Zinc in PDB 8aas: Crystal Structure of the Pyrococcus Abyssi Rpa Trimerization Core Bound to Poly-DT20 Ssdna

The structure of Crystal Structure of the Pyrococcus Abyssi Rpa Trimerization Core Bound to Poly-DT20 Ssdna, PDB code: 8aas was solved by C.Madru, P.Legrand, L.Sauguet, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	48.26 / 3.20
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	75.234, 75.234, 215.487, 90, 90, 120
R / Rfree (%)	26.4 / 29.3

The structure of Crystal Structure of the Pyrococcus Abyssi Rpa Trimerization Core Bound to Poly-DT20 Ssdna also contains other interesting chemical elements:

Calcium

(Ca)

5 atoms

The binding sites of Zinc atom in the Crystal Structure of the Pyrococcus Abyssi Rpa Trimerization Core Bound to Poly-DT20 Ssdna (pdb code 8aas). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Crystal Structure of the Pyrococcus Abyssi Rpa Trimerization Core Bound to Poly-DT20 Ssdna, PDB code: 8aas:

Zinc binding site 1 out of 1 in the Crystal Structure of the Pyrococcus Abyssi Rpa Trimerization Core Bound to Poly-DT20 Ssdna


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 Pyrococcus Abyssi Rpa Trimerization Core Bound to Poly-DT20 Ssdna within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn401 b:255.4 occ:1.00 ND1 A:HIS239 2.1 232.6 1.0 SG A:CYS236 2.2 230.1 1.0 SG A:CYS218 2.3 209.8 1.0 SG A:CYS221 2.3 209.4 1.0 CE1 A:HIS239 2.9 233.1 1.0 CB A:CYS218 2.9 207.7 1.0 CG A:HIS239 3.2 230.4 1.0 CB A:CYS221 3.5 208.0 1.0 CB A:CYS236 3.6 227.1 1.0 CB A:HIS239 3.7 227.3 1.0 N A:CYS221 3.7 207.3 1.0 N A:HIS239 4.0 225.4 1.0 NE2 A:HIS239 4.1 232.9 1.0 CA A:CYS221 4.2 207.9 1.0 CD2 A:HIS239 4.3 231.7 1.0 CB A:GLU238 4.3 227.9 1.0 CA A:CYS218 4.4 207.0 1.0 CA A:HIS239 4.5 226.0 1.0 CB A:GLU220 4.6 209.6 1.0 C A:GLU238 4.8 225.5 1.0 C A:GLU220 4.8 207.2 1.0 N A:GLU238 4.9 225.2 1.0 CA A:GLU238 4.9 225.5 1.0 N A:GLU220 4.9 206.8 1.0 CA A:CYS236 4.9 226.6 1.0 C A:CYS218 4.9 207.3 1.0 C A:CYS221 5.0 208.7 1.0 OE2 A:GLU238 5.0 241.2 1.0 CA A:GLU220 5.0 207.2 1.0

C.Madru, M.Martinez-Carranza, S.Laurent, A.C.Alberti, M.Chevreuil, B.Raynal, A.Haouz, R.A.Le Meur, M.Delarue, G.Henneke, D.Flament, M.Krupovic, P.Legrand, L.Sauguet. Dna-Binding Mechanism and Evolution of Replication Protein A. Nat Commun V. 14 2326 2023.
ISSN: ESSN 2041-1723
PubMed: 37087464
DOI: 10.1038/S41467-023-38048-W