Zinc in PDB 6egm: Crystal Structure of A De Novo Three-Stranded Coiled Coil Peptide Containing D-Leu in A D-Site Position of A Tris-Thiolate Binding Site

The structure of Crystal Structure of A De Novo Three-Stranded Coiled Coil Peptide Containing D-Leu in A D-Site Position of A Tris-Thiolate Binding Site, PDB code: 6egm was solved by L.Ruckthong, J.A.Stuckey, V.L.Pecoraro, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	23.44 / 1.84
Space group	H 3 2
Cell size a, b, c (Å), α, β, γ (°)	37.898, 37.898, 140.667, 90.00, 90.00, 120.00
R / Rfree (%)	20.1 / 20.6

The binding sites of Zinc atom in the Crystal Structure of A De Novo Three-Stranded Coiled Coil Peptide Containing D-Leu in A D-Site Position of A Tris-Thiolate Binding Site (pdb code 6egm). 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 Crystal Structure of A De Novo Three-Stranded Coiled Coil Peptide Containing D-Leu in A D-Site Position of A Tris-Thiolate Binding Site, PDB code: 6egm:

Zinc binding site 1 out of 1 in the Crystal Structure of A De Novo Three-Stranded Coiled Coil Peptide Containing D-Leu in A D-Site Position of A Tris-Thiolate Binding Site


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 A De Novo Three-Stranded Coiled Coil Peptide Containing D-Leu in A D-Site Position of A Tris-Thiolate Binding Site within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn101 b:17.8 occ:1.00 OE1 A:GLU34 1.9 20.1 1.0 NE2 A:HIS35 2.0 18.0 1.0 OE1 A:GLU31 2.0 17.3 1.0 CD A:GLU31 2.9 20.4 1.0 CD2 A:HIS35 3.0 18.2 1.0 CE1 A:HIS35 3.0 19.1 1.0 CD A:GLU34 3.0 32.8 1.0 OE2 A:GLU31 3.2 19.4 1.0 CG A:GLU34 3.6 26.1 1.0 OE2 A:GLU34 4.1 24.9 1.0 CG A:HIS35 4.1 17.9 1.0 ND1 A:HIS35 4.1 18.7 1.0 CB A:GLU34 4.1 19.2 1.0 CG A:GLU31 4.3 17.1 1.0 CB A:GLU31 4.7 13.7 1.0 CA A:GLU31 4.8 12.8 1.0

L.Ruckthong, J.A.Stuckey, V.L.Pecoraro. How Outer Coordination Sphere Modifications Can Impact Metal Structures in Proteins: A Crystallographic Evaluation. Chemistry V. 25 6773 2019.
ISSN: ISSN 0947-6539
PubMed: 30861211
DOI: 10.1002/CHEM.201806040