Zinc in PDB 6y22: Ring-Dtc Domains of Deltex 2, Form 1

All present enzymatic activity of Ring-Dtc Domains of Deltex 2, Form 1:
2.3.2.27;

The structure of Ring-Dtc Domains of Deltex 2, Form 1, PDB code: 6y22 was solved by M.Gabrielssen, L.Buetow, D.T.Huang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.01 / 2.07
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	106.418, 106.418, 74.669, 90.00, 90.00, 120.00
R / Rfree (%)	17.9 / 20.8

The binding sites of Zinc atom in the Ring-Dtc Domains of Deltex 2, Form 1 (pdb code 6y22). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Ring-Dtc Domains of Deltex 2, Form 1, PDB code: 6y22:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Ring-Dtc Domains of Deltex 2, Form 1


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Ring-Dtc Domains of Deltex 2, Form 1 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn701 b:48.5 occ:1.00 ND1 A:HIS447 2.1 46.0 1.0 SG A:CYS445 2.2 52.4 1.0 SG A:CYS469 2.3 49.1 1.0 SG A:CYS472 2.4 51.1 1.0 CE1 A:HIS447 3.0 50.3 1.0 CG A:HIS447 3.1 52.0 1.0 CB A:CYS469 3.1 43.8 1.0 CB A:CYS445 3.2 62.6 1.0 CB A:CYS472 3.4 51.9 1.0 OG A:SER471 3.5 75.2 1.0 CB A:HIS447 3.5 45.3 1.0 N A:CYS472 3.8 54.3 1.0 CA A:CYS472 4.1 54.8 1.0 NE2 A:HIS447 4.1 58.9 1.0 CD2 A:HIS447 4.2 47.4 1.0 CA A:CYS445 4.5 66.7 1.0 CA A:CYS469 4.6 48.0 1.0 N A:HIS447 4.6 59.3 1.0 O A:CYS445 4.6 65.3 1.0 CD1 A:LEU442 4.7 52.6 1.0 CA A:HIS447 4.7 55.7 1.0 C A:CYS445 4.7 68.6 1.0 OG1 A:THR474 4.7 58.0 1.0 C A:CYS472 4.8 58.9 1.0 CB A:SER471 4.8 66.0 1.0 C A:SER471 4.8 59.1 1.0 CB A:THR474 4.9 56.2 1.0 N A:LYS473 4.9 51.5 1.0

Zinc binding site 2 out of 2 in the Ring-Dtc Domains of Deltex 2, Form 1


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Ring-Dtc Domains of Deltex 2, Form 1 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn702 b:48.6 occ:1.00 ND1 A:HIS450 2.1 49.1 1.0 SG A:CYS415 2.2 52.9 1.0 SG A:CYS453 2.3 53.5 1.0 SG A:CYS412 2.4 46.0 1.0 CB A:CYS412 3.0 47.0 1.0 CE1 A:HIS450 3.1 48.4 1.0 CG A:HIS450 3.1 51.3 1.0 CB A:CYS453 3.3 50.1 1.0 CB A:CYS415 3.4 53.6 1.0 CB A:HIS450 3.5 46.3 1.0 N A:CYS415 3.9 56.5 1.0 N A:HIS450 4.1 45.4 1.0 NE2 A:HIS450 4.2 48.9 1.0 CA A:CYS415 4.2 56.6 1.0 CD2 A:HIS450 4.3 50.1 1.0 N A:GLY424 4.3 56.8 1.0 CA A:HIS450 4.4 49.0 1.0 CA A:CYS412 4.4 54.1 1.0 CA A:SER423 4.5 53.3 1.0 OG A:SER423 4.6 53.8 1.0 CB A:ILE414 4.6 57.9 1.0 CA A:CYS453 4.7 51.2 1.0 CB A:SER423 4.7 50.8 1.0 O A:CYS412 4.8 63.2 1.0 C A:CYS412 4.8 56.8 1.0 C A:ILE414 4.8 62.3 1.0 C A:SER423 5.0 55.9 1.0 N A:CYS453 5.0 52.7 1.0 O A:HIS450 5.0 51.7 1.0

S.F.Ahmed, L.Buetow, M.Gabrielsen, S.Lilla, C.Chatrin, G.J.Sibbet, S.Zanivan, D.T.Huang. DELTEX2 C-Terminal Domain Recognizes and Recruits Adp-Ribosylated Proteins For Ubiquitination. Sci Adv V. 6 2020.
ISSN: ESSN 2375-2548
PubMed: 32937373
DOI: 10.1126/SCIADV.ABC0629