Zinc in PDB 1i3o: Crystal Structure of the Complex of Xiap-BIR2 and Caspase 3

The structure of Crystal Structure of the Complex of Xiap-BIR2 and Caspase 3, PDB code: 1i3o was solved by S.J.Riedl, M.Renatus, R.Schwarzenbacher, Q.Zhou, C.Sun, S.W.Fesik, R.C.Liddington, G.S.Salvesen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	500.00 / 2.70
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	70.700, 95.500, 144.200, 90.00, 90.00, 90.00
R / Rfree (%)	24.8 / 27.8

The binding sites of Zinc atom in the Crystal Structure of the Complex of Xiap-BIR2 and Caspase 3 (pdb code 1i3o). 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 Complex of Xiap-BIR2 and Caspase 3, PDB code: 1i3o:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Crystal Structure of the Complex of Xiap-BIR2 and Caspase 3


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 Complex of Xiap-BIR2 and Caspase 3 within 5.0Å range: probe atom residue distance (Å) B Occ E:Zn1 b:46.1 occ:1.00 NE2 E:HIS220 2.2 40.0 1.0 SG E:CYS203 2.3 44.4 1.0 SG E:CYS200 2.3 46.7 1.0 SG E:CYS227 2.4 50.8 1.0 CE1 E:HIS220 2.9 40.0 1.0 CB E:CYS200 3.1 44.0 1.0 CB E:CYS227 3.3 46.8 1.0 CB E:CYS203 3.3 42.4 1.0 CD2 E:HIS220 3.4 40.4 1.0 N E:CYS203 3.7 43.5 1.0 ND1 E:HIS220 4.1 40.0 1.0 CA E:CYS203 4.1 43.0 1.0 CB E:ALA202 4.3 43.8 1.0 CG E:HIS220 4.4 40.6 1.0 CG2 E:VAL230 4.4 46.5 1.0 CA E:CYS200 4.6 42.6 1.0 CA E:CYS227 4.7 45.6 1.0 CB E:PHE224 4.7 40.3 1.0 CB E:PHE229 4.8 39.5 1.0 C E:ALA202 4.8 43.0 1.0 N E:GLY204 4.9 42.0 1.0 C E:CYS203 5.0 42.5 1.0 CA E:ALA202 5.0 43.1 1.0

Zinc binding site 2 out of 2 in the Crystal Structure of the Complex of Xiap-BIR2 and Caspase 3


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 Complex of Xiap-BIR2 and Caspase 3 within 5.0Å range: probe atom residue distance (Å) B Occ F:Zn2 b:59.4 occ:1.00 NE2 F:HIS220 2.0 62.3 1.0 SG F:CYS203 2.4 62.6 1.0 SG F:CYS200 2.4 70.3 1.0 SG F:CYS227 2.5 64.4 1.0 CE1 F:HIS220 2.7 62.5 1.0 CB F:CYS200 3.1 68.3 1.0 CD2 F:HIS220 3.2 62.8 1.0 CB F:CYS227 3.3 60.8 1.0 CB F:CYS203 3.5 62.3 1.0 N F:CYS203 3.9 61.5 1.0 ND1 F:HIS220 3.9 62.9 1.0 CG F:HIS220 4.2 63.5 1.0 CG2 F:VAL230 4.2 60.3 1.0 CA F:CYS203 4.3 62.6 1.0 CB F:ALA202 4.5 58.8 1.0 CA F:CYS200 4.6 67.8 1.0 CB F:PHE224 4.7 56.3 1.0 CA F:CYS227 4.7 60.0 1.0 CB F:PHE229 4.8 63.0 1.0 C F:ALA202 5.0 60.6 1.0

S.J.Riedl, M.Renatus, R.Schwarzenbacher, Q.Zhou, C.Sun, S.W.Fesik, R.C.Liddington, G.S.Salvesen. Structural Basis For the Inhibition of Caspase-3 By Xiap. Cell(Cambridge,Mass.) V. 104 791 2001.
ISSN: ISSN 0092-8674
PubMed: 11257232
DOI: 10.1016/S0092-8674(01)00274-4