.E.Wanker. Quantitative Interaction Mapping Reveals An Extended Ubx Domain in Aspl That Disrupts Functional P97 Hexamers. Nat Commun V. 7 13047 2016.
ISSN: ESSN 2041-1723
PubMed: 27762274
DOI: 10.1038/NCOMMS13047
Page generated: Sun Sep 29 16:41:07 2024

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