Aluminium in PDB 5c2k: Crystal Structure of the Fusion Protein Linked By Rhoa and the Gap Domain of Mgcracgap

The structure of Crystal Structure of the Fusion Protein Linked By Rhoa and the Gap Domain of Mgcracgap, PDB code: 5c2k was solved by K.Murayama, M.Kato-Murayama, T.Hosaka, T.Kitamura, S.Yokoyama, M.Shirouzu, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	32.26 / 1.42
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	44.491, 77.041, 62.253, 90.00, 108.53, 90.00
R / Rfree (%)	18.4 / 20.6

The structure of Crystal Structure of the Fusion Protein Linked By Rhoa and the Gap Domain of Mgcracgap also contains other interesting chemical elements:

Fluorine	(F)	3 atoms
Magnesium	(Mg)	1 atom

The binding sites of Aluminium atom in the Crystal Structure of the Fusion Protein Linked By Rhoa and the Gap Domain of Mgcracgap (pdb code 5c2k). This binding sites where shown within 5.0 Angstroms radius around Aluminium atom.
In total only one binding site of Aluminium was determined in the Crystal Structure of the Fusion Protein Linked By Rhoa and the Gap Domain of Mgcracgap, PDB code: 5c2k:

Aluminium binding site 1 out of 1 in the Crystal Structure of the Fusion Protein Linked By Rhoa and the Gap Domain of Mgcracgap


Mono view


Stereo pair view

A full contact list of Aluminium with other atoms in the Al binding site number 1 of Crystal Structure of the Fusion Protein Linked By Rhoa and the Gap Domain of Mgcracgap within 5.0Å range: probe atom residue distance (Å) B Occ A:Al502 b:9.1 occ:1.00 AL A:AF3502 0.0 9.1 1.0 F1 A:AF3502 1.7 11.4 1.0 F2 A:AF3502 1.7 10.1 1.0 F3 A:AF3502 1.8 10.5 1.0 O1B A:GDP503 2.1 11.2 1.0 O A:HOH697 2.2 10.0 1.0 PB A:GDP503 3.4 9.6 1.0 MG A:MG501 3.6 9.6 1.0 O2B A:GDP503 3.8 10.1 1.0 NH2 A:ARG247 3.8 10.3 1.0 N A:ALA15 3.9 9.8 1.0 NE2 A:GLN63 3.9 10.6 1.0 N A:THR37 3.9 10.4 1.0 O A:HOH695 4.0 9.6 1.0 NZ A:LYS18 4.0 9.6 1.0 O3B A:GDP503 4.1 8.8 1.0 CA A:GLY14 4.1 10.2 1.0 OE1 A:GLN63 4.2 10.5 1.0 N A:GLY62 4.2 9.2 1.0 NE A:ARG247 4.2 10.4 1.0 CA A:PRO36 4.2 11.7 1.0 O A:HOH753 4.4 10.4 1.0 CB A:PRO36 4.4 12.5 1.0 CZ A:ARG247 4.5 9.9 1.0 CD A:GLN63 4.5 10.8 1.0 C A:GLY14 4.6 10.2 1.0 O3A A:GDP503 4.6 9.0 1.0 O A:THR37 4.6 10.9 1.0 C A:PRO36 4.6 10.9 1.0 O A:THR60 4.7 10.9 1.0 CA A:ALA61 4.7 11.2 1.0 CB A:THR37 4.7 9.9 1.0 CE A:LYS18 4.7 10.8 1.0 OG1 A:THR37 4.7 10.4 1.0 CA A:THR37 4.9 9.9 1.0 CA A:ALA15 4.9 10.7 1.0 C A:ALA61 5.0 11.4 1.0

K.Murayama, M.Kato-Murayama, T.Hosaka, T.Kawashima, T.Kitamura, S.Yokoyama, M.Shirouzu. Structural Basis of G-Protein Target Alternation of Mgcracgap By Phospholylation To Be Published.