Zinc in PDB 3gj3: Crystal Structure of Human Rangdp-NUP153ZNF2 Complex

The structure of Crystal Structure of Human Rangdp-NUP153ZNF2 Complex, PDB code: 3gj3 was solved by J.R.Partridge, T.U.Schwartz, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	33.30 / 1.79
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	59.709, 80.236, 57.960, 90.00, 90.00, 90.00
R / Rfree (%)	16.1 / 19.4

The structure of Crystal Structure of Human Rangdp-NUP153ZNF2 Complex also contains other interesting chemical elements:

Magnesium

(Mg)

1 atom

The binding sites of Zinc atom in the Crystal Structure of Human Rangdp-NUP153ZNF2 Complex (pdb code 3gj3). 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 Rangdp-NUP153ZNF2 Complex, PDB code: 3gj3:

Zinc binding site 1 out of 1 in the Crystal Structure of Human Rangdp-NUP153ZNF2 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 Human Rangdp-NUP153ZNF2 Complex within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn300 b:30.2 occ:1.00 SG B:CYS730 2.3 27.0 1.0 SG B:CYS744 2.3 31.6 1.0 SG B:CYS741 2.3 31.8 1.0 SG B:CYS727 2.4 31.0 1.0 CB B:CYS741 3.0 30.9 1.0 CB B:CYS727 3.1 28.8 1.0 CB B:CYS730 3.3 28.0 1.0 CB B:CYS744 3.4 36.9 1.0 N B:CYS744 3.8 30.7 1.0 N B:CYS730 3.8 31.3 1.0 CA B:CYS730 4.1 25.1 1.0 CA B:CYS744 4.1 31.7 1.0 CA B:CYS741 4.5 30.1 1.0 CA B:CYS727 4.6 30.5 1.0 CB B:ALA743 4.6 29.4 1.0 CB B:THR729 4.6 30.1 1.0 CB B:VAL732 4.6 33.4 1.0 C B:CYS730 4.7 27.8 1.0 N B:LEU731 4.8 29.6 1.0 C B:THR729 4.8 30.2 1.0 C B:CYS744 4.8 30.5 1.0 O B:HOH53 4.8 43.7 1.0 C B:ALA743 4.8 39.1 1.0 N B:VAL732 4.8 28.1 1.0 CB B:THR746 4.9 41.1 1.0 N B:GLU745 4.9 32.3 1.0 OG1 B:THR746 5.0 36.4 1.0

J.R.Partridge, T.U.Schwartz. Crystallographic and Biochemical Analysis of the Ran-Binding Zinc Finger Domain. J.Mol.Biol. V. 391 375 2009.
ISSN: ISSN 0022-2836
PubMed: 19505478
DOI: 10.1016/J.JMB.2009.06.011