Zinc in PDB 3iqs: Crystal Structure of the Anti-Viral APOBEC3G Catalytic Domain

The structure of Crystal Structure of the Anti-Viral APOBEC3G Catalytic Domain, PDB code: 3iqs was solved by L.G.Holden, C.Prochnow, Y.P.Chang, R.Bransteitter, L.Chelico, U.Sen, R.C.Stevens, R.F.Goodman, X.S.Chen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.00 / 2.30
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	83.464, 57.329, 40.578, 90.00, 96.46, 90.00
R / Rfree (%)	25.1 / 26.3

The binding sites of Zinc atom in the Crystal Structure of the Anti-Viral APOBEC3G Catalytic Domain (pdb code 3iqs). 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 the Anti-Viral APOBEC3G Catalytic Domain, PDB code: 3iqs:

Zinc binding site 1 out of 1 in the Crystal Structure of the Anti-Viral APOBEC3G Catalytic Domain


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 Anti-Viral APOBEC3G Catalytic Domain within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn400 b:31.8 occ:1.00 ND1 A:HIS257 2.2 29.2 1.0 SG A:CYS291 2.3 22.8 1.0 SG A:CYS288 2.4 24.7 1.0 O A:HOH426 2.5 25.4 1.0 CB A:CYS291 3.2 24.5 1.0 CG A:HIS257 3.2 28.1 1.0 CE1 A:HIS257 3.2 29.0 1.0 CB A:CYS288 3.3 23.1 1.0 CB A:HIS257 3.5 27.9 1.0 N A:CYS291 3.9 25.5 1.0 N A:CYS288 4.0 23.4 1.0 CA A:CYS291 4.1 24.9 1.0 OE2 A:GLU259 4.2 25.1 1.0 CA A:CYS288 4.2 24.0 1.0 NE2 A:HIS257 4.3 29.4 1.0 CD2 A:HIS257 4.3 27.6 1.0 O A:HOH428 4.4 42.0 1.0 C A:CYS288 4.7 24.5 1.0 O A:CYS288 4.7 23.4 1.0 CD A:GLU259 4.7 24.0 1.0 C A:SER290 5.0 26.4 1.0 CA A:HIS257 5.0 27.7 1.0

L.G.Holden, C.Prochnow, Y.P.Chang, R.Bransteitter, L.Chelico, U.Sen, R.C.Stevens, M.F.Goodman, X.S.Chen. Crystal Structure of the Anti-Viral APOBEC3G Catalytic Domain and Functional Implications. Nature V. 456 121 2008.
ISSN: ISSN 0028-0836
PubMed: 18849968
DOI: 10.1038/NATURE07357