Zinc in PDB 2w0t: Solution Structure of the Fcs Zinc Finger Domain of Human LMBL2

The binding sites of Zinc atom in the Solution Structure of the Fcs Zinc Finger Domain of Human LMBL2 (pdb code 2w0t). 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 Structure of the Fcs Zinc Finger Domain of Human LMBL2, PDB code: 2w0t:

Zinc binding site 1 out of 1 in the Solution Structure of the Fcs Zinc Finger Domain of Human LMBL2


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Solution Structure of the Fcs Zinc Finger Domain of Human LMBL2 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn125 b:0.0 occ:1.00 SG A:CYS93 2.3 0.0 1.0 SG A:CYS90 2.4 0.0 1.0 SG A:CYS110 2.4 0.0 1.0 SG A:CYS114 2.4 0.0 1.0 H A:CYS93 3.0 0.0 1.0 HB3 A:MET92 3.1 0.0 1.0 H A:CYS110 3.2 0.0 1.0 HB2 A:CYS93 3.2 0.0 1.0 CB A:CYS93 3.4 0.0 1.0 HD11 A:ILE95 3.6 0.0 1.0 CB A:CYS114 3.6 0.0 1.0 HB3 A:CYS114 3.7 0.0 1.0 CB A:CYS90 3.7 0.0 1.0 N A:CYS93 3.8 0.0 1.0 HB2 A:CYS114 3.8 0.0 1.0 CB A:CYS110 3.9 0.0 1.0 HB3 A:CYS90 3.9 0.0 1.0 HB2 A:CYS90 3.9 0.0 1.0 N A:CYS110 3.9 0.0 1.0 HB3 A:PHE109 4.0 0.0 1.0 HB3 A:CYS110 4.0 0.0 1.0 H A:SER111 4.1 0.0 1.0 CB A:MET92 4.2 0.0 1.0 CA A:CYS93 4.2 0.0 1.0 HB3 A:CYS93 4.2 0.0 1.0 CA A:CYS110 4.4 0.0 1.0 H A:MET92 4.4 0.0 1.0 HB2 A:MET92 4.4 0.0 1.0 CD1 A:ILE95 4.5 0.0 1.0 HA A:PHE109 4.5 0.0 1.0 HD13 A:ILE95 4.5 0.0 1.0 N A:SER111 4.6 0.0 1.0 H A:GLY94 4.6 0.0 1.0 HB2 A:CYS110 4.7 0.0 1.0 HD1 A:PHE109 4.7 0.0 1.0 HB3 A:SER111 4.7 0.0 1.0 C A:MET92 4.7 0.0 1.0 SD A:MET92 4.8 0.0 1.0 OG A:SER111 4.8 0.0 1.0 C A:CYS110 4.8 0.0 1.0 HD12 A:ILE95 4.9 0.0 1.0 CA A:MET92 4.9 0.0 1.0 C A:PHE109 4.9 0.0 1.0 HA A:CYS93 4.9 0.0 1.0 CB A:PHE109 5.0 0.0 1.0 HB A:ILE95 5.0 0.0 1.0 CA A:CYS114 5.0 0.0 1.0

B.C.Lechtenberg, M.D.Allen, T.J.Rutherford, S.M.Freund, M.Bycroft. Solution Structure of the Fcs Zinc Finger Domain of the Human Polycomb Group Protein L(3)Mbt-Like 2. Protein Sci. V. 18 657 2009.
ISSN: ISSN 0961-8368
PubMed: 19241375
DOI: 10.1002/PRO.51