Zinc in PDB 2atq: RB69 Single-Stranded Dna Binding Protein-Dna Polymerase Fusion

All present enzymatic activity of RB69 Single-Stranded Dna Binding Protein-Dna Polymerase Fusion:
2.7.7.7;

The structure of RB69 Single-Stranded Dna Binding Protein-Dna Polymerase Fusion, PDB code: 2atq was solved by S.Sun, L.Geng, Y.Shamoo, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	37.99 / 3.20
Space group	P 65
Cell size a, b, c (Å), α, β, γ (°)	196.029, 196.029, 85.170, 90.00, 90.00, 120.00
R / Rfree (%)	28.4 / 34.5

The binding sites of Zinc atom in the RB69 Single-Stranded Dna Binding Protein-Dna Polymerase Fusion (pdb code 2atq). 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 RB69 Single-Stranded Dna Binding Protein-Dna Polymerase Fusion, PDB code: 2atq:

Zinc binding site 1 out of 1 in the RB69 Single-Stranded Dna Binding Protein-Dna Polymerase Fusion


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of RB69 Single-Stranded Dna Binding Protein-Dna Polymerase Fusion within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn1 b:0.2 occ:1.00 NE2 B:HIS64 2.0 0.4 1.0 SG B:CYS87 2.0 0.3 1.0 SG B:CYS77 2.1 0.8 1.0 SG B:CYS90 2.3 0.2 1.0 CE1 B:HIS64 2.8 0.3 1.0 CD2 B:HIS64 3.1 0.8 1.0 CB B:CYS77 3.3 0.4 1.0 CB B:CYS87 3.5 0.2 1.0 CB B:CYS90 3.6 0.6 1.0 N B:CYS90 3.7 0.3 1.0 OG B:SER79 3.9 0.5 1.0 ND1 B:HIS64 4.0 0.1 1.0 CA B:CYS77 4.0 1.0 1.0 CG B:HIS64 4.1 0.6 1.0 CA B:CYS90 4.2 0.3 1.0 CB B:VAL89 4.2 0.3 1.0 N B:SER78 4.5 0.1 1.0 O B:CYS87 4.6 0.2 1.0 CA B:CYS87 4.7 0.5 1.0 C B:VAL89 4.7 0.6 1.0 C B:CYS77 4.7 0.2 1.0 C B:CYS87 4.8 0.5 1.0 CA B:VAL89 4.8 0.2 1.0 N B:SER79 4.8 0.6 1.0 N B:VAL89 4.8 0.5 1.0 CG2 B:VAL89 4.8 0.2 1.0 CB B:SER79 4.9 0.9 1.0 CB B:ARG111 4.9 0.5 1.0 CG1 B:VAL89 5.0 0.5 1.0

S.Sun, L.Geng, Y.Shamoo. Structure and Enzymatic Properties of A Chimeric Bacteriophage RB69 Dna Polymerase and Single-Stranded Dna Binding Protein with Increased Processivity. Proteins V. 65 231 2006.
ISSN: ISSN 0887-3585
PubMed: 16881051
DOI: 10.1002/PROT.21088