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Magnesium in PDB 1vg1: Gdp-Bound RAB7

Protein crystallography data

The structure of Gdp-Bound RAB7, PDB code: 1vg1 was solved by A.Rak, O.Pylypenko, A.Niculae, K.Pyatkov, R.S.Goody, K.Alexandrov, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 18.79 / 1.90
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 64.500, 103.200, 51.700, 90.00, 90.00, 90.00
R / Rfree (%) 18.7 / 24.7

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Gdp-Bound RAB7 (pdb code 1vg1). 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 RAB7, PDB code: 1vg1:

Magnesium binding site 1 out of 1 in 1vg1

Go back to Magnesium Binding Sites List in 1vg1
Magnesium binding site 1 out of 1 in the Gdp-Bound RAB7


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Gdp-Bound RAB7 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg3000

b:37.4
occ:1.00
O A:HOH1087 2.0 27.1 1.0
O3B A:GDP1557 2.1 22.6 1.0
O A:HOH1088 2.2 26.2 1.0
O A:HOH1153 2.2 34.5 1.0
OG1 A:THR22 2.4 24.5 1.0
O A:HOH1085 2.4 40.3 1.0
PB A:GDP1557 3.2 18.9 1.0
O1B A:GDP1557 3.4 20.8 1.0
CB A:THR22 3.6 22.0 1.0
O A:HOH1086 4.1 33.2 1.0
N A:THR22 4.1 18.3 1.0
O2A A:GDP1557 4.2 29.9 1.0
O2B A:GDP1557 4.2 18.6 1.0
O A:HOH1009 4.2 25.0 1.0
OD2 A:ASP63 4.3 32.0 1.0
O A:THR64 4.4 47.7 1.0
OD1 A:ASP63 4.4 27.0 1.0
O3A A:GDP1557 4.4 22.3 1.0
CA A:THR22 4.5 19.5 1.0
CG2 A:THR22 4.7 24.5 1.0
CG A:ASP63 4.7 31.8 1.0
PA A:GDP1557 4.7 22.4 1.0
CE A:LYS21 4.8 17.2 1.0
NZ A:LYS21 4.8 18.4 1.0

Reference:

A.Rak, O.Pylypenko, A.Niculae, K.Pyatkov, R.S.Goody, K.Alexandrov. Structure of the RAB7:Rep-1 Complex: Insights Into the Mechanism of Rab Prenylation and Choroideremia Disease Cell(Cambridge,Mass.) V. 117 749 2004.
ISSN: ISSN 0092-8674
PubMed: 15186776
DOI: 10.1016/J.CELL.2004.05.017
Page generated: Tue Aug 13 15:04:20 2024

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