Zinc in PDB 2vl6: Structural Analysis of the Sulfolobus Solfataricus Mcm Protein N-Terminal Domain

The structure of Structural Analysis of the Sulfolobus Solfataricus Mcm Protein N-Terminal Domain, PDB code: 2vl6 was solved by W.Liu, B.Pucci, M.Rossi, F.M.Pisani, R.Ladenstein, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	31.88 / 2.8
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	193.994, 52.236, 115.574, 90.00, 124.15, 90.00
R / Rfree (%)	23.3 / 28.3

The binding sites of Zinc atom in the Structural Analysis of the Sulfolobus Solfataricus Mcm Protein N-Terminal Domain (pdb code 2vl6). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 3 binding sites of Zinc where determined in the Structural Analysis of the Sulfolobus Solfataricus Mcm Protein N-Terminal Domain, PDB code: 2vl6:
Jump to Zinc binding site number: 1; 2; 3;

Zinc binding site 1 out of 3 in the Structural Analysis of the Sulfolobus Solfataricus Mcm Protein N-Terminal Domain


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structural Analysis of the Sulfolobus Solfataricus Mcm Protein N-Terminal Domain within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1266 b:52.4 occ:1.00 ND1 A:HIS144 2.0 34.3 1.0 SG A:CYS171 2.1 29.4 1.0 SG A:CYS149 2.2 33.7 1.0 SG A:CYS174 2.3 37.5 1.0 CE1 A:HIS144 3.0 33.1 1.0 CB A:CYS174 3.0 33.8 1.0 CB A:CYS171 3.0 31.1 1.0 CG A:HIS144 3.1 33.3 1.0 CB A:CYS149 3.1 34.4 1.0 CB A:HIS144 3.4 32.9 1.0 N A:CYS174 3.5 34.1 1.0 CA A:CYS174 3.9 34.4 1.0 NE2 A:HIS144 4.1 33.1 1.0 CD2 A:HIS144 4.2 33.9 1.0 CA A:CYS171 4.4 31.4 1.0 C A:LYS173 4.5 33.9 1.0 CA A:CYS149 4.6 34.4 1.0 CB A:LYS173 4.6 33.0 1.0 N A:GLY175 4.7 34.2 1.0 C A:CYS174 4.7 34.2 1.0 O A:CYS171 4.7 32.7 1.0 C A:CYS171 4.7 32.1 1.0 O A:LYS176 4.8 34.9 1.0 CA A:LYS173 4.8 33.5 1.0 N A:LYS173 4.9 33.3 1.0 CA A:HIS144 4.9 33.5 1.0

Zinc binding site 2 out of 3 in the Structural Analysis of the Sulfolobus Solfataricus Mcm Protein N-Terminal Domain


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Structural Analysis of the Sulfolobus Solfataricus Mcm Protein N-Terminal Domain within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn1266 b:51.8 occ:1.00 SG B:CYS171 2.2 28.7 1.0 SG B:CYS149 2.2 33.0 1.0 ND1 B:HIS144 2.3 34.4 1.0 SG B:CYS174 2.5 36.7 1.0 CB B:CYS149 2.8 33.9 1.0 CG B:HIS144 3.2 33.5 1.0 CB B:CYS171 3.2 30.8 1.0 CB B:CYS174 3.2 34.2 1.0 CE1 B:HIS144 3.3 34.9 1.0 CB B:HIS144 3.4 32.8 1.0 N B:CYS174 3.6 34.2 1.0 CA B:CYS174 4.0 34.5 1.0 CA B:CYS149 4.3 34.3 1.0 CD2 B:HIS144 4.3 34.3 1.0 NE2 B:HIS144 4.4 34.0 1.0 CB B:LYS173 4.5 33.4 1.0 C B:LYS173 4.5 33.9 1.0 CA B:CYS171 4.6 31.5 1.0 C B:CYS174 4.9 34.3 1.0 CA B:LYS173 4.9 33.5 1.0 CA B:HIS144 4.9 33.5 1.0 N B:GLY175 4.9 34.3 1.0 C B:CYS149 4.9 34.5 1.0 N B:LYS173 5.0 33.4 1.0 N B:MET150 5.0 34.8 1.0 C B:CYS171 5.0 32.1 1.0

Zinc binding site 3 out of 3 in the Structural Analysis of the Sulfolobus Solfataricus Mcm Protein N-Terminal Domain


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Structural Analysis of the Sulfolobus Solfataricus Mcm Protein N-Terminal Domain within 5.0Å range: probe atom residue distance (Å) B Occ C:Zn1266 b:58.9 occ:1.00 ND1 C:HIS144 2.2 33.4 1.0 SG C:CYS171 2.2 30.2 1.0 SG C:CYS149 2.2 33.8 1.0 SG C:CYS174 2.5 38.0 1.0 CB C:CYS149 2.8 34.5 1.0 CG C:HIS144 3.1 33.0 1.0 CE1 C:HIS144 3.1 33.8 1.0 CB C:CYS171 3.2 31.3 1.0 CB C:CYS174 3.2 34.7 1.0 CB C:HIS144 3.4 33.4 1.0 N C:CYS174 3.8 34.1 1.0 CA C:CYS174 4.0 34.6 1.0 NE2 C:HIS144 4.3 33.3 1.0 CA C:CYS149 4.3 34.5 1.0 CD2 C:HIS144 4.3 33.2 1.0 CA C:CYS171 4.6 31.5 1.0 CB C:LYS173 4.8 33.0 1.0 C C:LYS173 4.8 33.9 1.0 C C:CYS174 4.8 34.4 1.0 O C:LYS176 4.8 34.8 1.0 N C:GLY175 4.9 34.4 1.0 CA C:HIS144 4.9 33.5 1.0

W.Liu, B.Pucci, M.Rossi, F.M.Pisani, R.Ladenstein. Structural Analysis of the Sulfolobus Solfataricus Mcm Protein N-Terminal Domain. Nucleic Acids Res. V. 36 3235 2008.
ISSN: ISSN 0305-1048
PubMed: 18417534
DOI: 10.1093/NAR/GKN183