Zinc in PDB 2j7j: Invariance of the Zinc Finger Module: A Comparison of the Free Structure with Those in Nucleic-Acid Complexes

The structure of Invariance of the Zinc Finger Module: A Comparison of the Free Structure with Those in Nucleic-Acid Complexes, PDB code: 2j7j was solved by D.Lu, A.Klug, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	44.28 / 1.65
Space group	P 61 2 2
Cell size a, b, c (Å), α, β, γ (°)	50.954, 50.954, 173.431, 90.00, 90.00, 120.00
R / Rfree (%)	21.7 / 22.8

The binding sites of Zinc atom in the Invariance of the Zinc Finger Module: A Comparison of the Free Structure with Those in Nucleic-Acid Complexes (pdb code 2j7j). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 3 binding sites of Zinc where determined in the Invariance of the Zinc Finger Module: A Comparison of the Free Structure with Those in Nucleic-Acid Complexes, PDB code: 2j7j:
Jump to Zinc binding site number: 1; 2; 3;

Zinc binding site 1 out of 3 in the Invariance of the Zinc Finger Module: A Comparison of the Free Structure with Those in Nucleic-Acid Complexes


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Invariance of the Zinc Finger Module: A Comparison of the Free Structure with Those in Nucleic-Acid Complexes within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1086 b:16.8 occ:1.00 NE2 A:HIS26 2.0 18.4 1.0 NE2 A:HIS22 2.1 17.7 1.0 SG A:CYS4 2.3 16.1 1.0 SG A:CYS9 2.3 17.1 1.0 CE1 A:HIS22 2.9 18.9 1.0 CD2 A:HIS26 3.0 19.1 1.0 CE1 A:HIS26 3.1 19.6 1.0 CD2 A:HIS22 3.1 19.0 1.0 CB A:CYS4 3.2 16.8 1.0 CB A:CYS9 3.2 16.3 1.0 ND1 A:HIS22 4.1 20.0 1.0 CG A:HIS26 4.1 19.6 1.0 ND1 A:HIS26 4.1 20.4 1.0 CG A:HIS22 4.2 18.8 1.0 O A:HOH2007 4.3 52.1 1.0 CB A:PHE6 4.5 16.8 1.0 CA A:CYS4 4.6 17.1 1.0 CA A:CYS9 4.7 16.3 1.0 CB A:LYS11 4.8 19.2 1.0 O A:HOH2052 4.8 44.8 1.0 N A:GLY10 4.8 16.8 1.0 CD A:LYS11 4.9 24.6 1.0 N A:LYS11 5.0 18.4 1.0 CD2 A:PHE6 5.0 15.9 1.0

Zinc binding site 2 out of 3 in the Invariance of the Zinc Finger Module: A Comparison of the Free Structure with Those in Nucleic-Acid Complexes


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Invariance of the Zinc Finger Module: A Comparison of the Free Structure with Those in Nucleic-Acid Complexes within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1087 b:16.2 occ:1.00 NE2 A:HIS56 2.1 17.2 1.0 NE2 A:HIS52 2.2 14.6 1.0 SG A:CYS39 2.2 21.0 1.0 SG A:CYS34 2.3 16.7 1.0 CD2 A:HIS56 3.0 17.4 1.0 CD2 A:HIS52 3.1 14.3 1.0 CE1 A:HIS56 3.1 17.9 1.0 CE1 A:HIS52 3.1 15.1 1.0 CB A:CYS39 3.1 22.6 1.0 CB A:CYS34 3.1 15.6 1.0 CG A:HIS56 4.1 18.5 1.0 ND1 A:HIS56 4.2 17.8 1.0 ND1 A:HIS52 4.2 14.4 1.0 CG A:HIS52 4.2 14.7 1.0 CB A:LYS41 4.3 19.7 1.0 ND1 A:HIS36 4.3 21.7 1.0 CB A:HIS36 4.5 21.0 1.0 CG A:LYS41 4.5 21.4 1.0 CA A:CYS39 4.6 22.8 1.0 CA A:CYS34 4.6 16.1 1.0 CG A:HIS36 4.8 20.7 1.0 O A:HOH2046 4.8 36.1 1.0 O A:HOH2109 4.9 48.3 1.0 C A:CYS39 5.0 22.8 1.0

Zinc binding site 3 out of 3 in the Invariance of the Zinc Finger Module: A Comparison of the Free Structure with Those in Nucleic-Acid Complexes


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Invariance of the Zinc Finger Module: A Comparison of the Free Structure with Those in Nucleic-Acid Complexes within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1088 b:25.9 occ:1.00 NE2 A:HIS85 2.1 41.9 1.0 NE2 A:HIS80 2.1 23.1 1.0 SG A:CYS61 2.2 31.2 1.0 SG A:CYS67 2.3 27.4 1.0 CE1 A:HIS85 2.9 42.1 1.0 CD2 A:HIS80 3.0 24.2 1.0 CB A:CYS61 3.0 31.3 1.0 CE1 A:HIS80 3.1 21.9 1.0 CB A:CYS67 3.1 29.8 1.0 CD2 A:HIS85 3.2 42.0 1.0 ND1 A:HIS85 4.1 42.5 1.0 CB A:PHE69 4.1 21.6 1.0 ND1 A:HIS80 4.2 22.5 1.0 CG A:HIS80 4.2 24.2 1.0 CG A:HIS85 4.3 41.5 1.0 CA A:CYS61 4.5 31.3 1.0 CA A:CYS67 4.6 29.8 1.0 CG A:PHE69 4.9 21.1 1.0 CB A:CYS84 5.0 38.5 1.0

D.Lu, A.Klug. Invariance of the Zinc Finger Module: A Comparison of the Free Structure with Those in Nucleic-Acid Complexes. Proteins V. 67 508 2007.
ISSN: ISSN 0887-3585
PubMed: 17335000
DOI: 10.1002/PROT.21289