Zinc in PDB 5vno: Crystal Structure of SEC23A/SEC24A/SEC22

The structure of Crystal Structure of SEC23A/SEC24A/SEC22, PDB code: 5vno was solved by W.Ma, J.Goldberg, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	49.94 / 2.91
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	158.046, 96.727, 126.796, 90.00, 91.45, 90.00
R / Rfree (%)	24.4 / 29.8

The binding sites of Zinc atom in the Crystal Structure of SEC23A/SEC24A/SEC22 (pdb code 5vno). 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 SEC23A/SEC24A/SEC22, PDB code: 5vno:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Crystal Structure of SEC23A/SEC24A/SEC22


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 SEC23A/SEC24A/SEC22 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn801 b:0.1 occ:1.00 SG A:CYS85 2.1 80.9 1.0 SG A:CYS88 2.2 88.5 1.0 SG A:CYS61 2.4 0.3 1.0 SG A:CYS66 2.5 97.2 1.0 CB A:CYS85 2.7 86.3 1.0 CB A:CYS61 3.3 97.0 1.0 CB A:CYS66 3.4 0.1 1.0 CB A:CYS88 3.6 95.0 1.0 N A:CYS88 4.0 81.3 1.0 CA A:CYS85 4.2 84.2 1.0 CA A:CYS88 4.3 99.4 1.0 CB A:GLN90 4.3 0.3 1.0 N A:GLN90 4.7 0.9 1.0 C A:CYS88 4.7 0.1 1.0 N A:ARG67 4.7 0.8 1.0 N A:ALA68 4.7 88.4 1.0 CB A:ALA68 4.8 80.3 1.0 CA A:CYS61 4.8 96.9 1.0 CA A:CYS66 4.8 0.5 1.0 C A:CYS85 4.9 94.6 1.0 N A:TYR89 4.9 0.5 1.0 CB A:ARG63 4.9 0.2 1.0 CB A:PHE87 5.0 91.2 1.0

Zinc binding site 2 out of 2 in the Crystal Structure of SEC23A/SEC24A/SEC22


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 SEC23A/SEC24A/SEC22 within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn1101 b:0.3 occ:1.00 SG B:CYS434 2.2 0.6 1.0 SG B:CYS431 2.2 0.5 1.0 SG B:CYS455 2.3 96.6 1.0 SG B:CYS452 2.4 0.6 1.0 CB B:CYS431 2.9 0.9 1.0 CB B:CYS452 3.1 0.2 1.0 CB B:CYS455 3.5 92.8 1.0 CB B:CYS434 3.7 0.4 1.0 N B:CYS434 3.8 0.7 1.0 N B:CYS455 3.9 89.0 1.0 CA B:CYS455 4.2 91.1 1.0 CA B:CYS434 4.3 0.4 1.0 CA B:CYS431 4.4 0.0 1.0 OG1 B:THR436 4.5 94.0 1.0 CB B:THR436 4.5 96.0 1.0 CA B:CYS452 4.6 0.3 1.0 C B:CYS455 4.7 94.0 1.0 CB B:SER433 4.7 0.4 1.0 C B:CYS434 4.7 0.8 1.0 N B:THR436 4.8 0.1 1.0 N B:ARG435 4.8 0.7 1.0 C B:LEU454 4.9 89.9 1.0 ND2 B:ASN459 4.9 1.0 1.0 CB B:ARG457 4.9 0.9 1.0 N B:TYR456 4.9 96.5 1.0 C B:CYS431 4.9 0.8 1.0 CB B:LEU454 4.9 89.8 1.0 C B:SER433 5.0 0.5 1.0 N B:ARG457 5.0 0.6 1.0 N B:SER433 5.0 0.5 1.0

W.Ma, E.Goldberg, J.Goldberg. Er Retention Is Imposed By Copii Protein Sorting and Attenuated By 4-Phenylbutyrate. Elife V. 6 2017.
ISSN: ESSN 2050-084X
PubMed: 28594326
DOI: 10.7554/ELIFE.26624