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Aluminium in PDB 3d7m: Crystal Structure of the G Protein Fast-Exchange Double Mutant I56C/Q333C

Protein crystallography data

The structure of Crystal Structure of the G Protein Fast-Exchange Double Mutant I56C/Q333C, PDB code: 3d7m was solved by M.A.Funk, A.M.Preininger, W.M.Oldham, S.M.Meier, H.E.Hamm, T.M.Iverson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.00 / 2.90
Space group P 43 21 2
Cell size a, b, c (Å), α, β, γ (°) 79.659, 79.659, 114.587, 90.00, 90.00, 90.00
R / Rfree (%) 24.9 / 29.4

Other elements in 3d7m:

The structure of Crystal Structure of the G Protein Fast-Exchange Double Mutant I56C/Q333C also contains other interesting chemical elements:

Fluorine (F) 4 atoms
Magnesium (Mg) 1 atom

Aluminium Binding Sites:

The binding sites of Aluminium atom in the Crystal Structure of the G Protein Fast-Exchange Double Mutant I56C/Q333C (pdb code 3d7m). This binding sites where shown within 5.0 Angstroms radius around Aluminium atom.
In total only one binding site of Aluminium was determined in the Crystal Structure of the G Protein Fast-Exchange Double Mutant I56C/Q333C, PDB code: 3d7m:

Aluminium binding site 1 out of 1 in 3d7m

Go back to Aluminium Binding Sites List in 3d7m
Aluminium binding site 1 out of 1 in the Crystal Structure of the G Protein Fast-Exchange Double Mutant I56C/Q333C


Mono view


Stereo pair view

A full contact list of Aluminium with other atoms in the Al binding site number 1 of Crystal Structure of the G Protein Fast-Exchange Double Mutant I56C/Q333C within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Al357

b:95.6
occ:1.00
AL A:ALF357 0.0 95.6 1.0
F3 A:ALF357 1.7 95.8 1.0
F2 A:ALF357 1.7 94.7 1.0
F1 A:ALF357 1.7 95.9 1.0
F4 A:ALF357 1.8 97.0 1.0
O3B A:GDP355 2.3 70.9 1.0
PB A:GDP355 3.5 69.3 1.0
MG A:MG356 3.6 54.7 1.0
O2B A:GDP355 3.8 72.0 1.0
NH2 A:ARG178 3.8 64.8 1.0
NE2 A:GLN204 3.8 0.1 1.0
N A:THR181 3.9 81.7 1.0
NH1 A:ARG178 3.9 64.1 1.0
NZ A:LYS46 4.0 64.8 1.0
N A:GLU43 4.0 74.0 1.0
N A:GLY203 4.1 0.2 1.0
O A:HOH412 4.2 65.5 1.0
CB A:THR181 4.3 84.0 1.0
CZ A:ARG178 4.3 64.6 1.0
O A:THR181 4.4 89.8 1.0
O3A A:GDP355 4.4 66.7 1.0
CA A:GLY42 4.5 73.8 1.0
O1B A:GDP355 4.5 68.7 1.0
CA A:GLY202 4.6 0.9 1.0
CA A:THR181 4.6 85.0 1.0
CD A:GLN204 4.7 0.2 1.0
OG1 A:THR181 4.8 84.8 1.0
CA A:LYS180 4.8 79.5 1.0
C A:GLY42 4.8 74.4 1.0
CE A:LYS46 4.8 67.1 1.0
C A:LYS180 4.8 79.9 1.0
C A:GLY202 4.8 0.4 1.0
CA A:GLU43 4.9 73.2 1.0
C A:THR181 5.0 88.0 1.0

Reference:

A.M.Preininger, M.A.Funk, W.M.Oldham, S.M.Meier, C.A.Johnston, S.Adhikary, A.J.Kimple, D.P.Siderovski, H.E.Hamm, T.M.Iverson. Helix Dipole Movement and Conformational Variability Contribute to Allosteric Gdp Release in Galphai Subunits. Biochemistry V. 48 2630 2009.
ISSN: ISSN 0006-2960
PubMed: 19222191
DOI: 10.1021/BI801853A
Page generated: Sat Dec 12 01:32:19 2020

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