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Aluminium in PDB 4ido: Human Atlastin-1 1-446, C-HIS6, GDPALF4-

Protein crystallography data

The structure of Human Atlastin-1 1-446, C-HIS6, GDPALF4-, PDB code: 4ido was solved by L.J.Byrnes, A.Singh, K.Szeto, N.M.Benvin, J.P.O'donnell, W.R.Zipfel, H.Sondermann, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 43.74 / 2.09
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 49.610, 116.430, 185.400, 90.00, 90.00, 90.00
R / Rfree (%) 19.9 / 24.9

Other elements in 4ido:

The structure of Human Atlastin-1 1-446, C-HIS6, GDPALF4- 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 Human Atlastin-1 1-446, C-HIS6, GDPALF4- (pdb code 4ido). This binding sites where shown within 5.0 Angstroms radius around Aluminium atom.
In total 2 binding sites of Aluminium where determined in the Human Atlastin-1 1-446, C-HIS6, GDPALF4-, PDB code: 4ido:
Jump to Aluminium binding site number: 1; 2;

Aluminium binding site 1 out of 2 in 4ido

Go back to Aluminium Binding Sites List in 4ido
Aluminium binding site 1 out of 2 in the Human Atlastin-1 1-446, C-HIS6, GDPALF4-


Mono view


Stereo pair view

A full contact list of Aluminium with other atoms in the Al binding site number 1 of Human Atlastin-1 1-446, C-HIS6, GDPALF4- within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Al502

b:20.3
occ:1.00
AL A:ALF502 0.0 20.3 1.0
F3 A:ALF502 1.8 17.6 1.0
F1 A:ALF502 1.8 22.9 1.0
F4 A:ALF502 1.8 17.7 1.0
F2 A:ALF502 1.8 14.8 1.0
O3B A:GDP501 2.1 20.1 1.0
O A:HOH697 2.2 12.8 1.0
PB A:GDP501 3.3 14.6 1.0
MG A:MG503 3.5 14.1 1.0
O1B A:GDP501 3.6 11.2 1.0
N A:ARG77 3.9 12.5 1.0
NH2 A:ARG77 3.9 16.2 1.0
O A:HOH601 4.0 14.9 1.0
N A:THR120 4.0 13.1 1.0
O2B A:GDP501 4.0 17.1 1.0
N A:GLU119 4.0 16.0 1.0
N A:GLY149 4.1 19.1 1.0
NZ A:LYS80 4.1 8.8 1.0
NE A:ARG77 4.1 15.0 1.0
O A:HOH625 4.3 9.9 1.0
CB A:PHE76 4.3 15.2 1.0
CB A:THR120 4.4 18.5 1.0
O A:THR120 4.4 24.3 1.0
OG1 A:THR120 4.4 18.2 1.0
CA A:PHE76 4.4 19.8 1.0
O A:HOH920 4.5 10.3 1.0
CZ A:ARG77 4.5 13.3 1.0
O3A A:GDP501 4.5 13.9 1.0
CA A:GLY149 4.6 8.8 1.0
CA A:ARG118 4.6 23.1 1.0
CB A:ARG118 4.6 19.9 1.0
CA A:ARG77 4.7 14.3 1.0
CA A:THR120 4.7 20.9 1.0
C A:PHE76 4.7 12.1 1.0
CA A:GLU119 4.8 21.8 1.0
C A:GLU119 4.8 16.0 1.0
C A:ARG118 4.8 21.7 1.0

Aluminium binding site 2 out of 2 in 4ido

Go back to Aluminium Binding Sites List in 4ido
Aluminium binding site 2 out of 2 in the Human Atlastin-1 1-446, C-HIS6, GDPALF4-


Mono view


Stereo pair view

A full contact list of Aluminium with other atoms in the Al binding site number 2 of Human Atlastin-1 1-446, C-HIS6, GDPALF4- within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Al502

b:17.7
occ:1.00
AL B:ALF502 0.0 17.7 1.0
F2 B:ALF502 1.8 22.8 1.0
F3 B:ALF502 1.8 21.2 1.0
F1 B:ALF502 1.8 20.4 1.0
F4 B:ALF502 1.8 21.4 1.0
O3B B:GDP501 2.1 10.6 1.0
O B:HOH789 2.1 12.2 1.0
PB B:GDP501 3.3 16.4 1.0
O2B B:GDP501 3.6 13.8 1.0
MG B:MG503 3.6 17.5 1.0
N B:ARG77 3.8 15.0 1.0
NH2 B:ARG77 3.9 16.3 1.0
O B:HOH601 4.0 18.9 1.0
N B:GLU119 4.0 23.3 1.0
O1B B:GDP501 4.0 27.4 1.0
N B:THR120 4.0 15.2 1.0
NE B:ARG77 4.1 22.8 1.0
N B:GLY149 4.2 17.7 1.0
O B:HOH911 4.2 14.5 1.0
NZ B:LYS80 4.2 11.2 1.0
OG1 B:THR120 4.3 17.8 1.0
CB B:THR120 4.3 21.3 1.0
CB B:PHE76 4.4 21.4 1.0
O B:THR120 4.4 13.8 1.0
CA B:ARG118 4.5 23.0 1.0
O B:HOH938 4.5 15.5 1.0
CA B:PHE76 4.5 16.9 1.0
O3A B:GDP501 4.5 19.4 1.0
CZ B:ARG77 4.5 20.4 1.0
CB B:ARG118 4.6 25.9 1.0
CA B:GLY149 4.6 12.7 1.0
CA B:ARG77 4.6 16.7 1.0
CA B:THR120 4.7 19.1 1.0
C B:PHE76 4.7 19.8 1.0
C B:ARG118 4.8 21.1 1.0
CA B:GLU119 4.8 22.0 1.0
C B:GLU119 4.8 23.9 1.0
O1A B:GDP501 4.9 25.6 1.0
CB B:GLU119 5.0 20.9 1.0

Reference:

L.J.Byrnes, A.Singh, K.Szeto, N.M.Benvin, J.P.O'donnell, W.R.Zipfel, H.Sondermann. Structural Basis For Conformational Switching and Gtp Loading of the Large G Protein Atlastin. Embo J. V. 32 369 2013.
ISSN: ISSN 0261-4189
PubMed: 23334294
DOI: 10.1038/EMBOJ.2012.353
Page generated: Sun Jul 6 21:53:27 2025

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