Zinc in PDB 1rni: Bifunctional Dna Primase/Polymerase Domain of ORF904 From the Archaeal Plasmid PRN1

The structure of Bifunctional Dna Primase/Polymerase Domain of ORF904 From the Archaeal Plasmid PRN1, PDB code: 1rni was solved by G.Lipps, A.O.Weinzierl, G.Von Scheven, C.Buchen, P.Cramer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 1.85
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	46.120, 123.630, 41.860, 90.00, 90.00, 90.00
R / Rfree (%)	24.3 / 26.1

The binding sites of Zinc atom in the Bifunctional Dna Primase/Polymerase Domain of ORF904 From the Archaeal Plasmid PRN1 (pdb code 1rni). 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 Bifunctional Dna Primase/Polymerase Domain of ORF904 From the Archaeal Plasmid PRN1, PDB code: 1rni:

Zinc binding site 1 out of 1 in the Bifunctional Dna Primase/Polymerase Domain of ORF904 From the Archaeal Plasmid PRN1


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Bifunctional Dna Primase/Polymerase Domain of ORF904 From the Archaeal Plasmid PRN1 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn256 b:40.3 occ:1.00 ND1 A:HIS188 2.2 33.4 1.0 NE2 A:HIS141 2.2 42.5 1.0 SG A:CYS196 2.3 36.4 1.0 SG A:CYS191 2.4 41.2 1.0 CD2 A:HIS141 3.0 41.1 1.0 CB A:CYS196 3.1 42.5 1.0 CE1 A:HIS188 3.1 39.0 1.0 CG A:HIS188 3.1 31.7 1.0 CB A:CYS191 3.2 46.4 1.0 CE1 A:HIS141 3.3 41.9 1.0 CB A:HIS188 3.4 33.5 1.0 CA A:HIS188 3.8 38.4 1.0 CA A:CYS196 4.1 46.0 1.0 NE2 A:HIS188 4.2 38.3 1.0 CG A:HIS141 4.2 42.2 1.0 CD2 A:HIS188 4.2 33.8 1.0 ND1 A:HIS141 4.3 44.8 1.0 CA A:CYS191 4.7 51.0 1.0 O A:HIS188 4.7 41.7 1.0 C A:HIS188 4.8 40.2 1.0 N A:HIS188 4.8 35.6 1.0 CG1 A:VAL186 4.9 41.5 1.0 CD1 A:TRP198 4.9 42.1 1.0 C A:CYS196 4.9 43.6 1.0

G.Lipps, A.O.Weinzierl, G.Von Scheven, C.Buchen, P.Cramer. Structure of A Bifunctional Dna Primase-Polymerase Nat.Struct.Mol.Biol. V. 11 157 2004.
ISSN: ISSN 1545-9993
PubMed: 14730355
DOI: 10.1038/NSMB723