Zinc in PDB 2ms1: Solution uc(Nmr) Structure of Trnapro:Mlv Nucleocapsid Protein (1:1) Complex

The binding sites of Zinc atom in the Solution uc(Nmr) Structure of Trnapro:Mlv Nucleocapsid Protein (1:1) Complex (pdb code 2ms1). 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 Solution uc(Nmr) Structure of Trnapro:Mlv Nucleocapsid Protein (1:1) Complex, PDB code: 2ms1:

Zinc binding site 1 out of 1 in the Solution uc(Nmr) Structure of Trnapro:Mlv Nucleocapsid Protein (1:1) Complex


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Solution uc(Nmr) Structure of Trnapro:Mlv Nucleocapsid Protein (1:1) Complex within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn101 b:0.0 occ:1.00 NE2 A:HIS34 2.4 0.0 1.0 SG A:CYS29 2.6 0.0 1.0 SG A:CYS39 2.6 0.0 1.0 SG A:CYS26 2.6 0.0 1.0 HD2 A:PRO40 2.8 0.0 1.0 HB2 A:CYS39 3.0 0.0 1.0 HA A:CYS39 3.1 0.0 1.0 HB3 A:CYS26 3.1 0.0 1.0 HB2 A:CYS26 3.2 0.0 1.0 CB A:CYS26 3.2 0.0 1.0 CB A:CYS39 3.3 0.0 1.0 CD2 A:HIS34 3.3 0.0 1.0 HD2 A:HIS34 3.3 0.0 1.0 H A:CYS29 3.4 0.0 1.0 HB3 A:CYS29 3.4 0.0 1.0 HB2 A:GLU31 3.5 0.0 1.0 CE1 A:HIS34 3.6 0.0 1.0 CB A:CYS29 3.6 0.0 1.0 CA A:CYS39 3.7 0.0 1.0 CD A:PRO40 3.9 0.0 1.0 HE1 A:HIS34 3.9 0.0 1.0 HB3 A:TYR28 4.0 0.0 1.0 H A:GLU31 4.1 0.0 1.0 N A:CYS29 4.1 0.0 1.0 HD3 A:PRO40 4.1 0.0 1.0 HA A:ALA36 4.2 0.0 1.0 HB3 A:CYS39 4.3 0.0 1.0 H A:LYS41 4.4 0.0 1.0 CA A:CYS29 4.4 0.0 1.0 CG A:HIS34 4.5 0.0 1.0 HB2 A:CYS29 4.5 0.0 1.0 N A:PRO40 4.6 0.0 1.0 C A:CYS39 4.6 0.0 1.0 CB A:GLU31 4.6 0.0 1.0 ND1 A:HIS34 4.6 0.0 1.0 HD2 A:TYR28 4.6 0.0 1.0 CA A:CYS26 4.7 0.0 1.0 HG2 A:PRO40 4.7 0.0 1.0 H A:LYS30 4.7 0.0 1.0 N A:CYS39 4.8 0.0 1.0 H A:TYR28 4.8 0.0 1.0 CG A:PRO40 4.9 0.0 1.0 HB3 A:LYS41 4.9 0.0 1.0 HG3 A:GLU31 4.9 0.0 1.0 HB2 A:LYS41 4.9 0.0 1.0 O A:TRP35 4.9 0.0 1.0 C A:CYS29 4.9 0.0 1.0 N A:GLU31 5.0 0.0 1.0

S.B.Miller, F.Z.Yildiz, J.A.Lo, B.Wang, V.M.D'souza. A Structure-Based Mechanism For Trna and Retroviral Rna Remodelling During Primer Annealing. Nature 2014.
ISSN: ESSN 1476-4687
PubMed: 25209668
DOI: 10.1038/NATURE13709