Atomistry » Aluminium » PDB 1a6e-1tx4 » 1tad
Atomistry »
  Aluminium »
    PDB 1a6e-1tx4 »
      1tad »

Aluminium in PDB 1tad: Gtpase Mechanism of Gproteins From the 1.7-Angstrom Crystal Structure of Transducin Alpha-Gdp-ALF4-

Protein crystallography data

The structure of Gtpase Mechanism of Gproteins From the 1.7-Angstrom Crystal Structure of Transducin Alpha-Gdp-ALF4-, PDB code: 1tad was solved by J.Sondek, D.G.Lambright, J.P.Noel, H.E.Hamm, P.B.Sigler, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 8.00 / 1.70
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 74.900, 108.200, 79.000, 90.00, 111.70, 90.00
R / Rfree (%) 20.9 / 26.6

Other elements in 1tad:

The structure of Gtpase Mechanism of Gproteins From the 1.7-Angstrom Crystal Structure of Transducin Alpha-Gdp-ALF4- also contains other interesting chemical elements:

Fluorine (F) 12 atoms
Arsenic (As) 6 atoms
Calcium (Ca) 3 atoms

Aluminium Binding Sites:

The binding sites of Aluminium atom in the Gtpase Mechanism of Gproteins From the 1.7-Angstrom Crystal Structure of Transducin Alpha-Gdp-ALF4- (pdb code 1tad). This binding sites where shown within 5.0 Angstroms radius around Aluminium atom.
In total 3 binding sites of Aluminium where determined in the Gtpase Mechanism of Gproteins From the 1.7-Angstrom Crystal Structure of Transducin Alpha-Gdp-ALF4-, PDB code: 1tad:
Jump to Aluminium binding site number: 1; 2; 3;

Aluminium binding site 1 out of 3 in 1tad

Go back to Aluminium Binding Sites List in 1tad
Aluminium binding site 1 out of 3 in the Gtpase Mechanism of Gproteins From the 1.7-Angstrom Crystal Structure of Transducin Alpha-Gdp-ALF4-


Mono view


Stereo pair view

A full contact list of Aluminium with other atoms in the Al binding site number 1 of Gtpase Mechanism of Gproteins From the 1.7-Angstrom Crystal Structure of Transducin Alpha-Gdp-ALF4- within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Al355

b:10.3
occ:1.00
AL A:ALF355 0.0 10.3 1.0
F3 A:ALF355 1.8 10.0 1.0
F1 A:ALF355 1.8 10.2 1.0
F2 A:ALF355 1.8 11.4 1.0
F4 A:ALF355 1.8 11.5 1.0
O3B A:GDP351 1.9 9.0 1.0
O A:HOH400 2.0 9.8 1.0
PB A:GDP351 3.3 9.7 1.0
CA A:CA352 3.3 13.4 1.0
O2B A:GDP351 3.7 8.5 1.0
NH1 A:ARG174 3.9 6.9 1.0
NE2 A:GLN200 3.9 11.2 1.0
O1B A:GDP351 3.9 9.8 1.0
N A:GLU39 3.9 11.1 1.0
NZ A:LYS42 4.0 9.2 1.0
N A:GLY199 4.0 12.6 1.0
OE1 A:GLN200 4.0 16.7 1.0
NH2 A:ARG174 4.1 12.6 1.0
O A:THR177 4.2 14.3 1.0
O3A A:GDP351 4.3 11.5 1.0
CE A:LYS42 4.4 8.8 1.0
N A:THR177 4.4 11.2 1.0
CA A:GLY198 4.4 13.2 1.0
CD A:GLN200 4.4 15.2 1.0
O A:HOH401 4.4 8.0 1.0
OG1 A:THR177 4.4 10.2 1.0
CA A:GLY38 4.5 12.5 1.0
CZ A:ARG174 4.5 9.3 1.0
O A:HOH402 4.6 9.5 1.0
C A:GLY198 4.7 12.9 1.0
CA A:GLU39 4.7 12.5 1.0
C A:GLY38 4.7 11.8 1.0
CA A:GLY199 4.9 9.2 1.0
CG A:LYS176 4.9 17.0 1.0
CA A:LYS176 5.0 12.6 1.0

Aluminium binding site 2 out of 3 in 1tad

Go back to Aluminium Binding Sites List in 1tad
Aluminium binding site 2 out of 3 in the Gtpase Mechanism of Gproteins From the 1.7-Angstrom Crystal Structure of Transducin Alpha-Gdp-ALF4-


Mono view


Stereo pair view

A full contact list of Aluminium with other atoms in the Al binding site number 2 of Gtpase Mechanism of Gproteins From the 1.7-Angstrom Crystal Structure of Transducin Alpha-Gdp-ALF4- within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Al355

b:11.6
occ:1.00
AL B:ALF355 0.0 11.6 1.0
F4 B:ALF355 1.8 11.6 1.0
F1 B:ALF355 1.8 14.0 1.0
F2 B:ALF355 1.8 14.1 1.0
F3 B:ALF355 1.8 13.9 1.0
O3B B:GDP351 1.9 10.8 1.0
O B:HOH403 2.0 12.4 1.0
PB B:GDP351 3.2 10.9 1.0
CA B:CA352 3.3 16.9 1.0
O2B B:GDP351 3.7 9.4 1.0
N B:GLY199 3.9 14.9 1.0
N B:GLU39 3.9 16.1 1.0
O1B B:GDP351 3.9 12.9 1.0
OE1 B:GLN200 4.0 20.4 1.0
NH1 B:ARG174 4.0 10.3 1.0
NZ B:LYS42 4.0 11.8 1.0
NE2 B:GLN200 4.1 18.8 1.0
O B:THR177 4.2 16.8 1.0
NH2 B:ARG174 4.2 12.7 1.0
CA B:GLY198 4.3 15.7 1.0
O3A B:GDP351 4.3 14.9 1.0
CE B:LYS42 4.3 12.5 1.0
O B:HOH405 4.3 11.1 1.0
CD B:GLN200 4.5 20.4 1.0
CA B:GLY38 4.5 15.1 1.0
N B:THR177 4.5 16.0 1.0
OG1 B:THR177 4.5 13.6 1.0
CZ B:ARG174 4.6 12.1 1.0
C B:GLY198 4.6 15.6 1.0
O B:HOH404 4.7 11.7 1.0
CA B:GLU39 4.7 16.1 1.0
C B:GLY38 4.7 17.2 1.0
CA B:GLY199 4.8 15.9 1.0
O B:VAL197 4.9 15.6 1.0
CG B:LYS176 5.0 23.5 1.0

Aluminium binding site 3 out of 3 in 1tad

Go back to Aluminium Binding Sites List in 1tad
Aluminium binding site 3 out of 3 in the Gtpase Mechanism of Gproteins From the 1.7-Angstrom Crystal Structure of Transducin Alpha-Gdp-ALF4-


Mono view


Stereo pair view

A full contact list of Aluminium with other atoms in the Al binding site number 3 of Gtpase Mechanism of Gproteins From the 1.7-Angstrom Crystal Structure of Transducin Alpha-Gdp-ALF4- within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Al355

b:12.3
occ:1.00
AL C:ALF355 0.0 12.3 1.0
F1 C:ALF355 1.8 12.3 1.0
F4 C:ALF355 1.8 11.9 1.0
F3 C:ALF355 1.8 13.8 1.0
F2 C:ALF355 1.8 12.5 1.0
O C:HOH406 2.0 10.9 1.0
O3B C:GDP351 2.1 11.9 1.0
CA C:CA352 3.3 12.3 1.0
PB C:GDP351 3.3 9.6 1.0
O2B C:GDP351 3.6 7.7 1.0
NH1 C:ARG174 3.8 13.7 1.0
N C:GLY199 3.9 11.4 1.0
N C:GLU39 3.9 13.3 1.0
NE2 C:GLN200 3.9 11.9 1.0
O1B C:GDP351 3.9 10.3 1.0
NZ C:LYS42 4.0 7.5 1.0
OE1 C:GLN200 4.0 16.2 1.0
O C:THR177 4.1 15.7 1.0
NH2 C:ARG174 4.2 11.1 1.0
CA C:GLY198 4.3 10.9 1.0
CE C:LYS42 4.4 8.4 1.0
O C:HOH408 4.4 7.3 1.0
CD C:GLN200 4.4 13.2 1.0
O3A C:GDP351 4.4 12.1 1.0
N C:THR177 4.5 14.9 1.0
CZ C:ARG174 4.5 13.8 1.0
OG1 C:THR177 4.5 15.5 1.0
CA C:GLY38 4.6 10.5 1.0
C C:GLY198 4.6 12.0 1.0
O C:HOH407 4.7 11.6 1.0
CA C:GLU39 4.7 12.5 1.0
C C:GLY38 4.8 8.6 1.0
CA C:GLY199 4.8 11.3 1.0
CG C:LYS176 4.9 23.4 1.0

Reference:

J.Sondek, D.G.Lambright, J.P.Noel, H.E.Hamm, P.B.Sigler. Gtpase Mechanism of Gproteins From the 1.7-A Crystal Structure of Transducin Alpha-Gdp-Aif-4. Nature V. 372 276 1994.
ISSN: ISSN 0028-0836
PubMed: 7969474
DOI: 10.1038/372276A0
Page generated: Sat Dec 12 01:30:36 2020

Last articles

Zn in 8WB0
Zn in 8WAX
Zn in 8WAU
Zn in 8WAZ
Zn in 8WAY
Zn in 8WAV
Zn in 8WAW
Zn in 8WAT
Zn in 8W7M
Zn in 8WD3
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy