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Aluminium in PDB 2x2e: Dynamin Gtpase Dimer, Long Axis Form

Enzymatic activity of Dynamin Gtpase Dimer, Long Axis Form

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

Protein crystallography data

The structure of Dynamin Gtpase Dimer, Long Axis Form, PDB code: 2x2e 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 (°) 43.610, 81.020, 181.540, 90.00, 90.00, 90.00
R / Rfree (%) 18.5 / 23

Other elements in 2x2e:

The structure of Dynamin Gtpase Dimer, Long 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 Gtpase Dimer, Long Axis Form (pdb code 2x2e). 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 Gtpase Dimer, Long Axis Form, PDB code: 2x2e:
Jump to Aluminium binding site number: 1; 2;

Aluminium binding site 1 out of 2 in 2x2e

Go back to Aluminium Binding Sites List in 2x2e
Aluminium binding site 1 out of 2 in the Dynamin Gtpase Dimer, Long 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 Gtpase Dimer, Long Axis Form within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Al1745

b:15.0
occ:1.00
AL A:ALF1745 0.0 15.0 1.0
F3 A:ALF1745 1.8 15.6 1.0
F4 A:ALF1745 1.8 15.3 1.0
F1 A:ALF1745 1.8 15.4 1.0
F2 A:ALF1745 1.8 15.0 1.0
O3B A:GDP1744 2.0 4.0 1.0
O A:HOH2071 2.1 15.1 1.0
PB A:GDP1744 3.2 4.0 1.0
NA A:NA1747 3.3 8.6 1.0
MG A:MG1746 3.5 5.7 1.0
O2B A:GDP1744 3.7 4.0 1.0
O1B A:GDP1744 3.7 3.8 1.0
O A:HOH2331 3.8 5.6 1.0
N A:SER41 3.9 5.0 1.0
N A:THR65 4.0 4.2 1.0
O A:HOH2141 4.1 7.1 1.0
N A:VAL64 4.1 5.3 1.0
O A:HOH2139 4.1 6.0 1.0
NZ A:LYS44 4.2 2.7 1.0
N A:GLY139 4.2 4.4 1.0
OG1 A:THR65 4.3 3.2 1.0
CB A:THR65 4.3 1.0 1.0
O A:THR65 4.5 6.1 1.0
CA A:SER41 4.5 6.3 1.0
O A:GLY62 4.5 10.6 1.0
CG A:GLN40 4.5 2.7 1.0
O3A A:GDP1744 4.5 4.7 1.0
CA A:THR65 4.7 1.7 1.0
OG A:SER41 4.7 4.7 1.0
CA A:GLN40 4.8 3.4 1.0
O2A A:GDP1744 4.8 5.9 1.0
CA A:VAL64 4.9 3.7 1.0
CA A:PRO138 4.9 5.2 1.0
C A:VAL64 4.9 4.1 1.0
CB A:VAL64 4.9 4.2 1.0
C A:GLN40 4.9 3.9 1.0
CA A:GLY139 4.9 5.3 1.0
CA A:ILE63 5.0 8.6 1.0
CE A:LYS44 5.0 2.9 1.0

Aluminium binding site 2 out of 2 in 2x2e

Go back to Aluminium Binding Sites List in 2x2e
Aluminium binding site 2 out of 2 in the Dynamin Gtpase Dimer, Long 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 Gtpase Dimer, Long Axis Form within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Al1745

b:12.2
occ:1.00
AL D:ALF1745 0.0 12.2 1.0
F3 D:ALF1745 1.8 13.1 1.0
F1 D:ALF1745 1.8 12.8 1.0
F4 D:ALF1745 1.8 12.8 1.0
F2 D:ALF1745 1.8 12.0 1.0
O3B D:GDP1744 2.0 6.7 1.0
O D:HOH2051 2.1 12.3 1.0
PB D:GDP1744 3.2 6.5 1.0
NA D:NA1747 3.3 9.2 1.0
MG D:MG1746 3.5 4.7 1.0
O1B D:GDP1744 3.7 7.0 1.0
O2B D:GDP1744 3.7 6.6 1.0
O D:HOH2287 3.8 4.4 1.0
N D:SER41 3.8 4.2 1.0
O D:HOH2117 4.0 10.5 1.0
N D:THR65 4.1 5.2 1.0
N D:GLY139 4.1 6.8 1.0
NZ D:LYS44 4.2 1.0 1.0
N D:VAL64 4.2 7.0 1.0
OG1 D:THR65 4.3 4.0 1.0
CB D:THR65 4.3 2.5 1.0
O D:HOH2115 4.3 4.7 1.0
CA D:SER41 4.4 3.3 1.0
O D:GLY62 4.6 6.2 1.0
O D:THR65 4.6 7.0 1.0
O3A D:GDP1744 4.6 6.2 1.0
CG D:GLN40 4.6 5.7 1.0
OG D:SER41 4.7 7.2 1.0
CA D:THR65 4.7 7.2 1.0
CA D:GLY139 4.8 5.3 1.0
CA D:GLN40 4.8 3.9 1.0
C D:GLN40 4.8 5.1 1.0
CB D:VAL64 4.8 5.3 1.0
O2A D:GDP1744 4.9 7.1 1.0
CA D:PRO138 4.9 7.5 1.0
CA D:VAL64 4.9 5.9 1.0
C D:VAL64 4.9 6.6 1.0
CE D:LYS44 5.0 1.6 1.0
C D:PRO138 5.0 7.6 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: Wed Jul 10 09:33:36 2024

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