Zinc in PDB 1lpv: Drosophila Melanogaster Doublesex (Dsx), uc(Nmr), 18 Structures

The binding sites of Zinc atom in the Drosophila Melanogaster Doublesex (Dsx), uc(Nmr), 18 Structures (pdb code 1lpv). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Drosophila Melanogaster Doublesex (Dsx), uc(Nmr), 18 Structures, PDB code: 1lpv:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Drosophila Melanogaster Doublesex (Dsx), uc(Nmr), 18 Structures


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Drosophila Melanogaster Doublesex (Dsx), uc(Nmr), 18 Structures within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn53 b:0.0 occ:1.00 NE2 A:HIS16 2.0 0.0 1.0 SG A:CYS36 2.3 0.0 1.0 SG A:CYS34 2.3 0.0 1.0 SG A:CYS39 2.3 0.0 1.0 HB2 A:CYS39 2.7 0.0 1.0 HB3 A:CYS34 3.0 0.0 1.0 CE1 A:HIS16 3.0 0.0 1.0 CB A:CYS39 3.1 0.0 1.0 CD2 A:HIS16 3.1 0.0 1.0 HD2 A:PHE31 3.2 0.0 1.0 CB A:CYS34 3.2 0.0 1.0 HB3 A:CYS36 3.2 0.0 1.0 HE1 A:HIS16 3.2 0.0 1.0 H A:CYS36 3.3 0.0 1.0 HD2 A:HIS16 3.3 0.0 1.0 CB A:CYS36 3.4 0.0 1.0 HB3 A:ASN15 3.6 0.0 1.0 HB2 A:CYS34 3.7 0.0 1.0 HB2 A:ASN15 3.7 0.0 1.0 HB3 A:PHE31 3.8 0.0 1.0 H A:CYS39 3.8 0.0 1.0 HB3 A:CYS39 3.8 0.0 1.0 N A:CYS36 3.9 0.0 1.0 N A:CYS39 4.1 0.0 1.0 CB A:ASN15 4.1 0.0 1.0 CA A:CYS39 4.1 0.0 1.0 CD2 A:PHE31 4.1 0.0 1.0 H A:THR35 4.2 0.0 1.0 HB2 A:CYS36 4.2 0.0 1.0 HD21 A:ASN15 4.2 0.0 1.0 ND1 A:HIS16 4.2 0.0 1.0 CG A:HIS16 4.2 0.0 1.0 CA A:CYS36 4.2 0.0 1.0 O A:ARG12 4.4 0.0 1.0 HA A:CYS39 4.4 0.0 1.0 N A:THR35 4.4 0.0 1.0 CA A:CYS34 4.5 0.0 1.0 H A:LYS38 4.6 0.0 1.0 C A:CYS34 4.6 0.0 1.0 HB2 A:LYS38 4.6 0.0 1.0 ND2 A:ASN15 4.7 0.0 1.0 CG A:ASN15 4.7 0.0 1.0 CB A:PHE31 4.7 0.0 1.0 HE A:ARG12 4.8 0.0 1.0 C A:CYS36 4.8 0.0 1.0 C A:THR35 4.9 0.0 1.0 HE2 A:PHE31 4.9 0.0 1.0 O A:CYS36 4.9 0.0 1.0 HG3 A:ARG12 4.9 0.0 1.0 CG A:PHE31 4.9 0.0 1.0 HA A:CYS34 4.9 0.0 1.0 C A:LYS38 5.0 0.0 1.0 HB3 A:LYS38 5.0 0.0 1.0 CE2 A:PHE31 5.0 0.0 1.0

Zinc binding site 2 out of 2 in the Drosophila Melanogaster Doublesex (Dsx), uc(Nmr), 18 Structures


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Drosophila Melanogaster Doublesex (Dsx), uc(Nmr), 18 Structures within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn54 b:0.0 occ:1.00 NE2 A:HIS25 2.1 0.0 1.0 SG A:CYS10 2.2 0.0 1.0 SG A:CYS29 2.3 0.0 1.0 HB3 A:CYS13 2.3 0.0 1.0 SG A:CYS13 2.3 0.0 1.0 HB3 A:CYS10 2.5 0.0 1.0 H A:CYS13 2.5 0.0 1.0 HD13 A:ILE20 2.7 0.0 1.0 CB A:CYS13 2.8 0.0 1.0 CB A:CYS10 2.8 0.0 1.0 CD2 A:HIS25 2.8 0.0 1.0 HD2 A:HIS25 2.9 0.0 1.0 HB3 A:ARG12 3.0 0.0 1.0 HB2 A:CYS29 3.0 0.0 1.0 CB A:CYS29 3.2 0.0 1.0 HB2 A:CYS10 3.2 0.0 1.0 HA A:CYS29 3.2 0.0 1.0 CE1 A:HIS25 3.2 0.0 1.0 N A:CYS13 3.2 0.0 1.0 HB2 A:CYS13 3.6 0.0 1.0 HE1 A:HIS25 3.6 0.0 1.0 CA A:CYS13 3.7 0.0 1.0 HG21 A:ILE20 3.7 0.0 1.0 CD1 A:ILE20 3.7 0.0 1.0 CA A:CYS29 3.7 0.0 1.0 HG23 A:ILE20 3.7 0.0 1.0 HD11 A:ILE20 3.8 0.0 1.0 HD1 A:PHE31 4.0 0.0 1.0 CB A:ARG12 4.1 0.0 1.0 CG A:HIS25 4.1 0.0 1.0 HB2 A:PHE31 4.1 0.0 1.0 HB3 A:CYS29 4.1 0.0 1.0 CA A:CYS10 4.1 0.0 1.0 HD12 A:ILE20 4.2 0.0 1.0 CG2 A:ILE20 4.2 0.0 1.0 H A:ARG12 4.2 0.0 1.0 ND1 A:HIS25 4.3 0.0 1.0 C A:ARG12 4.3 0.0 1.0 HA A:CYS13 4.3 0.0 1.0 C A:CYS10 4.3 0.0 1.0 O A:CYS10 4.4 0.0 1.0 H A:PHE31 4.4 0.0 1.0 HG2 A:ARG12 4.5 0.0 1.0 N A:ARG12 4.5 0.0 1.0 CA A:ARG12 4.6 0.0 1.0 HB2 A:ARG12 4.6 0.0 1.0 H A:ARG14 4.7 0.0 1.0 HB3 A:LEU18 4.7 0.0 1.0 HG13 A:ILE20 4.7 0.0 1.0 N A:CYS29 4.7 0.0 1.0 H A:CYS10 4.7 0.0 1.0 C A:CYS29 4.7 0.0 1.0 HA A:CYS10 4.7 0.0 1.0 H A:LYS26 4.8 0.0 1.0 CG1 A:ILE20 4.8 0.0 1.0 H A:LYS30 4.8 0.0 1.0 C A:CYS13 4.8 0.0 1.0 CG A:ARG12 4.8 0.0 1.0 HA A:LYS26 4.9 0.0 1.0 N A:CYS10 5.0 0.0 1.0 CD1 A:PHE31 5.0 0.0 1.0 HG22 A:ILE20 5.0 0.0 1.0 H A:CYS29 5.0 0.0 1.0

L.Zhu, J.Wilken, N.B.Phillips, U.Narendra, G.Chan, S.M.Stratton, S.B.Kent, M.A.Weiss. Sexual Dimorphism in Diverse Metazoans Is Regulated By A Novel Class of Intertwined Zinc Fingers. Genes Dev. V. 14 1750 2000.
ISSN: ISSN 0890-9369
PubMed: 10898790
DOI: 10.1101/GAD.189500