Zinc in PDB 6cyt: Hiv-1 Tar Loop in Complex with Tat:AFF4:P-Tefb

All present enzymatic activity of Hiv-1 Tar Loop in Complex with Tat:AFF4:P-Tefb:
2.7.11.22; 2.7.11.23;

The structure of Hiv-1 Tar Loop in Complex with Tat:AFF4:P-Tefb, PDB code: 6cyt was solved by U.Schulze Gahmen, J.H.Hurley, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	128.67 / 3.50
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	148.580, 148.580, 104.630, 90.00, 90.00, 120.00
R / Rfree (%)	24.8 / 28.3

The binding sites of Zinc atom in the Hiv-1 Tar Loop in Complex with Tat:AFF4:P-Tefb (pdb code 6cyt). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Hiv-1 Tar Loop in Complex with Tat:AFF4:P-Tefb, PDB code: 6cyt:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Hiv-1 Tar Loop in Complex with Tat:AFF4:P-Tefb


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Hiv-1 Tar Loop in Complex with Tat:AFF4:P-Tefb within 5.0Å range: probe atom residue distance (Å) B Occ D:Zn101 b:0.6 occ:1.00 ND1 D:HIS33 2.0 0.8 1.0 SG D:CYS37 2.3 0.6 1.0 SG D:CYS34 2.3 0.5 1.0 SG D:CYS22 2.3 0.6 1.0 CE1 D:HIS33 2.9 0.1 1.0 CG D:HIS33 3.1 0.3 1.0 CB D:CYS37 3.4 0.9 1.0 CB D:CYS34 3.4 0.8 1.0 CB D:HIS33 3.5 1.0 1.0 CB D:CYS22 3.6 0.5 1.0 N D:CYS34 3.7 1.0 1.0 N D:CYS37 4.0 0.7 1.0 NE2 D:HIS33 4.0 0.7 1.0 CA D:CYS34 4.0 0.7 1.0 C D:HIS33 4.1 0.6 1.0 CD2 D:HIS33 4.2 0.3 1.0 CA D:CYS22 4.2 0.8 1.0 CA D:CYS37 4.2 0.4 1.0 CA D:HIS33 4.4 0.9 1.0 C D:CYS34 4.6 0.0 1.0 O D:HIS33 4.7 0.3 1.0 O D:CYS34 4.7 0.4 1.0 CG D:PRO18 4.8 0.0 1.0 N D:CYS22 4.8 0.8 1.0 CB D:VAL36 5.0 0.4 1.0

Zinc binding site 2 out of 2 in the Hiv-1 Tar Loop in Complex with Tat:AFF4:P-Tefb


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Hiv-1 Tar Loop in Complex with Tat:AFF4:P-Tefb within 5.0Å range: probe atom residue distance (Å) B Occ D:Zn102 b:0.6 occ:0.80 SG D:CYS25 2.3 0.3 1.0 SG D:CYS27 2.4 0.2 1.0 SG D:CYS30 2.5 0.1 1.0 SG B:CYS261 2.8 0.2 1.0 CB D:CYS25 2.9 0.4 1.0 CB D:CYS27 3.7 0.7 1.0 CB D:CYS30 3.9 0.7 1.0 CB B:CYS261 3.9 0.8 1.0 CA B:CYS261 3.9 0.1 1.0 CA D:CYS25 4.2 0.6 1.0 O B:ALA260 4.3 0.5 1.0 N D:CYS27 4.4 1.0 1.0 N B:CYS261 4.5 0.1 1.0 C D:CYS25 4.5 0.0 1.0 C B:ALA260 4.6 1.0 1.0 OG1 D:THR23 4.7 0.6 1.0 CA D:CYS27 4.7 0.0 1.0 N D:CYS30 4.7 0.4 1.0 O D:CYS25 4.8 0.1 1.0 CA D:CYS30 4.9 0.4 1.0 N D:TYR26 4.9 0.1 1.0

U.Schulze-Gahmen, J.H.Hurley. Structural Mechanism For Hiv-1 Tar Loop Recognition By Tat and the Super Elongation Complex. Proc. Natl. Acad. Sci. V. 115 12973 2018U.S.A..
ISSN: ESSN 1091-6490
PubMed: 30514815
DOI: 10.1073/PNAS.1806438115