Zinc in PDB 4cc9: Crystal Structure of Human SAMHD1 (Amino Acid Residues 582- 626) Bound to Vpx Isolated From Sooty Mangabey and Human DCAF1 (Amino Acid Residues 1058-1396)

The structure of Crystal Structure of Human SAMHD1 (Amino Acid Residues 582- 626) Bound to Vpx Isolated From Sooty Mangabey and Human DCAF1 (Amino Acid Residues 1058-1396), PDB code: 4cc9 was solved by D.Schwefel, H.C.T.Groom, V.C.Boucherit, E.Christodoulou, P.A.Walker, J.P.Stoye, K.N.Bishop, I.A.Taylor, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.227 / 2.47
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	74.250, 82.881, 115.561, 90.00, 90.00, 90.00
R / Rfree (%)	17.57 / 21.64

The binding sites of Zinc atom in the Crystal Structure of Human SAMHD1 (Amino Acid Residues 582- 626) Bound to Vpx Isolated From Sooty Mangabey and Human DCAF1 (Amino Acid Residues 1058-1396) (pdb code 4cc9). 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 Crystal Structure of Human SAMHD1 (Amino Acid Residues 582- 626) Bound to Vpx Isolated From Sooty Mangabey and Human DCAF1 (Amino Acid Residues 1058-1396), PDB code: 4cc9:

Zinc binding site 1 out of 1 in the Crystal Structure of Human SAMHD1 (Amino Acid Residues 582- 626) Bound to Vpx Isolated From Sooty Mangabey and Human DCAF1 (Amino Acid Residues 1058-1396)


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 Human SAMHD1 (Amino Acid Residues 582- 626) Bound to Vpx Isolated From Sooty Mangabey and Human DCAF1 (Amino Acid Residues 1058-1396) within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn1112 b:43.9 occ:1.00 ND1 B:HIS39 2.0 40.4 1.0 NE2 B:HIS82 2.1 34.8 1.0 SG B:CYS87 2.3 64.2 1.0 SG B:CYS89 2.3 60.4 1.0 CE1 B:HIS39 2.9 41.0 1.0 CB B:CYS89 2.9 85.6 1.0 CE1 B:HIS82 3.0 30.4 1.0 CD2 B:HIS82 3.0 28.4 1.0 CG B:HIS39 3.1 33.4 1.0 CB B:CYS87 3.4 64.6 1.0 CB B:HIS39 3.5 20.7 1.0 CA B:HIS39 3.9 26.8 1.0 NE2 B:HIS39 4.0 44.4 1.0 CA B:CYS89 4.1 88.0 1.0 N B:CYS89 4.1 86.6 1.0 ND1 B:HIS82 4.1 33.2 1.0 CD2 B:HIS39 4.1 36.4 1.0 CG B:HIS82 4.2 24.8 1.0 CA B:CYS87 4.3 68.8 1.0 O B:ASN38 4.5 48.0 1.0 C B:CYS87 4.7 75.9 1.0 O B:HIS39 4.8 38.9 1.0 C B:HIS39 4.9 32.6 1.0 N B:ARG88 4.9 79.1 1.0 N B:HIS39 5.0 33.9 1.0

D.Schwefel, H.C.T.Groom, V.C.Boucherit, E.Christodoulou, P.A.Walker, J.P.Stoye, K.N.Bishop, I.A.Taylor. Structural Basis of Lentiviral Subversion of A Cellular Protein Degradation Pathway. Nature V. 505 234 2014.
ISSN: ISSN 0028-0836
PubMed: 24336198
DOI: 10.1038/NATURE12815