Zinc in PDB 2pop: The Crystal Structure of TAB1 and BIR1 Complex

All present enzymatic activity of The Crystal Structure of TAB1 and BIR1 Complex:
2.3.2.27;

The structure of The Crystal Structure of TAB1 and BIR1 Complex, PDB code: 2pop was solved by S.C.Lin, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.00 / 3.10
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	60.986, 108.712, 175.698, 90.00, 90.00, 90.00
R / Rfree (%)	20.9 / 25.4

The binding sites of Zinc atom in the The Crystal Structure of TAB1 and BIR1 Complex (pdb code 2pop). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the The Crystal Structure of TAB1 and BIR1 Complex, PDB code: 2pop:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the The Crystal Structure of TAB1 and BIR1 Complex


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of The Crystal Structure of TAB1 and BIR1 Complex within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn1500 b:82.5 occ:1.00 SG B:CYS1090 1.8 52.9 1.0 CB B:CYS1090 1.8 62.9 1.0 NE2 B:HIS1083 1.9 60.3 1.0 SG B:CYS1063 2.1 49.3 1.0 SG B:CYS1066 2.6 46.6 1.0 CE1 B:HIS1083 2.6 71.1 1.0 CB B:CYS1063 2.8 50.2 1.0 CD2 B:HIS1083 3.0 65.5 1.0 CA B:CYS1090 3.4 80.8 1.0 ND1 B:HIS1083 3.7 62.1 1.0 O B:CYS1090 3.9 87.7 1.0 CG B:HIS1083 4.0 60.1 1.0 C B:CYS1090 4.1 89.2 1.0 CB B:CYS1066 4.1 59.2 1.0 N B:CYS1090 4.2 79.5 1.0 CG1 B:ILE1093 4.2 65.4 1.0 CA B:CYS1063 4.3 83.2 1.0 OG B:SER1087 4.4 61.8 1.0 CB B:SER1087 4.5 54.6 1.0 N B:CYS1066 4.5 67.5 1.0 O B:SER1087 4.9 67.0 1.0 CA B:CYS1066 4.9 62.8 1.0 CB B:SER1065 4.9 52.7 1.0

Zinc binding site 2 out of 2 in the The Crystal Structure of TAB1 and BIR1 Complex


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of The Crystal Structure of TAB1 and BIR1 Complex within 5.0Å range: probe atom residue distance (Å) B Occ D:Zn3500 b:85.5 occ:1.00 SG D:CYS3090 1.9 61.1 1.0 CB D:CYS3090 2.0 51.2 1.0 SG D:CYS3066 2.2 59.4 1.0 NE2 D:HIS3083 2.2 59.5 1.0 SG D:CYS3063 2.2 45.4 1.0 CB D:CYS3063 2.4 55.1 1.0 CE1 D:HIS3083 2.9 62.0 1.0 CD2 D:HIS3083 3.3 53.0 1.0 CB D:CYS3066 3.5 52.3 1.0 CA D:CYS3090 3.5 89.4 1.0 OG D:SER3087 3.9 87.2 1.0 N D:CYS3066 4.0 57.2 1.0 CA D:CYS3063 4.0 51.0 1.0 CB D:SER3087 4.1 73.4 1.0 ND1 D:HIS3083 4.1 71.4 1.0 CA D:CYS3066 4.3 59.6 1.0 CG D:HIS3083 4.3 64.9 1.0 N D:CYS3090 4.3 85.5 1.0 O D:CYS3090 4.4 0.2 1.0 C D:CYS3090 4.4 99.5 1.0 CB D:ALA3068 4.6 46.8 1.0 N D:CYS3063 4.8 44.0 1.0 C D:CYS3063 4.8 52.0 1.0 C D:CYS3066 4.8 59.7 1.0 CB D:SER3065 4.9 66.9 1.0 O D:SER3087 5.0 79.1 1.0

M.Lu, S.C.Lin, Y.Huang, Y.J.Kang, R.Rich, Y.C.Lo, D.Myszka, J.Han, H.Wu. Xiap Induces Nf-Kappab Activation Via the BIR1/TAB1 Interaction and BIR1 Dimerization. Mol.Cell V. 26 689 2007.
ISSN: ISSN 1097-2765
PubMed: 17560374
DOI: 10.1016/J.MOLCEL.2007.05.006