Zinc in PDB 1xa6: Crystal Structure of the Human BETA2-Chimaerin

The structure of Crystal Structure of the Human BETA2-Chimaerin, PDB code: 1xa6 was solved by B.Canagarajah, F.C.Leskow, J.Y.Ho, H.Mischak, L.F.Saidi, M.G.Kazanietz, J.H.Hurley, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 3.20
Space group	P 61 2 2
Cell size a, b, c (Å), α, β, γ (°)	131.090, 131.090, 288.750, 90.00, 90.00, 120.00
R / Rfree (%)	25.2 / 29.8

The binding sites of Zinc atom in the Crystal Structure of the Human BETA2-Chimaerin (pdb code 1xa6). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Crystal Structure of the Human BETA2-Chimaerin, PDB code: 1xa6:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Crystal Structure of the Human BETA2-Chimaerin


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of the Human BETA2-Chimaerin within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn467 b:86.7 occ:1.00 ND1 A:HIS213 2.3 64.5 1.0 CE1 A:HIS213 2.5 59.6 1.0 CB A:CYS246 2.6 73.2 1.0 SG A:CYS243 2.6 83.2 1.0 SG A:CYS262 2.6 0.9 1.0 SG A:CYS246 2.6 79.9 1.0 N A:CYS246 3.2 76.9 1.0 CG A:HIS213 3.3 99.3 1.0 CB A:CYS262 3.3 90.2 1.0 CA A:CYS246 3.5 76.1 1.0 NE2 A:HIS213 3.5 70.6 1.0 CB A:CYS243 3.6 59.0 1.0 CD2 A:HIS213 3.9 88.5 1.0 CB A:HIS213 4.1 0.5 1.0 CA A:HIS213 4.2 0.7 1.0 CA A:CYS262 4.4 0.5 1.0 C A:CYS246 4.4 76.8 1.0 C A:ASP245 4.4 96.5 1.0 CB A:ASP245 4.6 0.1 1.0 N A:GLY247 4.8 79.2 1.0 N A:ASN214 4.9 0.3 1.0 CA A:ASP245 4.9 0.1 1.0 O A:THR212 4.9 0.1 1.0 N A:ASP245 5.0 0.9 1.0 C A:CYS262 5.0 0.6 1.0

Zinc binding site 2 out of 2 in the Crystal Structure of the Human BETA2-Chimaerin


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure of the Human BETA2-Chimaerin within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn468 b:62.2 occ:1.00 SG A:CYS226 2.4 49.3 1.0 ND1 A:HIS251 2.5 74.9 1.0 SG A:CYS229 2.5 85.4 1.0 SG A:CYS254 2.6 74.6 1.0 CB A:CYS226 2.7 55.8 1.0 CG A:HIS251 3.0 66.9 1.0 CB A:CYS229 3.0 85.7 1.0 CE1 A:HIS251 3.1 81.1 1.0 N A:CYS229 3.4 49.8 1.0 CB A:HIS251 3.5 59.5 1.0 CA A:CYS229 3.7 58.1 1.0 CD2 A:HIS251 3.8 72.9 1.0 NE2 A:HIS251 3.9 57.9 1.0 CB A:CYS254 3.9 90.0 1.0 N A:HIS251 4.2 79.7 1.0 CA A:CYS226 4.2 52.2 1.0 C A:CYS229 4.3 60.4 1.0 CB A:TYR228 4.5 81.0 1.0 CA A:HIS251 4.5 84.6 1.0 N A:ALA230 4.6 62.0 1.0 C A:TYR228 4.6 61.4 1.0 N A:ASN231 4.7 78.2 1.0 O A:CYS226 4.8 47.3 1.0 C A:CYS226 4.8 59.1 1.0 O A:ASN231 4.9 71.5 1.0 CD2 A:TYR228 5.0 93.5 1.0 O A:CYS229 5.0 59.2 1.0 CA A:TYR228 5.0 57.6 1.0 CB A:ASN231 5.0 33.4 1.0 N A:CYS226 5.0 41.2 1.0

B.Canagarajah, F.C.Leskow, J.Y.Ho, H.Mischak, L.F.Saidi, M.G.Kazanietz, J.H.Hurley. Structural Mechanism For Lipid Activation of the Rac-Specific Gap, BETA2-Chimaerin. Cell(Cambridge,Mass.) V. 119 407 2004.
ISSN: ISSN 0092-8674
PubMed: 15507211
DOI: 10.1016/J.CELL.2004.10.012