Zinc in PDB 2di2: uc(Nmr) Structure of the Hiv-2 Nucleocapsid Protein

The binding sites of Zinc atom in the uc(Nmr) Structure of the Hiv-2 Nucleocapsid Protein (pdb code 2di2). 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 uc(Nmr) Structure of the Hiv-2 Nucleocapsid Protein, PDB code: 2di2:

Zinc binding site 1 out of 1 in the uc(Nmr) Structure of the Hiv-2 Nucleocapsid Protein


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of uc(Nmr) Structure of the Hiv-2 Nucleocapsid Protein within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn30 b:0.0 occ:1.00 NE2 A:HIS17 2.0 0.0 1.0 HA A:CYS22 2.1 0.0 1.0 HD2 A:HIS17 2.3 0.0 1.0 SG A:CYS9 2.3 0.0 1.0 SG A:CYS22 2.3 0.0 1.0 SG A:CYS12 2.3 0.0 1.0 CD2 A:HIS17 2.4 0.0 1.0 HB2 A:CYS12 2.7 0.0 1.0 CB A:CYS12 3.0 0.0 1.0 CA A:CYS22 3.1 0.0 1.0 CB A:CYS9 3.1 0.0 1.0 HB3 A:CYS9 3.2 0.0 1.0 HB2 A:CYS9 3.2 0.0 1.0 CB A:CYS22 3.3 0.0 1.0 CE1 A:HIS17 3.3 0.0 1.0 HB3 A:CYS12 3.4 0.0 1.0 H A:ARG23 3.5 0.0 1.0 H A:ALA24 3.6 0.0 1.0 CG A:HIS17 3.8 0.0 1.0 HB1 A:ALA24 3.9 0.0 1.0 HE1 A:HIS17 3.9 0.0 1.0 C A:CYS22 3.9 0.0 1.0 HB2 A:CYS22 4.0 0.0 1.0 HB2 A:ALA24 4.0 0.0 1.0 N A:ARG23 4.0 0.0 1.0 HB3 A:CYS22 4.0 0.0 1.0 N A:CYS22 4.2 0.0 1.0 ND1 A:HIS17 4.2 0.0 1.0 H A:CYS12 4.3 0.0 1.0 HA A:ALA19 4.3 0.0 1.0 CA A:CYS12 4.4 0.0 1.0 HB2 A:LYS14 4.4 0.0 1.0 N A:CYS12 4.4 0.0 1.0 CB A:ALA24 4.4 0.0 1.0 N A:ALA24 4.5 0.0 1.0 CA A:CYS9 4.6 0.0 1.0 H A:CYS22 4.6 0.0 1.0 H A:GLY13 4.6 0.0 1.0 HB3 A:ALA11 4.6 0.0 1.0 O A:CYS9 4.7 0.0 1.0 O A:CYS22 4.9 0.0 1.0 H A:LYS14 4.9 0.0 1.0 O A:GLN21 4.9 0.0 1.0 HA A:CYS9 4.9 0.0 1.0 C A:GLN21 4.9 0.0 1.0 O A:SER18 4.9 0.0 1.0 HA A:CYS12 5.0 0.0 1.0 HD3 A:LYS14 5.0 0.0 1.0

T.Matsui, Y.Kodera, H.Endoh, E.Miyauchi, H.Komatsu, K.Sato, T.Tanaka, T.Kohno, T.Maeda. Rna Recognition Mechanism of the Minimal Active Domain of the Human Immunodeficiency Virus Type-2 Nucleocapsid Protein J.Biochem.(Tokyo) V. 141 269 2007.
ISSN: ISSN 0021-924X
PubMed: 17202191
DOI: 10.1093/JB/MVM037