Zinc in PDB 5vzt: Crystal Structure of the SKP1-FBXO31 Complex

The structure of Crystal Structure of the SKP1-FBXO31 Complex, PDB code: 5vzt was solved by Y.Li, K.Jin, B.Hao, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 2.70
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	87.521, 156.310, 154.596, 90.00, 103.62, 90.00
R / Rfree (%)	19.5 / 24.2

The binding sites of Zinc atom in the Crystal Structure of the SKP1-FBXO31 Complex (pdb code 5vzt). 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 the SKP1-FBXO31 Complex, PDB code: 5vzt:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Crystal Structure of the SKP1-FBXO31 Complex


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 the SKP1-FBXO31 Complex within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn601 b:29.6 occ:1.00 NE2 B:HIS236 2.2 59.5 1.0 NE2 B:HIS214 2.3 61.2 1.0 SG B:CYS206 2.3 49.1 1.0 SG B:CYS230 2.3 47.7 1.0 CE1 B:HIS236 3.0 63.4 1.0 CE1 B:HIS214 3.1 65.9 1.0 CB B:CYS230 3.1 51.0 1.0 O B:TYR208 3.2 0.4 1.0 CD2 B:HIS214 3.2 69.5 1.0 CB B:CYS206 3.2 53.4 1.0 CD2 B:HIS236 3.4 73.2 1.0 ND1 B:HIS214 4.2 68.0 1.0 ND1 B:HIS236 4.2 72.2 1.0 CG B:HIS214 4.3 65.7 1.0 C B:TYR208 4.3 98.0 1.0 CG B:HIS236 4.4 82.3 1.0 CA B:CYS230 4.4 59.0 1.0 O B:GLN232 4.5 67.9 1.0 CB B:TYR208 4.5 77.7 1.0 CA B:CYS206 4.5 50.2 1.0 N B:TYR208 4.6 70.7 1.0 C B:CYS206 4.7 58.3 1.0 ND2 B:ASN282 4.7 86.4 1.0 CA B:TYR208 4.8 76.3 1.0 O B:CYS206 4.8 58.0 1.0 CA B:THR233 4.9 70.0 1.0 C B:GLN232 5.0 75.3 1.0

Zinc binding site 2 out of 2 in the Crystal Structure of the SKP1-FBXO31 Complex


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 the SKP1-FBXO31 Complex within 5.0Å range: probe atom residue distance (Å) B Occ D:Zn601 b:28.3 occ:1.00 NE2 D:HIS236 2.2 42.1 1.0 NE2 D:HIS214 2.3 53.4 1.0 SG D:CYS206 2.3 43.1 1.0 SG D:CYS230 2.3 44.1 1.0 CE1 D:HIS236 2.8 38.8 1.0 CD2 D:HIS214 3.1 55.3 1.0 CB D:CYS230 3.1 39.5 1.0 CB D:CYS206 3.2 47.7 1.0 CE1 D:HIS214 3.3 55.5 1.0 CD2 D:HIS236 3.4 44.3 1.0 ND1 D:HIS236 4.0 42.5 1.0 CG D:HIS214 4.3 46.5 1.0 CG D:HIS236 4.4 43.6 1.0 ND1 D:HIS214 4.4 56.1 1.0 O D:GLN232 4.4 48.9 1.0 CB D:TYR208 4.5 61.2 1.0 CA D:CYS230 4.5 37.0 1.0 CA D:CYS206 4.6 49.8 1.0 C D:CYS206 4.8 47.1 1.0 C D:GLN232 4.8 51.9 1.0 O D:TYR208 4.8 76.3 1.0 CA D:THR233 4.9 41.2 1.0 O D:CYS206 4.9 53.2 1.0 N D:TYR208 4.9 64.2 1.0

Y.Li, K.Jin, E.Bunker, X.Zhang, X.Luo, X.Liu, B.Hao. Structural Basis of the Phosphorylation-Independent Recognition of Cyclin D1 By the SCFFBXO31 Ubiquitin Ligase. Proc. Natl. Acad. Sci. V. 115 319 2018U.S.A..
ISSN: ESSN 1091-6490
PubMed: 29279382
DOI: 10.1073/PNAS.1708677115