Zinc in PDB 1tw6: Structure of An Ml-Iap/Xiap Chimera Bound to A 9MER Peptide Derived From Smac

The structure of Structure of An Ml-Iap/Xiap Chimera Bound to A 9MER Peptide Derived From Smac, PDB code: 1tw6 was solved by M.C.Franklin, D.Vucic, H.J.A.Wallweber, K.Das, H.Shin, L.O.Elliott, S.Kadkhodayan, K.Deshayes, G.S.Salvesen, W.J.Fairbrother, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	47.75 / 1.71
Space group	P 41 21 2
Cell size a, b, c (Å), α, β, γ (°)	87.856, 87.856, 74.634, 90.00, 90.00, 90.00
R / Rfree (%)	15.5 / 17.1

The binding sites of Zinc atom in the Structure of An Ml-Iap/Xiap Chimera Bound to A 9MER Peptide Derived From Smac (pdb code 1tw6). 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 9MER Peptide Derived From Smac, PDB code: 1tw6:
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 9MER Peptide Derived From Smac


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 9MER Peptide Derived From Smac within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1001 b:8.9 occ:1.00 NE2 A:HIS144 2.1 6.9 1.0 SG A:CYS151 2.3 8.4 1.0 SG A:CYS127 2.3 8.3 1.0 SG A:CYS124 2.3 8.9 1.0 CE1 A:HIS144 2.9 9.2 1.0 CB A:CYS124 3.2 9.4 1.0 CB A:CYS151 3.2 8.0 1.0 CD2 A:HIS144 3.2 8.3 1.0 CB A:CYS127 3.3 8.5 1.0 N A:CYS127 3.7 6.4 1.0 CA A:CYS127 4.1 6.9 1.0 ND1 A:HIS144 4.1 8.4 1.0 CG A:HIS144 4.3 7.0 1.0 CA A:CYS151 4.5 7.4 1.0 CB A:PHE126 4.6 8.5 1.0 CA A:CYS124 4.6 8.2 1.0 C A:PHE126 4.8 7.3 1.0 CB A:PHE148 4.9 8.9 1.0 C A:CYS127 4.9 6.0 1.0 N A:PHE126 5.0 6.9 1.0

Zinc binding site 2 out of 2 in the Structure of An Ml-Iap/Xiap Chimera Bound to A 9MER Peptide Derived From Smac


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 9MER Peptide Derived From Smac within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn1001 b:8.6 occ:1.00 NE2 B:HIS144 2.1 7.6 1.0 SG B:CYS151 2.3 7.8 1.0 SG B:CYS127 2.3 8.6 1.0 SG B:CYS124 2.3 7.7 1.0 CE1 B:HIS144 2.9 9.9 1.0 CB B:CYS124 3.1 8.6 1.0 CB B:CYS151 3.2 6.2 1.0 CD2 B:HIS144 3.2 8.4 1.0 CB B:CYS127 3.3 8.7 1.0 N B:CYS127 3.8 8.0 1.0 CA B:CYS127 4.1 9.0 1.0 ND1 B:HIS144 4.1 9.3 1.0 CG B:HIS144 4.3 8.8 1.0 CA B:CYS151 4.5 7.0 1.0 CA B:CYS124 4.6 7.0 1.0 CB B:PHE126 4.8 7.0 1.0 CB B:PHE148 4.8 8.6 1.0 C B:PHE126 4.9 6.5 1.0 C B:CYS127 4.9 7.8 1.0 CB B:PHE153 5.0 7.5 1.0

D.Vucic, M.C.Franklin, H.J.A.Wallweber, K.Das, B.P.Eckelman, H.Shin, L.O.Elliott, S.Kadkhodayan, K.Deshayes, G.S.Salvesen, W.J.Fairbrother. Engineering Ml-Iap to Produce An Extraordinarily Potent Caspase 9 Inhibitor: Implications For Smac-Dependent Anti-Apoptotic Activity of Ml-Iap Biochem.J. V. 385 11 2005.
ISSN: ISSN 0264-6021
PubMed: 15485396
DOI: 10.1042/BJ20041108