Zinc in PDB 3t92: Crystal Structure of the TAZ2:C/Ebpepsilon-Tad Chimera Protein

All present enzymatic activity of Crystal Structure of the TAZ2:C/Ebpepsilon-Tad Chimera Protein:
2.3.1.48;

The structure of Crystal Structure of the TAZ2:C/Ebpepsilon-Tad Chimera Protein, PDB code: 3t92 was solved by P.Bhaumik, M.Maria, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.00 / 1.50
Space group	P 65
Cell size a, b, c (Å), α, β, γ (°)	47.860, 47.860, 104.130, 90.00, 90.00, 120.00
R / Rfree (%)	17.8 / 22.8

The binding sites of Zinc atom in the Crystal Structure of the TAZ2:C/Ebpepsilon-Tad Chimera Protein (pdb code 3t92). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 3 binding sites of Zinc where determined in the Crystal Structure of the TAZ2:C/Ebpepsilon-Tad Chimera Protein, PDB code: 3t92:
Jump to Zinc binding site number: 1; 2; 3;

Zinc binding site 1 out of 3 in the Crystal Structure of the TAZ2:C/Ebpepsilon-Tad Chimera Protein


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 TAZ2:C/Ebpepsilon-Tad Chimera Protein within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn122 b:18.9 occ:1.00 NE2 A:HIS22 2.1 18.1 1.0 SG A:CYS31 2.2 19.4 1.0 SG A:CYS26 2.3 22.4 1.0 SG A:CYS36 2.4 19.2 1.0 CD2 A:HIS22 3.0 17.4 1.0 CB A:CYS31 3.1 24.8 1.0 CE1 A:HIS22 3.1 18.3 1.0 CB A:CYS26 3.2 22.4 1.0 CB A:CYS36 3.2 18.5 1.0 CG A:HIS22 4.2 18.8 1.0 ND1 A:HIS22 4.2 18.7 1.0 O A:HOH184 4.3 14.1 1.0 NZ A:LYS40 4.3 32.1 1.0 O A:HOH162 4.4 13.3 1.0 O A:HOH241 4.4 17.5 1.0 CD1 A:LEU33 4.5 19.3 1.0 CA A:CYS31 4.6 26.5 1.0 CE A:LYS40 4.6 28.7 1.0 CA A:CYS26 4.6 24.9 1.0 CA A:CYS36 4.6 17.7 1.0 CB A:LEU33 5.0 15.7 1.0 O A:ASN28 5.0 34.4 1.0

Zinc binding site 2 out of 3 in the Crystal Structure of the TAZ2:C/Ebpepsilon-Tad Chimera Protein


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 TAZ2:C/Ebpepsilon-Tad Chimera Protein within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn123 b:17.5 occ:1.00 CE1 A:HIS45 2.0 14.2 1.0 SG A:CYS57 2.3 18.6 1.0 SG A:CYS60 2.3 17.3 1.0 SG A:CYS49 2.3 19.4 1.0 NE2 A:HIS45 3.0 23.4 1.0 ND1 A:HIS45 3.0 22.6 1.0 CB A:CYS49 3.1 20.9 1.0 CB A:CYS57 3.2 17.9 1.0 CB A:CYS60 3.5 13.9 1.0 N A:CYS60 3.7 14.7 1.0 CA A:CYS60 4.1 14.5 1.0 CD2 A:HIS45 4.1 20.2 1.0 CG A:HIS45 4.2 19.9 1.0 N A:LYS52 4.5 18.4 1.0 O A:HOH290 4.5 22.2 1.0 CB A:ILE59 4.5 18.1 1.0 CA A:CYS49 4.6 22.2 1.0 CA A:CYS57 4.6 18.4 1.0 CA A:LYS52 4.7 16.9 0.5 C A:ILE59 4.8 15.6 1.0 CA A:LYS52 4.8 17.0 0.5 C A:CYS57 5.0 17.3 1.0

Zinc binding site 3 out of 3 in the Crystal Structure of the TAZ2:C/Ebpepsilon-Tad Chimera Protein


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Crystal Structure of the TAZ2:C/Ebpepsilon-Tad Chimera Protein within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn124 b:20.4 occ:1.00 NE2 A:HIS70 2.1 19.4 1.0 SG A:CYS84 2.2 20.3 1.0 SG A:CYS79 2.3 23.1 1.0 SG A:CYS74 2.4 27.1 1.0 CD2 A:HIS70 3.0 17.3 1.0 CB A:CYS79 3.1 27.5 1.0 CE1 A:HIS70 3.1 20.2 1.0 CB A:CYS74 3.2 25.9 1.0 CB A:CYS84 3.3 18.8 1.0 CG A:HIS70 4.2 17.3 1.0 ND1 A:HIS70 4.2 18.6 1.0 CB A:VAL81 4.3 18.8 1.0 CG2 A:VAL81 4.4 20.0 1.0 NZ A:LYS88 4.4 30.5 1.0 O A:HOH250 4.4 23.0 1.0 CA A:CYS79 4.5 29.5 1.0 CA A:CYS74 4.6 29.2 1.0 CA A:CYS84 4.7 18.1 1.0 CE A:LYS88 4.7 30.2 1.0 O A:HOH187 4.7 17.7 1.0 O A:GLU76 4.9 39.0 1.0

P.Bhaumik, J.Davis, J.E.Tropea, S.Cherry, P.F.Johnson, M.Miller. Structural Insights Into Interactions of C/Ebp Transcriptional Activators with the TAZ2 Domain of P300. Acta Crystallogr. D Biol. V. 70 1914 2014CRYSTALLOGR..
ISSN: ESSN 1399-0047
PubMed: 25004968
DOI: 10.1107/S1399004714009262