Zinc in PDB 3t6p: Iap Antagonist-Induced Conformational Change in CIAP1 Promotes E3 Ligase Activation Via Dimerization

The structure of Iap Antagonist-Induced Conformational Change in CIAP1 Promotes E3 Ligase Activation Via Dimerization, PDB code: 3t6p was solved by E.C.Dueber, A.J.Schoeffler, A.Lingel, M.Elliott, A.V.Fedorova, A.M.Giannetti, K.Zobel, B.Maurer, E.Varfolomeev, P.Wu, H.Wallweber, S.Hymowitz, K.Deshayes, D.Vucic, W.J.Fairbrother, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	32.78 / 1.90
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	37.971, 85.432, 106.484, 90.00, 90.00, 90.00
R / Rfree (%)	19.1 / 23.3

The binding sites of Zinc atom in the Iap Antagonist-Induced Conformational Change in CIAP1 Promotes E3 Ligase Activation Via Dimerization (pdb code 3t6p). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 3 binding sites of Zinc where determined in the Iap Antagonist-Induced Conformational Change in CIAP1 Promotes E3 Ligase Activation Via Dimerization, PDB code: 3t6p:
Jump to Zinc binding site number: 1; 2; 3;

Zinc binding site 1 out of 3 in the Iap Antagonist-Induced Conformational Change in CIAP1 Promotes E3 Ligase Activation Via Dimerization


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Iap Antagonist-Induced Conformational Change in CIAP1 Promotes E3 Ligase Activation Via Dimerization within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1001 b:31.5 occ:1.00 SG A:CYS571 2.4 26.3 1.0 SG A:CYS592 2.4 29.2 1.0 SG A:CYS595 2.4 34.2 1.0 SG A:CYS574 2.4 33.6 1.0 CB A:CYS571 3.1 24.2 1.0 CB A:CYS595 3.1 32.2 1.0 CB A:CYS574 3.2 42.6 1.0 CB A:CYS592 3.6 26.9 1.0 N A:CYS574 3.6 27.3 1.0 N A:CYS592 4.0 30.6 1.0 CA A:CYS574 4.0 37.9 1.0 O A:HOH195 4.1 53.7 1.0 N A:CYS595 4.2 35.9 1.0 CA A:CYS595 4.3 29.8 1.0 CA A:CYS592 4.3 29.2 1.0 CA A:CYS571 4.6 23.3 1.0 CB A:VAL573 4.6 36.6 1.0 C A:VAL573 4.7 39.5 1.0 C A:CYS592 4.8 34.6 1.0 O A:CYS592 4.8 26.2 1.0 CB A:LYS577 4.9 33.7 1.0 C A:CYS574 4.9 36.7 1.0 C A:CYS571 5.0 27.4 1.0

Zinc binding site 2 out of 3 in the Iap Antagonist-Induced Conformational Change in CIAP1 Promotes E3 Ligase Activation Via Dimerization


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Iap Antagonist-Induced Conformational Change in CIAP1 Promotes E3 Ligase Activation Via Dimerization within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1002 b:25.2 occ:1.00 NE2 A:HIS326 2.2 27.2 1.0 SG A:CYS306 2.3 23.8 1.0 SG A:CYS333 2.3 24.0 1.0 SG A:CYS309 2.4 25.9 1.0 CE1 A:HIS326 2.8 35.1 1.0 CB A:CYS333 3.1 25.2 1.0 CB A:CYS306 3.1 25.3 1.0 CB A:CYS309 3.2 29.1 1.0 CD2 A:HIS326 3.4 29.3 1.0 N A:CYS309 3.6 29.0 1.0 CA A:CYS309 4.0 33.0 1.0 ND1 A:HIS326 4.1 28.4 1.0 CG A:HIS326 4.3 27.8 1.0 CB A:SER308 4.4 27.7 1.0 CA A:CYS333 4.5 26.6 1.0 CA A:CYS306 4.6 27.1 1.0 C A:SER308 4.7 36.6 1.0 CB A:PHE330 4.8 23.4 1.0 C A:CYS309 4.8 31.0 1.0 N A:SER308 4.9 29.0 1.0 CA A:SER308 4.9 35.4 1.0 N A:ASP310 5.0 36.3 1.0

Zinc binding site 3 out of 3 in the Iap Antagonist-Induced Conformational Change in CIAP1 Promotes E3 Ligase Activation Via Dimerization


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Iap Antagonist-Induced Conformational Change in CIAP1 Promotes E3 Ligase Activation Via Dimerization within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1003 b:30.9 occ:1.00 ND1 A:HIS588 2.1 31.7 1.0 SG A:CYS602 2.1 28.7 1.0 SG A:CYS586 2.4 31.7 1.0 SG A:CYS605 2.4 35.6 1.0 CB A:CYS602 3.0 23.5 1.0 CE1 A:HIS588 3.1 41.4 1.0 CG A:HIS588 3.2 27.9 1.0 CB A:CYS586 3.2 33.8 1.0 CB A:HIS588 3.5 27.1 1.0 CB A:CYS605 3.5 41.5 1.0 N A:CYS605 3.9 36.5 1.0 NE2 A:HIS588 4.2 36.9 1.0 CD2 A:HIS588 4.2 36.5 1.0 CA A:CYS605 4.3 34.8 1.0 CA A:CYS602 4.4 27.9 1.0 CB A:ILE604 4.5 35.1 1.0 CA A:CYS586 4.6 37.8 1.0 N A:HIS588 4.6 28.0 1.0 CA A:HIS588 4.7 27.4 1.0 CD2 A:PHE583 4.7 28.6 1.0 C A:CYS586 4.8 36.6 1.0 C A:ILE604 4.9 43.1 1.0 O A:CYS586 4.9 33.7 1.0 C A:CYS602 5.0 35.8 1.0 C A:CYS605 5.0 32.2 1.0

E.C.Dueber, A.J.Schoeffler, A.Lingel, J.M.Elliott, A.V.Fedorova, A.M.Giannetti, K.Zobel, B.Maurer, E.Varfolomeev, P.Wu, H.J.Wallweber, S.G.Hymowitz, K.Deshayes, D.Vucic, W.J.Fairbrother. Antagonists Induce A Conformational Change in CIAP1 That Promotes Autoubiquitination. Science V. 334 376 2011.
ISSN: ISSN 0036-8075
PubMed: 22021857
DOI: 10.1126/SCIENCE.1207862