Zinc in PDB 7jfs: The Structure of the CBM32-1, CBM32-2, and M60 Catalytic Domains From Clostridium Perfringens Zmpb

The structure of The Structure of the CBM32-1, CBM32-2, and M60 Catalytic Domains From Clostridium Perfringens Zmpb, PDB code: 7jfs was solved by B.Pluvinage, A.B.Boraston, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.93 / 4.60
Space group	P 61
Cell size a, b, c (Å), α, β, γ (°)	185.743, 185.743, 81.591, 90, 90, 120
R / Rfree (%)	26.1 / 30.9

The binding sites of Zinc atom in the The Structure of the CBM32-1, CBM32-2, and M60 Catalytic Domains From Clostridium Perfringens Zmpb (pdb code 7jfs). 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 The Structure of the CBM32-1, CBM32-2, and M60 Catalytic Domains From Clostridium Perfringens Zmpb, PDB code: 7jfs:

Zinc binding site 1 out of 1 in the The Structure of the CBM32-1, CBM32-2, and M60 Catalytic Domains From Clostridium Perfringens Zmpb


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of The Structure of the CBM32-1, CBM32-2, and M60 Catalytic Domains From Clostridium Perfringens Zmpb within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1101 b:129.1 occ:1.00 OE2 A:GLU771 1.7 83.8 1.0 OE1 A:GLU771 1.8 82.3 1.0 CD A:GLU771 1.9 83.7 1.0 NE2 A:HIS760 2.4 79.9 1.0 NE2 A:HIS756 2.6 79.1 1.0 CE1 A:HIS760 3.3 80.3 1.0 CE1 A:HIS756 3.4 79.9 1.0 CG A:GLU771 3.4 85.5 1.0 CD2 A:HIS760 3.5 78.1 1.0 CD2 A:HIS756 3.7 78.5 1.0 CB A:GLU771 4.3 86.2 1.0 ND2 A:ASN774 4.4 78.8 1.0 CA A:GLU771 4.5 83.9 1.0 ND1 A:HIS760 4.5 78.1 1.0 OE2 A:GLU757 4.5 77.1 1.0 ND1 A:HIS756 4.6 79.8 1.0 CG A:HIS760 4.6 76.9 1.0 CG A:HIS756 4.7 78.9 1.0 OE1 A:GLU757 4.9 76.2 1.0 N A:GLU771 5.0 83.4 1.0

B.Pluvinage, E.Ficko-Blean, I.Noach, C.Stuart, N.Thompson, H.Mcclure, N.Buenbrazo, W.Wakarchuck, A.B.Boraston. Molecular Insights Into Architecturally Complex Glycopeptidases To Be Published.