Zinc in PDB 5fey: TRIM32 Ring

The structure of TRIM32 Ring, PDB code: 5fey was solved by K.Rittinger, D.Esposito, M.G.Koliopoulos, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	47.78 / 2.23
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	54.536, 54.536, 99.120, 90.00, 90.00, 90.00
R / Rfree (%)	24.8 / 27.3

The binding sites of Zinc atom in the TRIM32 Ring (pdb code 5fey). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the TRIM32 Ring, PDB code: 5fey:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in the TRIM32 Ring


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of TRIM32 Ring within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn101 b:0.8 occ:1.00 SG A:CYS44 2.4 73.4 1.0 SG A:CYS23 2.4 93.5 1.0 SG A:CYS20 2.4 84.1 1.0 SG A:CYS47 2.4 0.8 1.0 CB A:CYS20 2.9 80.1 1.0 CB A:CYS44 3.3 69.8 1.0 CB A:CYS23 3.4 99.2 1.0 CB A:CYS47 3.4 98.0 1.0 N A:CYS23 3.7 99.1 1.0 CA A:CYS23 4.1 0.6 1.0 N A:CYS44 4.2 63.5 1.0 N A:CYS47 4.2 95.8 1.0 CA A:CYS44 4.3 65.3 1.0 CA A:CYS20 4.4 77.1 1.0 CA A:CYS47 4.4 0.5 1.0 CB A:ILE22 4.6 93.9 1.0 CD1 A:LEU32 4.7 0.8 1.0 C A:ILE22 4.8 0.2 1.0 C A:CYS23 4.9 0.7 1.0 C A:CYS44 4.9 72.4 1.0 C A:CYS20 4.9 85.9 1.0 N A:ILE22 5.0 95.1 1.0

Zinc binding site 2 out of 4 in the TRIM32 Ring


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of TRIM32 Ring within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn102 b:0.2 occ:1.00 ND1 A:HIS41 2.2 89.2 1.0 SG A:CYS39 2.4 64.5 1.0 SG A:CYS61 2.4 93.0 1.0 SG A:CYS64 2.5 93.7 1.0 CE1 A:HIS41 3.0 90.9 1.0 CB A:CYS61 3.2 94.6 1.0 CG A:HIS41 3.2 79.8 1.0 CB A:CYS39 3.3 75.0 1.0 O A:CYS64 3.5 0.8 1.0 CB A:CYS64 3.5 0.8 1.0 N A:CYS64 3.6 0.4 1.0 CB A:HIS41 3.6 72.7 1.0 CA A:CYS64 3.9 0.5 1.0 C A:CYS64 4.1 0.9 1.0 NE2 A:HIS41 4.2 86.8 1.0 CD2 A:HIS41 4.3 81.0 1.0 N A:HIS41 4.5 73.0 1.0 CA A:CYS39 4.6 75.4 1.0 O A:HOH209 4.6 0.1 1.0 CA A:CYS61 4.6 98.5 1.0 CA A:HIS41 4.7 68.0 1.0 C A:CYS39 4.7 76.5 1.0 C A:PHE63 4.7 0.9 1.0 O A:CYS39 4.8 78.6 1.0 CB A:PHE63 4.8 0.1 1.0 N A:PHE63 5.0 0.5 1.0

Zinc binding site 3 out of 4 in the TRIM32 Ring


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of TRIM32 Ring within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn101 b:81.2 occ:1.00 SG B:CYS44 2.4 65.0 1.0 SG B:CYS23 2.4 78.8 1.0 SG B:CYS20 2.4 63.9 1.0 SG B:CYS47 2.5 82.5 1.0 CB B:CYS20 3.0 62.7 1.0 CB B:CYS44 3.3 62.4 1.0 CB B:CYS23 3.3 87.6 1.0 CB B:CYS47 3.3 78.4 1.0 N B:CYS23 3.7 83.4 1.0 CA B:CYS23 4.1 89.2 1.0 N B:CYS44 4.1 57.8 1.0 N B:CYS47 4.2 83.0 1.0 CA B:CYS44 4.3 62.6 1.0 CA B:CYS47 4.4 81.9 1.0 CA B:CYS20 4.5 61.8 1.0 CB B:ILE22 4.6 79.2 1.0 C B:ILE22 4.8 84.1 1.0 C B:CYS44 4.9 69.9 1.0 C B:CYS23 4.9 93.6 1.0 C B:CYS20 5.0 63.7 1.0 N B:ILE22 5.0 74.0 1.0

Zinc binding site 4 out of 4 in the TRIM32 Ring


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of TRIM32 Ring within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn102 b:81.8 occ:1.00 ND1 B:HIS41 2.3 79.0 1.0 SG B:CYS39 2.4 53.8 1.0 SG B:CYS64 2.4 69.4 1.0 SG B:CYS61 2.4 70.4 1.0 CE1 B:HIS41 3.1 81.0 1.0 CB B:CYS61 3.2 76.6 1.0 CG B:HIS41 3.3 68.9 1.0 CB B:CYS39 3.4 61.0 1.0 CB B:CYS64 3.6 80.9 1.0 O B:CYS64 3.6 0.5 1.0 CB B:HIS41 3.7 58.4 1.0 N B:CYS64 3.7 86.5 1.0 CA B:CYS64 4.0 88.1 1.0 C B:CYS64 4.2 95.3 1.0 NE2 B:HIS41 4.2 77.4 1.0 CD2 B:HIS41 4.3 72.9 1.0 CA B:CYS61 4.6 82.1 1.0 N B:HIS41 4.7 59.4 1.0 CA B:CYS39 4.7 64.1 1.0 CA B:HIS41 4.8 57.6 1.0 C B:PHE63 4.9 90.7 1.0 C B:CYS39 4.9 64.9 1.0 CB B:PHE63 5.0 90.0 1.0

M.G.Koliopoulos, D.Esposito, E.Christodoulou, I.A.Taylor, K.Rittinger. Functional Role of Trim E3 Ligase Oligomerization and Regulation of Catalytic Activity. Embo J. V. 35 1204 2016.
ISSN: ESSN 1460-2075
PubMed: 27154206
DOI: 10.15252/EMBJ.201593741