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

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

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

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

Fluorine	(F)	8 atoms
Aluminium	(Al)	2 atoms
Sodium	(Na)	2 atoms

The binding sites of Magnesium atom in the Dynamin Gtpase Dimer, Long Axis Form (pdb code 2x2e). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Dynamin Gtpase Dimer, Long Axis Form, PDB code: 2x2e:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Dynamin Gtpase Dimer, Long Axis Form


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Dynamin Gtpase Dimer, Long Axis Form within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg1746 b:5.7 occ:1.00 F4 A:ALF1745 1.9 15.3 1.0 OG A:SER45 1.9 3.1 1.0 O1B A:GDP1744 2.0 3.8 1.0 O A:HOH2331 2.1 5.6 1.0 OG1 A:THR65 2.1 3.2 1.0 O A:HOH2139 2.1 6.0 1.0 CB A:SER45 3.1 3.4 1.0 CB A:THR65 3.1 1.0 1.0 PB A:GDP1744 3.1 4.0 1.0 O3B A:GDP1744 3.4 4.0 1.0 AL A:ALF1745 3.5 15.0 1.0 F1 A:ALF1745 3.7 15.4 1.0 N A:SER45 3.8 2.4 1.0 OD2 A:ASP136 3.9 8.5 1.0 CA A:SER45 4.0 4.4 1.0 CG2 A:THR65 4.1 2.8 1.0 OD1 A:ASP136 4.1 7.2 1.0 N A:THR65 4.1 4.2 1.0 O A:HOH2072 4.1 4.2 1.0 O2B A:GDP1744 4.2 4.0 1.0 CA A:THR65 4.2 1.7 1.0 O2A A:GDP1744 4.2 5.9 1.0 F2 A:ALF1745 4.2 15.0 1.0 O3A A:GDP1744 4.4 4.7 1.0 CG A:ASP136 4.4 8.0 1.0 O A:PRO58 4.6 9.7 1.0 O A:HOH2071 4.6 15.1 1.0 O A:LEU137 4.6 7.2 1.0 PA A:GDP1744 4.6 5.5 1.0 O1A A:GDP1744 4.8 6.0 1.0 C A:LYS44 4.9 3.9 1.0 CB A:LYS44 5.0 4.2 1.0

Magnesium binding site 2 out of 2 in the Dynamin Gtpase Dimer, Long Axis Form


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Dynamin Gtpase Dimer, Long Axis Form within 5.0Å range: probe atom residue distance (Å) B Occ D:Mg1746 b:4.7 occ:1.00 F4 D:ALF1745 1.9 12.8 1.0 O1B D:GDP1744 2.0 7.0 1.0 O D:HOH2115 2.0 4.7 1.0 O D:HOH2287 2.1 4.4 1.0 OG D:SER45 2.1 4.1 1.0 OG1 D:THR65 2.1 4.0 1.0 PB D:GDP1744 3.1 6.5 1.0 CB D:SER45 3.1 4.2 1.0 CB D:THR65 3.2 2.5 1.0 O3B D:GDP1744 3.4 6.7 1.0 AL D:ALF1745 3.5 12.2 1.0 F1 D:ALF1745 3.7 12.8 1.0 N D:SER45 3.7 4.9 1.0 OD1 D:ASP136 4.0 12.6 1.0 OD2 D:ASP136 4.0 5.3 1.0 CA D:SER45 4.0 4.7 1.0 O2B D:GDP1744 4.1 6.6 1.0 N D:THR65 4.1 5.2 1.0 CG2 D:THR65 4.2 1.0 1.0 O2A D:GDP1744 4.2 7.1 1.0 O D:HOH2050 4.2 7.7 1.0 CA D:THR65 4.2 7.2 1.0 F2 D:ALF1745 4.3 12.0 1.0 O3A D:GDP1744 4.3 6.2 1.0 CG D:ASP136 4.3 10.3 1.0 O D:PRO58 4.5 4.8 1.0 O D:LEU137 4.6 7.8 1.0 PA D:GDP1744 4.6 6.7 1.0 O D:HOH2051 4.6 12.3 1.0 O1A D:GDP1744 4.8 7.2 1.0 C D:LYS44 4.8 5.8 1.0 CB D:LYS44 4.9 3.8 1.0

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