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Magnesium in PDB 1z22: Gdp-Bound RAB23 Gtpase Crystallized in C222(1) Space Group

Protein crystallography data

The structure of Gdp-Bound RAB23 Gtpase Crystallized in C222(1) Space Group, PDB code: 1z22 was solved by S.Eathiraj, X.Pan, C.Ritacco, D.G.Lambright, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 6.00 / 2.06
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 67.010, 71.333, 65.684, 90.00, 90.00, 90.00
R / Rfree (%) 19.4 / 23.4

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Gdp-Bound RAB23 Gtpase Crystallized in C222(1) Space Group (pdb code 1z22). 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 Gdp-Bound RAB23 Gtpase Crystallized in C222(1) Space Group, PDB code: 1z22:

Magnesium binding site 1 out of 1 in 1z22

Go back to Magnesium Binding Sites List in 1z22
Magnesium binding site 1 out of 1 in the Gdp-Bound RAB23 Gtpase Crystallized in C222(1) Space Group


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Gdp-Bound RAB23 Gtpase Crystallized in C222(1) Space Group within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg300

b:33.8
occ:1.00
OD2 A:ASP64 2.5 15.9 1.0
O3B A:GDP201 2.8 16.1 1.0
O A:HOH341 3.0 27.6 1.0
O A:HOH466 3.3 46.0 1.0
CG A:ASP64 3.4 15.2 1.0
OD1 A:ASP64 3.5 14.4 1.0
O1B A:GDP201 3.5 15.5 1.0
PB A:GDP201 3.6 15.0 1.0
CA A:ALA66 4.0 17.1 1.0
CE A:LYS22 4.1 13.6 1.0
NZ A:LYS22 4.2 13.5 1.0
O2B A:GDP201 4.2 15.9 1.0
CB A:ALA66 4.2 17.0 1.0
CB A:SER23 4.2 13.7 1.0
OG A:SER23 4.2 14.8 1.0
N A:SER23 4.5 13.4 1.0
CB A:LYS22 4.6 13.2 1.0
N A:ALA66 4.7 16.6 1.0
CB A:ASP64 4.8 15.5 1.0
C A:ALA66 4.9 17.6 1.0
O A:HOH427 4.9 56.0 1.0
CA A:SER23 4.9 13.6 1.0

Reference:

S.Eathiraj, X.Pan, C.Ritacco, D.G.Lambright. Structural Basis of Family-Wide Rab Gtpase Recognition By Rabenosyn-5. Nature V. 436 415 2005.
ISSN: ISSN 0028-0836
PubMed: 16034420
DOI: 10.1038/NATURE03798
Page generated: Tue Aug 13 20:00:32 2024

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