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Aluminium in PDB 1agr: Complex of ALF4-Activated Gi-Alpha-1 with RGS4

Protein crystallography data

The structure of Complex of ALF4-Activated Gi-Alpha-1 with RGS4, PDB code: 1agr was solved by J.J.G.Tesmer, S.R.Sprang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 5.00 / 2.80
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 164.000, 97.200, 110.000, 90.00, 90.00, 90.00
R / Rfree (%) 21.6 / 29.1

Other elements in 1agr:

The structure of Complex of ALF4-Activated Gi-Alpha-1 with RGS4 also contains other interesting chemical elements:

Fluorine (F) 8 atoms
Magnesium (Mg) 2 atoms

Aluminium Binding Sites:

The binding sites of Aluminium atom in the Complex of ALF4-Activated Gi-Alpha-1 with RGS4 (pdb code 1agr). This binding sites where shown within 5.0 Angstroms radius around Aluminium atom.
In total 2 binding sites of Aluminium where determined in the Complex of ALF4-Activated Gi-Alpha-1 with RGS4, PDB code: 1agr:
Jump to Aluminium binding site number: 1; 2;

Aluminium binding site 1 out of 2 in 1agr

Go back to Aluminium Binding Sites List in 1agr
Aluminium binding site 1 out of 2 in the Complex of ALF4-Activated Gi-Alpha-1 with RGS4


Mono view


Stereo pair view

A full contact list of Aluminium with other atoms in the Al binding site number 1 of Complex of ALF4-Activated Gi-Alpha-1 with RGS4 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Al357

b:12.3
occ:1.00
AL A:ALF357 0.0 12.3 1.0
F4 A:ALF357 1.7 8.3 1.0
F3 A:ALF357 1.7 19.3 1.0
F2 A:ALF357 1.8 2.6 1.0
F1 A:ALF357 1.8 9.2 1.0
O A:HOH359A 2.0 22.2 1.0
O3B A:GDP355 2.1 28.5 1.0
PB A:GDP355 3.2 16.9 1.0
MG A:MG356 3.3 14.3 1.0
O2B A:GDP355 3.6 2.0 1.0
NH2 A:ARG178 3.7 11.1 1.0
N A:THR181 3.7 21.3 1.0
O A:HOH365 3.8 11.6 1.0
O1B A:GDP355 3.8 7.8 1.0
NH1 A:ARG178 3.8 22.4 1.0
N A:GLU43 3.9 25.9 1.0
N A:GLY203 4.0 12.0 1.0
OE1 A:GLN204 4.1 8.7 1.0
OG1 A:THR181 4.2 29.4 1.0
CB A:THR181 4.2 26.5 1.0
O A:HOH364 4.2 15.1 1.0
NE2 A:GLN204 4.2 2.4 1.0
CZ A:ARG178 4.3 19.8 1.0
NZ A:LYS46 4.3 15.0 1.0
O A:THR181 4.3 17.8 1.0
CA A:GLY42 4.3 19.1 1.0
CA A:THR181 4.5 21.4 1.0
O3A A:GDP355 4.5 11.5 1.0
CA A:GLY202 4.5 8.6 1.0
CD A:GLN204 4.5 5.4 1.0
CG A:LYS180 4.6 29.1 1.0
CA A:LYS180 4.6 19.4 1.0
C A:GLY42 4.6 21.6 1.0
C A:LYS180 4.7 22.1 1.0
O A:VAL201 4.7 29.0 1.0
CE A:LYS46 4.8 19.8 1.0
C A:GLY202 4.8 11.3 1.0
CA A:GLU43 4.8 27.7 1.0
CA A:GLY203 4.8 12.1 1.0
C A:THR181 4.9 19.6 1.0

Aluminium binding site 2 out of 2 in 1agr

Go back to Aluminium Binding Sites List in 1agr
Aluminium binding site 2 out of 2 in the Complex of ALF4-Activated Gi-Alpha-1 with RGS4


Mono view


Stereo pair view

A full contact list of Aluminium with other atoms in the Al binding site number 2 of Complex of ALF4-Activated Gi-Alpha-1 with RGS4 within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Al357

b:28.8
occ:1.00
AL D:ALF357 0.0 28.8 1.0
F1 D:ALF357 1.7 22.4 1.0
F4 D:ALF357 1.7 18.6 1.0
F3 D:ALF357 1.7 21.1 1.0
F2 D:ALF357 1.8 14.2 1.0
O3B D:GDP355 2.0 31.5 1.0
O D:HOH360D 2.0 25.5 1.0
PB D:GDP355 3.1 27.5 1.0
MG D:MG356 3.3 15.2 1.0
O2B D:GDP355 3.6 17.7 1.0
NH2 D:ARG178 3.7 11.8 1.0
N D:THR181 3.7 26.9 1.0
O1B D:GDP355 3.8 17.7 1.0
O D:HOH366 3.8 14.5 1.0
N D:GLU43 3.8 23.5 1.0
NH1 D:ARG178 3.8 15.3 1.0
N D:GLY203 4.0 22.9 1.0
OE1 D:GLN204 4.1 15.8 1.0
OG1 D:THR181 4.2 42.7 1.0
CB D:THR181 4.2 37.7 1.0
NE2 D:GLN204 4.2 17.3 1.0
O D:HOH365 4.2 18.9 1.0
CZ D:ARG178 4.2 18.1 1.0
NZ D:LYS46 4.3 32.9 1.0
CA D:GLY42 4.3 22.9 1.0
O D:THR181 4.3 21.7 1.0
O3A D:GDP355 4.4 19.4 1.0
CA D:THR181 4.5 30.9 1.0
CD D:GLN204 4.6 10.6 1.0
CA D:GLY202 4.6 21.7 1.0
CA D:LYS180 4.6 17.3 1.0
C D:GLY42 4.6 20.2 1.0
CG D:LYS180 4.6 25.0 1.0
C D:LYS180 4.7 24.4 1.0
O D:VAL201 4.7 39.4 1.0
CA D:GLU43 4.7 28.3 1.0
CE D:LYS46 4.8 34.7 1.0
C D:GLY202 4.8 22.7 1.0
CA D:GLY203 4.8 18.9 1.0
C D:THR181 4.9 28.3 1.0

Reference:

J.J.Tesmer, D.M.Berman, A.G.Gilman, S.R.Sprang. Structure of RGS4 Bound to ALF4--Activated G(I ALPHA1): Stabilization of the Transition State For Gtp Hydrolysis. Cell(Cambridge,Mass.) V. 89 251 1997.
ISSN: ISSN 0092-8674
PubMed: 9108480
DOI: 10.1016/S0092-8674(00)80204-4
Page generated: Sat Dec 12 01:30:03 2020

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