Zinc in PDB 2i3h: Structure of An Ml-Iap/Xiap Chimera Bound to A 4-Mer Peptide (Avpw)

The structure of Structure of An Ml-Iap/Xiap Chimera Bound to A 4-Mer Peptide (Avpw), PDB code: 2i3h was solved by W.J.Fairbrother, M.C.Franklin, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 1.62
Space group	P 41 21 2
Cell size a, b, c (Å), α, β, γ (°)	87.541, 87.541, 73.876, 90.00, 90.00, 90.00
R / Rfree (%)	16.1 / 18

The binding sites of Zinc atom in the Structure of An Ml-Iap/Xiap Chimera Bound to A 4-Mer Peptide (Avpw) (pdb code 2i3h). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Structure of An Ml-Iap/Xiap Chimera Bound to A 4-Mer Peptide (Avpw), PDB code: 2i3h:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Structure of An Ml-Iap/Xiap Chimera Bound to A 4-Mer Peptide (Avpw)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structure of An Ml-Iap/Xiap Chimera Bound to A 4-Mer Peptide (Avpw) within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1001 b:6.8 occ:1.00 NE2 A:HIS144 2.1 5.4 1.0 SG A:CYS151 2.3 5.9 1.0 SG A:CYS127 2.3 6.7 1.0 SG A:CYS124 2.3 6.5 1.0 CE1 A:HIS144 2.9 7.2 1.0 CB A:CYS124 3.2 5.8 1.0 CB A:CYS151 3.2 7.3 1.0 CD2 A:HIS144 3.2 6.7 1.0 CB A:CYS127 3.3 5.4 1.0 N A:CYS127 3.7 4.6 1.0 ND1 A:HIS144 4.1 6.1 1.0 CA A:CYS127 4.1 5.0 1.0 CG A:HIS144 4.3 6.1 1.0 CA A:CYS151 4.5 7.3 1.0 CB A:PHE126 4.6 6.1 1.0 CA A:CYS124 4.6 4.9 1.0 C A:PHE126 4.8 5.2 1.0 CB A:PHE148 4.9 7.6 1.0 C A:CYS127 4.9 4.7 1.0 N A:PHE126 5.0 5.1 1.0 CA A:PHE126 5.0 5.0 1.0

Zinc binding site 2 out of 2 in the Structure of An Ml-Iap/Xiap Chimera Bound to A 4-Mer Peptide (Avpw)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Structure of An Ml-Iap/Xiap Chimera Bound to A 4-Mer Peptide (Avpw) within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn1001 b:6.8 occ:1.00 NE2 B:HIS144 2.1 9.2 1.0 SG B:CYS151 2.3 6.7 1.0 SG B:CYS127 2.3 6.2 1.0 SG B:CYS124 2.3 6.3 1.0 CE1 B:HIS144 2.9 10.2 1.0 CB B:CYS124 3.1 6.0 1.0 CB B:CYS151 3.2 5.7 1.0 CB B:CYS127 3.3 6.3 1.0 CD2 B:HIS144 3.3 11.1 1.0 N B:CYS127 3.8 5.7 1.0 ND1 B:HIS144 4.1 11.2 1.0 CA B:CYS127 4.1 5.9 1.0 CG B:HIS144 4.3 9.1 1.0 CA B:CYS151 4.5 6.5 1.0 CA B:CYS124 4.6 5.3 1.0 CB B:PHE126 4.8 6.6 1.0 C B:PHE126 4.9 5.5 1.0 CB B:PHE148 4.9 6.4 1.0 C B:CYS127 4.9 5.5 1.0 CB B:PHE153 5.0 6.2 1.0

K.Zobel, L.Wang, E.Varfolomeev, M.C.Franklin, L.O.Elliott, H.J.Wallweber, D.C.Okawa, J.A.Flygare, D.Vucic, W.J.Fairbrother, K.Deshayes. Design, Synthesis, and Biological Activity of A Potent Smac Mimetic That Sensitizes Cancer Cells to Apoptosis By Antagonizing Iaps. Acs Chem.Biol. V. 1 525 2006.
ISSN: ISSN 1554-8929
PubMed: 17168540
DOI: 10.1021/CB600276Q