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Aluminium in PDB 3zq6: Adp-ALF4 Complex of M. Therm. TRC40

Enzymatic activity of Adp-ALF4 Complex of M. Therm. TRC40

All present enzymatic activity of Adp-ALF4 Complex of M. Therm. TRC40:
3.6.3.16;

Protein crystallography data

The structure of Adp-ALF4 Complex of M. Therm. TRC40, PDB code: 3zq6 was solved by J.Sherrill, M.Mariappan, P.Dominik, R.S.Hegde, R.J.Keenan, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 41.206 / 2.11
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 206.948, 49.768, 147.363, 90.00, 115.04, 90.00
R / Rfree (%) 17.3 / 22.14

Other elements in 3zq6:

The structure of Adp-ALF4 Complex of M. Therm. TRC40 also contains other interesting chemical elements:

Fluorine (F) 16 atoms
Magnesium (Mg) 4 atoms
Potassium (K) 4 atoms
Zinc (Zn) 2 atoms

Aluminium Binding Sites:

The binding sites of Aluminium atom in the Adp-ALF4 Complex of M. Therm. TRC40 (pdb code 3zq6). This binding sites where shown within 5.0 Angstroms radius around Aluminium atom.
In total 4 binding sites of Aluminium where determined in the Adp-ALF4 Complex of M. Therm. TRC40, PDB code: 3zq6:
Jump to Aluminium binding site number: 1; 2; 3; 4;

Aluminium binding site 1 out of 4 in 3zq6

Go back to Aluminium Binding Sites List in 3zq6
Aluminium binding site 1 out of 4 in the Adp-ALF4 Complex of M. Therm. TRC40


Mono view


Stereo pair view

A full contact list of Aluminium with other atoms in the Al binding site number 1 of Adp-ALF4 Complex of M. Therm. TRC40 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Al402

b:16.4
occ:1.00
AL A:ALF402 0.0 16.4 1.0
F4 A:ALF402 1.7 18.6 1.0
F1 A:ALF402 1.7 19.7 1.0
F3 A:ALF402 1.8 17.3 1.0
F2 A:ALF402 1.8 18.2 1.0
O1B A:ADP401 1.9 14.6 1.0
O A:HOH2030 2.0 15.1 1.0
PB A:ADP401 3.2 15.4 1.0
MG A:MG403 3.4 17.5 1.0
O A:HOH4003 3.6 16.8 1.0
O2B A:ADP401 3.7 15.2 1.0
NZ B:LYS22 3.8 18.5 1.0
N A:GLY24 3.9 12.6 1.0
K A:K404 3.9 23.1 1.0
OD2 A:ASP51 3.9 18.1 1.0
O3B A:ADP401 4.0 17.6 1.0
NZ A:LYS27 4.0 14.9 1.0
O B:HOH2016 4.0 20.1 1.0
O A:HOH4002 4.0 13.1 1.0
CG A:PRO148 4.2 14.5 1.0
O3A A:ADP401 4.3 14.8 1.0
N B:GLY23 4.3 16.5 1.0
CA B:GLY23 4.5 14.5 1.0
CE A:LYS27 4.5 13.7 1.0
CE B:LYS22 4.5 12.0 1.0
CD A:PRO148 4.6 15.5 1.0
CA A:GLY24 4.6 9.8 1.0
CG B:LYS22 4.6 17.2 1.0
O A:HOH4001 4.6 18.4 1.0
CA A:GLY23 4.6 10.5 1.0
C A:GLY23 4.8 17.0 1.0
O2A A:ADP401 4.9 16.1 1.0

Aluminium binding site 2 out of 4 in 3zq6

Go back to Aluminium Binding Sites List in 3zq6
Aluminium binding site 2 out of 4 in the Adp-ALF4 Complex of M. Therm. TRC40


Mono view


Stereo pair view

A full contact list of Aluminium with other atoms in the Al binding site number 2 of Adp-ALF4 Complex of M. Therm. TRC40 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Al402

b:17.1
occ:1.00
AL B:ALF402 0.0 17.1 1.0
F4 B:ALF402 1.8 20.3 1.0
F2 B:ALF402 1.8 18.6 1.0
F1 B:ALF402 1.8 19.2 1.0
F3 B:ALF402 1.8 19.2 1.0
O1B B:ADP401 1.9 11.9 1.0
O B:HOH2027 2.0 11.1 1.0
PB B:ADP401 3.2 15.1 1.0
MG B:MG403 3.4 17.6 1.0
O B:HOH4003 3.6 17.0 1.0
NZ A:LYS22 3.6 16.8 1.0
O2B B:ADP401 3.6 13.8 1.0
N B:GLY24 3.8 15.6 1.0
K B:K404 3.9 22.9 1.0
O3B B:ADP401 3.9 16.1 1.0
OD2 B:ASP51 4.0 25.2 1.0
O A:HOH2017 4.0 17.4 1.0
NZ B:LYS27 4.0 18.1 1.0
O B:HOH4002 4.1 16.3 1.0
CE A:LYS22 4.3 22.4 1.0
O3A B:ADP401 4.3 17.4 1.0
N A:GLY23 4.4 12.3 1.0
CA A:GLY23 4.4 10.5 1.0
CG B:PRO148 4.4 21.4 1.0
CG A:LYS22 4.5 16.8 1.0
CE B:LYS27 4.5 14.1 1.0
CA B:GLY24 4.6 10.2 1.0
CA B:GLY23 4.6 14.5 1.0
O B:HOH4001 4.7 17.8 1.0
C B:GLY23 4.7 18.8 1.0
O2A B:ADP401 4.8 13.9 1.0
CD B:PRO148 4.8 17.9 1.0

Aluminium binding site 3 out of 4 in 3zq6

Go back to Aluminium Binding Sites List in 3zq6
Aluminium binding site 3 out of 4 in the Adp-ALF4 Complex of M. Therm. TRC40


Mono view


Stereo pair view

A full contact list of Aluminium with other atoms in the Al binding site number 3 of Adp-ALF4 Complex of M. Therm. TRC40 within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Al402

b:29.9
occ:1.00
AL C:ALF402 0.0 29.9 1.0
F4 C:ALF402 1.8 35.2 1.0
F2 C:ALF402 1.8 27.9 1.0
F3 C:ALF402 1.8 28.2 1.0
F1 C:ALF402 1.8 36.3 1.0
O1B C:ADP401 1.9 27.7 1.0
O C:HOH2019 2.0 28.6 1.0
PB C:ADP401 3.2 28.0 1.0
MG C:MG403 3.4 31.8 1.0
O C:HOH4003 3.6 39.2 1.0
O2B C:ADP401 3.6 24.4 1.0
NZ D:LYS22 3.8 38.6 1.0
O3B C:ADP401 3.8 33.6 1.0
N C:GLY24 3.9 32.8 1.0
K C:K404 3.9 40.1 1.0
NZ C:LYS27 4.0 27.6 1.0
OD2 C:ASP51 4.0 34.5 1.0
O D:HOH2022 4.1 30.5 1.0
O C:HOH4002 4.1 31.6 1.0
CG C:PRO148 4.3 37.1 1.0
O3A C:ADP401 4.3 34.6 1.0
N D:GLY23 4.4 33.9 1.0
CA D:GLY23 4.4 34.2 1.0
CA C:GLY24 4.5 30.9 1.0
CE D:LYS22 4.5 37.3 1.0
CG D:LYS22 4.6 28.9 1.0
O C:HOH4001 4.6 31.6 1.0
CE C:LYS27 4.6 29.1 1.0
CD C:PRO148 4.7 35.7 1.0
O2A C:ADP401 4.8 30.6 1.0
CA C:GLY23 4.8 25.9 1.0
C C:GLY23 4.8 33.4 1.0

Aluminium binding site 4 out of 4 in 3zq6

Go back to Aluminium Binding Sites List in 3zq6
Aluminium binding site 4 out of 4 in the Adp-ALF4 Complex of M. Therm. TRC40


Mono view


Stereo pair view

A full contact list of Aluminium with other atoms in the Al binding site number 4 of Adp-ALF4 Complex of M. Therm. TRC40 within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Al402

b:33.7
occ:1.00
AL D:ALF402 0.0 33.7 1.0
F4 D:ALF402 1.8 35.8 1.0
F1 D:ALF402 1.8 33.1 1.0
F3 D:ALF402 1.8 36.9 1.0
F2 D:ALF402 1.8 42.9 1.0
O1B D:ADP401 1.9 23.5 1.0
O D:HOH2010 2.0 27.6 1.0
PB D:ADP401 3.2 34.9 1.0
O D:HOH4003 3.3 32.8 1.0
MG D:MG403 3.4 33.1 1.0
NZ C:LYS22 3.6 31.4 1.0
O2B D:ADP401 3.6 30.1 1.0
N D:GLY24 3.8 34.0 1.0
O3B D:ADP401 3.9 36.7 1.0
K D:K404 3.9 38.1 1.0
OD2 D:ASP51 4.0 30.4 1.0
NZ D:LYS27 4.0 35.6 1.0
O C:HOH2010 4.1 30.1 1.0
O3A D:ADP401 4.2 37.6 1.0
O D:HOH4002 4.2 37.9 1.0
CA C:GLY23 4.3 25.9 1.0
N C:GLY23 4.3 32.2 1.0
CE C:LYS22 4.4 31.6 1.0
CA D:GLY24 4.5 37.1 1.0
CG D:PRO148 4.5 33.2 1.0
CE D:LYS27 4.6 37.5 1.0
CG C:LYS22 4.6 31.8 1.0
O D:HOH4001 4.7 31.6 1.0
CA D:GLY23 4.7 34.2 1.0
C D:GLY23 4.8 32.2 1.0
O2A D:ADP401 4.8 39.3 1.0
CD D:PRO148 4.9 39.9 1.0

Reference:

J.Sherrill, M.Mariappan, P.Dominik, R.S.Hegde, R.J.Keenan. A Conserved Archaeal Pathway For Tail-Anchored Membrane Protein Insertion. Traffic V. 12 1119 2011.
ISSN: ISSN 1398-9219
PubMed: 21658170
DOI: 10.1111/J.1600-0854.2011.01229.X
Page generated: Wed Jul 10 09:43:01 2024

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