Zinc in PDB 1u05: Crystal Structure of Protein Yfih From Shigella Flexneri, Pfam DUF152

The structure of Crystal Structure of Protein Yfih From Shigella Flexneri, Pfam DUF152, PDB code: 1u05 was solved by J.Seetharaman, S.Swaminathan, S.K.Burley, New York Sgx Research Centerfor Structural Genomics (Nysgxrc), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	33.00 / 2.50
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	43.683, 50.465, 55.265, 90.25, 96.51, 90.29
R / Rfree (%)	21.7 / 28.3

The binding sites of Zinc atom in the Crystal Structure of Protein Yfih From Shigella Flexneri, Pfam DUF152 (pdb code 1u05). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Crystal Structure of Protein Yfih From Shigella Flexneri, Pfam DUF152, PDB code: 1u05:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Crystal Structure of Protein Yfih From Shigella Flexneri, Pfam DUF152


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of Protein Yfih From Shigella Flexneri, Pfam DUF152 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn500 b:7.6 occ:1.00 NE2 A:HIS124 2.2 18.3 1.0 NE2 A:HIS71 2.3 22.9 1.0 SG A:CYS107 2.3 13.2 1.0 O A:HOH584 2.3 19.4 1.0 CE1 A:HIS124 2.9 18.9 1.0 CE1 A:HIS71 3.0 20.8 1.0 CB A:CYS107 3.1 12.9 1.0 CD2 A:HIS71 3.3 19.8 1.0 CD2 A:HIS124 3.3 18.2 1.0 O A:HOH581 3.5 26.0 1.0 ND1 A:HIS71 4.0 16.6 1.0 O A:HOH576 4.0 25.8 1.0 ND1 A:HIS124 4.1 16.8 1.0 CG A:HIS71 4.2 17.5 1.0 CG A:HIS124 4.4 17.9 1.0 CA A:CYS107 4.4 11.8 1.0 N A:CYS107 4.7 10.4 1.0

Zinc binding site 2 out of 2 in the Crystal Structure of Protein Yfih From Shigella Flexneri, Pfam DUF152


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure of Protein Yfih From Shigella Flexneri, Pfam DUF152 within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn501 b:7.6 occ:1.00 NE2 B:HIS124 2.2 18.1 1.0 NE2 B:HIS71 2.2 18.3 1.0 SG B:CYS107 2.3 5.5 1.0 O B:HOH509 2.4 19.4 1.0 O B:HOH528 3.0 16.5 1.0 CE1 B:HIS71 3.0 16.3 1.0 CE1 B:HIS124 3.0 18.2 1.0 CB B:CYS107 3.1 13.1 1.0 CD2 B:HIS71 3.2 15.7 1.0 CD2 B:HIS124 3.3 18.0 1.0 O B:HOH583 3.8 26.9 1.0 ND1 B:HIS71 4.1 15.1 1.0 CG B:HIS71 4.2 15.9 1.0 ND1 B:HIS124 4.2 16.5 1.0 CG B:HIS124 4.4 17.7 1.0 CA B:CYS107 4.4 10.2 1.0 N B:CYS107 4.7 11.1 1.0 CA B:GLY126 4.9 16.1 1.0

J.Seetharaman, S.Swaminathan. Crystal Structure of Conserved Hypothetical Protein To Be Published.