Zinc in PDB 2e1x: 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 2e1x). 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: 2e1x:

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:Zn50 b:0.0 occ:1.00 NE2 A:HIS38 2.0 0.0 1.0 CE1 A:HIS38 2.2 0.0 1.0 SG A:CYS30 2.3 0.0 1.0 SG A:CYS43 2.3 0.0 1.0 SG A:CYS33 2.3 0.0 1.0 HE1 A:HIS38 2.5 0.0 1.0 CD2 A:HIS38 2.7 0.0 1.0 ND1 A:HIS38 2.9 0.0 1.0 HB3 A:LYS35 3.0 0.0 1.0 CG A:HIS38 3.1 0.0 1.0 HD2 A:HIS38 3.3 0.0 1.0 CB A:CYS33 3.5 0.0 1.0 HB3 A:CYS33 3.6 0.0 1.0 H A:CYS30 3.6 0.0 1.0 HD1 A:HIS38 3.6 0.0 1.0 HB2 A:CYS30 3.6 0.0 1.0 CB A:CYS30 3.7 0.0 1.0 HB2 A:CYS33 3.7 0.0 1.0 O A:HIS38 3.8 0.0 1.0 O A:LYS35 3.8 0.0 1.0 HA A:CYS43 3.8 0.0 1.0 HB2 A:LYS35 3.8 0.0 1.0 CB A:LYS35 3.8 0.0 1.0 H A:LYS35 3.9 0.0 1.0 HD2 A:PRO44 3.9 0.0 1.0 HD3 A:PRO44 4.0 0.0 1.0 CB A:CYS43 4.0 0.0 1.0 HE2 A:LYS35 4.2 0.0 1.0 HB3 A:CYS30 4.3 0.0 1.0 C A:HIS38 4.4 0.0 1.0 N A:CYS30 4.4 0.0 1.0 N A:LYS35 4.4 0.0 1.0 C A:LYS35 4.4 0.0 1.0 CB A:HIS38 4.4 0.0 1.0 CD A:PRO44 4.4 0.0 1.0 CA A:CYS43 4.5 0.0 1.0 CA A:LYS35 4.5 0.0 1.0 HB3 A:CYS43 4.5 0.0 1.0 HA A:VAL39 4.5 0.0 1.0 HB2 A:HIS38 4.5 0.0 1.0 HB2 A:CYS43 4.7 0.0 1.0 H A:GLY34 4.7 0.0 1.0 CA A:CYS30 4.7 0.0 1.0 O A:VAL39 4.8 0.0 1.0 H A:CYS33 4.9 0.0 1.0 CA A:CYS33 4.9 0.0 1.0 O A:THR36 4.9 0.0 1.0 N A:VAL39 5.0 0.0 1.0 CA A:HIS38 5.0 0.0 1.0

T.Matsui, Y.Kodera, E.Miyauchi, H.Tanaka, H.Endoh, H.Komatsu, T.Tanaka, T.Kohno, T.Maeda. Structural Role of the Secondary Active Domain of Hiv-2 NCP8 in Multi-Functionality Biochem.Biophys.Res.Commun. V. 358 673 2007.
ISSN: ISSN 0006-291X
PubMed: 17511966
DOI: 10.1016/J.BBRC.2007.04.141