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Aluminium in PDB 2x2f: Dynamin 1 Gtpase Dimer, Short Axis Form

Enzymatic activity of Dynamin 1 Gtpase Dimer, Short Axis Form

All present enzymatic activity of Dynamin 1 Gtpase Dimer, Short Axis Form:
3.6.5.5;

Protein crystallography data

The structure of Dynamin 1 Gtpase Dimer, Short Axis Form, PDB code: 2x2f was solved by J.S.Chappie, S.Acharya, M.Leonard, S.L.Schmid, F.Dyda, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 2.00
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 43.444, 81.274, 175.697, 90.00, 90.00, 90.00
R / Rfree (%) 20 / 25.4

Other elements in 2x2f:

The structure of Dynamin 1 Gtpase Dimer, Short Axis Form also contains other interesting chemical elements:

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

Aluminium Binding Sites:

The binding sites of Aluminium atom in the Dynamin 1 Gtpase Dimer, Short Axis Form (pdb code 2x2f). This binding sites where shown within 5.0 Angstroms radius around Aluminium atom.
In total 2 binding sites of Aluminium where determined in the Dynamin 1 Gtpase Dimer, Short Axis Form, PDB code: 2x2f:
Jump to Aluminium binding site number: 1; 2;

Aluminium binding site 1 out of 2 in 2x2f

Go back to Aluminium Binding Sites List in 2x2f
Aluminium binding site 1 out of 2 in the Dynamin 1 Gtpase Dimer, Short Axis Form


Mono view


Stereo pair view

A full contact list of Aluminium with other atoms in the Al binding site number 1 of Dynamin 1 Gtpase Dimer, Short Axis Form within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Al1748

b:14.3
occ:1.00
AL A:ALF1748 0.0 14.3 1.0
F3 A:ALF1748 1.8 15.9 1.0
F4 A:ALF1748 1.8 16.1 1.0
F1 A:ALF1748 1.8 15.2 1.0
F2 A:ALF1748 1.8 15.3 1.0
O3B A:GDP1747 2.0 7.1 1.0
O A:HOH2027 2.2 13.8 1.0
PB A:GDP1747 3.2 7.8 1.0
NA A:NA1750 3.4 14.6 1.0
MG A:MG1749 3.5 7.9 1.0
O2B A:GDP1747 3.7 6.3 1.0
O1B A:GDP1747 3.7 9.7 1.0
N A:SER41 3.8 7.4 1.0
O A:HOH2171 3.9 7.7 1.0
NZ A:LYS44 4.0 2.1 1.0
N A:THR65 4.1 10.2 1.0
O A:HOH2066 4.1 7.4 1.0
N A:GLY139 4.1 9.7 1.0
O A:HOH2063 4.2 7.6 1.0
N A:VAL64 4.3 11.8 1.0
CB A:THR65 4.3 4.4 1.0
OG1 A:THR65 4.4 6.9 1.0
CA A:SER41 4.4 7.3 1.0
O A:THR65 4.5 9.6 1.0
O3A A:GDP1747 4.5 9.1 1.0
CG A:GLN40 4.6 6.4 1.0
O A:GLY62 4.6 16.2 1.0
CA A:GLN40 4.7 8.6 1.0
CA A:THR65 4.7 6.2 1.0
CA A:GLY139 4.7 10.2 1.0
C A:GLN40 4.8 8.2 1.0
CE A:LYS44 4.8 2.0 1.0
OG A:SER41 4.8 8.7 1.0
O2A A:GDP1747 4.9 6.8 1.0
CA A:VAL64 5.0 10.5 1.0
CB A:VAL64 5.0 10.1 1.0
CA A:PRO138 5.0 10.5 1.0

Aluminium binding site 2 out of 2 in 2x2f

Go back to Aluminium Binding Sites List in 2x2f
Aluminium binding site 2 out of 2 in the Dynamin 1 Gtpase Dimer, Short Axis Form


Mono view


Stereo pair view

A full contact list of Aluminium with other atoms in the Al binding site number 2 of Dynamin 1 Gtpase Dimer, Short Axis Form within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Al1747

b:10.9
occ:1.00
AL D:ALF1747 0.0 10.9 1.0
F1 D:ALF1747 1.8 11.9 1.0
F4 D:ALF1747 1.8 13.6 1.0
F3 D:ALF1747 1.8 14.3 1.0
F2 D:ALF1747 1.8 12.6 1.0
O3B D:GDP1746 2.0 8.0 1.0
O D:HOH2020 2.1 8.2 1.0
PB D:GDP1746 3.2 7.9 1.0
NA D:NA1749 3.3 17.5 1.0
MG D:MG1748 3.6 8.2 1.0
O2B D:GDP1746 3.7 5.6 1.0
O1B D:GDP1746 3.7 8.5 1.0
N D:SER41 3.9 6.9 1.0
O D:HOH2150 3.9 9.8 1.0
O D:HOH2052 3.9 12.4 1.0
NZ D:LYS44 4.0 6.5 1.0
N D:THR65 4.1 7.3 1.0
N D:GLY139 4.1 10.8 1.0
OG1 D:THR65 4.2 10.7 1.0
N D:VAL64 4.2 8.2 1.0
O D:HOH2050 4.2 7.5 1.0
CB D:THR65 4.3 3.3 1.0
O D:THR65 4.5 10.8 1.0
CA D:SER41 4.5 6.7 1.0
O3A D:GDP1746 4.5 7.3 1.0
CG D:GLN40 4.5 3.1 1.0
O D:GLY62 4.6 10.6 1.0
OG D:SER41 4.7 10.6 1.0
CA D:GLN40 4.7 9.0 1.0
CA D:THR65 4.7 7.2 1.0
O2A D:GDP1746 4.8 9.6 1.0
C D:GLN40 4.8 9.6 1.0
CA D:PRO138 4.8 8.6 1.0
CA D:GLY139 4.8 10.3 1.0
CE D:LYS44 4.8 8.2 1.0
C D:PRO138 4.9 10.2 1.0
CA D:VAL64 4.9 6.2 1.0
CA D:ILE63 4.9 9.8 1.0
CB D:VAL64 5.0 5.4 1.0
C D:VAL64 5.0 7.2 1.0

Reference:

J.S.Chappie, S.Acharya, M.Leonard, S.L.Schmid, F.Dyda. G Domain Dimerization Controls Dynamin'S Assembly-Stimulated Gtpase Activity. Nature V. 465 435 2010.
ISSN: ISSN 0028-0836
PubMed: 20428113
DOI: 10.1038/NATURE09032
Page generated: Sat Dec 12 01:31:55 2020

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