Zinc in PDB 1l1o: Structure of the Human Replication Protein A (Rpa) Trimerization Core

The structure of Structure of the Human Replication Protein A (Rpa) Trimerization Core, PDB code: 1l1o was solved by E.V.Bochkareva, S.Korolev, S.P.Lees-Miller, A.Bochkarev, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.92 / 2.80
Space group	P 31 2 1
Cell size a, b, c (Å), α, β, γ (°)	88.527, 88.527, 341.090, 90.00, 90.00, 120.00
R / Rfree (%)	23.6 / 28.2

The binding sites of Zinc atom in the Structure of the Human Replication Protein A (Rpa) Trimerization Core (pdb code 1l1o). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Structure of the Human Replication Protein A (Rpa) Trimerization Core, PDB code: 1l1o:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Structure of the Human Replication Protein A (Rpa) Trimerization Core


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structure of the Human Replication Protein A (Rpa) Trimerization Core within 5.0Å range: probe atom residue distance (Å) B Occ C:Zn1 b:67.3 occ:1.00 SG C:CYS481 2.1 69.7 1.0 SG C:CYS503 2.2 76.9 1.0 SG C:CYS500 2.2 53.6 1.0 SG C:CYS486 2.5 70.6 1.0 OG1 C:THR483 2.7 82.2 1.0 CB C:CYS481 3.0 73.3 1.0 CB C:CYS500 3.1 61.7 1.0 CB C:CYS486 3.3 78.9 1.0 CB C:THR483 3.9 84.2 1.0 CB C:CYS503 4.0 79.4 1.0 CG2 C:THR483 4.1 84.3 1.0 N C:CYS503 4.3 79.7 1.0 CA C:CYS481 4.4 74.0 1.0 CA C:CYS500 4.6 64.2 1.0 CD C:LYS502 4.7 80.9 1.0 CB C:LYS502 4.7 79.4 1.0 CA C:CYS486 4.7 79.3 1.0 CA C:CYS503 4.8 79.7 1.0 CB C:LYS488 4.8 66.1 1.0 C C:CYS486 5.0 76.8 1.0 N C:THR483 5.0 77.9 1.0

Zinc binding site 2 out of 2 in the Structure of the Human Replication Protein A (Rpa) Trimerization Core


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Structure of the Human Replication Protein A (Rpa) Trimerization Core within 5.0Å range: probe atom residue distance (Å) B Occ F:Zn2 b:66.6 occ:1.00 SG F:CYS481 2.2 66.2 1.0 SG F:CYS500 2.2 60.8 1.0 SG F:CYS503 2.3 65.7 1.0 SG F:CYS486 2.6 68.1 1.0 CB F:CYS481 2.8 74.3 1.0 CB F:CYS500 3.0 65.3 1.0 CB F:CYS503 3.2 68.4 1.0 CB F:CYS486 3.3 76.7 1.0 N F:CYS503 3.7 67.8 1.0 CA F:CYS503 4.1 68.2 1.0 OG1 F:THR483 4.1 93.5 1.0 CA F:CYS481 4.2 74.6 1.0 CA F:CYS500 4.5 66.7 1.0 CB F:LYS502 4.6 75.7 1.0 CE1 F:PHE507 4.7 85.4 1.0 O F:CYS500 4.7 66.5 1.0 NZ F:LYS502 4.7 75.0 1.0 CA F:CYS486 4.8 78.0 1.0 C F:LYS502 4.8 69.7 1.0 C F:CYS500 4.9 67.0 1.0 CB F:LYS488 5.0 69.0 1.0 CD F:LYS502 5.0 75.2 1.0 CZ F:PHE507 5.0 85.8 1.0

E.Bochkareva, S.Korolev, S.P.Lees-Miller, A.Bochkarev. Structure of the Rpa Trimerization Core and Its Role in the Multistep Dna-Binding Mechanism of Rpa. Embo J. V. 21 1855 2002.
ISSN: ISSN 0261-4189
PubMed: 11927569
DOI: 10.1093/EMBOJ/21.7.1855