Zinc in PDB 1x3z: Structure of A Peptide:N-Glycanase-RAD23 Complex

All present enzymatic activity of Structure of A Peptide:N-Glycanase-RAD23 Complex:
3.5.1.52;

The structure of Structure of A Peptide:N-Glycanase-RAD23 Complex, PDB code: 1x3z was solved by J.-H.Lee, J.M.Choi, C.Lee, K.J.Yi, Y.Cho, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 2.80
Space group	P 31 2 1
Cell size a, b, c (Å), α, β, γ (°)	128.801, 128.801, 128.376, 90.00, 90.00, 120.00
R / Rfree (%)	23.6 / 27

The binding sites of Zinc atom in the Structure of A Peptide:N-Glycanase-RAD23 Complex (pdb code 1x3z). 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 Structure of A Peptide:N-Glycanase-RAD23 Complex, PDB code: 1x3z:

Zinc binding site 1 out of 1 in the Structure of A Peptide:N-Glycanase-RAD23 Complex


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structure of A Peptide:N-Glycanase-RAD23 Complex within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn999 b:62.0 occ:1.00 SG A:CYS132 2.1 73.4 1.0 SG A:CYS168 2.3 57.7 1.0 SG A:CYS165 2.3 51.2 1.0 SG A:CYS129 2.3 65.0 1.0 CB A:CYS165 3.1 52.2 1.0 CB A:CYS168 3.2 57.3 1.0 CB A:CYS132 3.4 74.9 1.0 CB A:CYS129 3.5 64.8 1.0 N A:CYS168 3.8 57.0 1.0 N A:CYS132 3.8 74.8 1.0 CA A:CYS168 4.1 57.2 1.0 CA A:CYS132 4.2 75.5 1.0 CD2 A:HIS131 4.5 79.6 1.0 CA A:CYS165 4.5 52.2 1.0 CB A:ARG167 4.6 57.1 1.0 C A:ARG167 4.6 56.7 1.0 N A:GLY169 4.7 57.5 1.0 C A:CYS168 4.7 57.3 1.0 CB A:HIS131 4.8 75.0 1.0 N A:ARG167 4.8 55.5 1.0 CA A:CYS129 4.8 64.8 1.0 C A:HIS131 4.9 74.2 1.0 N A:ASN170 4.9 58.6 1.0 C A:CYS165 4.9 52.9 1.0 CA A:ARG167 4.9 56.6 1.0 CB A:ASN170 5.0 59.1 1.0

J.H.Lee, J.M.Choi, C.Lee, K.J.Yi, Y.Cho. Structure of A Peptide:N-Glycanase-RAD23 Complex: Insight Into the Deglycosylation For Denatured Glycoproteins. Proc.Natl.Acad.Sci.Usa V. 102 9144 2005.
ISSN: ISSN 0027-8424
PubMed: 15964983
DOI: 10.1073/PNAS.0502082102