Zinc in PDB 1cxx: Mutant R122A of Quail Cysteine and Glycine-Rich Protein, uc(Nmr), Minimized Structure

The binding sites of Zinc atom in the Mutant R122A of Quail Cysteine and Glycine-Rich Protein, uc(Nmr), Minimized Structure (pdb code 1cxx). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Mutant R122A of Quail Cysteine and Glycine-Rich Protein, uc(Nmr), Minimized Structure, PDB code: 1cxx:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Mutant R122A of Quail Cysteine and Glycine-Rich Protein, uc(Nmr), Minimized Structure


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Mutant R122A of Quail Cysteine and Glycine-Rich Protein, uc(Nmr), Minimized Structure within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1 b:0.0 occ:1.00 ND1 A:HIS141 2.0 0.0 1.0 SG A:CYS120 2.3 0.0 1.0 SG A:CYS144 2.3 0.0 1.0 SG A:CYS123 2.3 0.0 1.0 HB3 A:CYS120 2.9 0.0 1.0 CE1 A:HIS141 3.0 0.0 1.0 H A:CYS123 3.0 0.0 1.0 HB2 A:HIS141 3.0 0.0 1.0 CG A:HIS141 3.1 0.0 1.0 CB A:CYS120 3.1 0.0 1.0 HB3 A:CYS123 3.2 0.0 1.0 HE1 A:HIS141 3.2 0.0 1.0 HB2 A:CYS144 3.2 0.0 1.0 CB A:CYS144 3.3 0.0 1.0 H A:HIS141 3.3 0.0 1.0 CB A:CYS123 3.3 0.0 1.0 HB2 A:CYS120 3.4 0.0 1.0 HB3 A:CYS144 3.5 0.0 1.0 HB1 A:ALA122 3.5 0.0 1.0 CB A:HIS141 3.5 0.0 1.0 N A:CYS123 3.8 0.0 1.0 N A:HIS141 4.1 0.0 1.0 HB2 A:ASP125 4.1 0.0 1.0 NE2 A:HIS141 4.2 0.0 1.0 HB2 A:CYS123 4.2 0.0 1.0 CA A:CYS123 4.2 0.0 1.0 CD2 A:HIS141 4.2 0.0 1.0 H A:ASP125 4.2 0.0 1.0 H A:ALA122 4.3 0.0 1.0 HB3 A:HIS141 4.3 0.0 1.0 CA A:HIS141 4.5 0.0 1.0 CA A:CYS120 4.5 0.0 1.0 H A:GLY124 4.5 0.0 1.0 CB A:ALA122 4.5 0.0 1.0 HA A:TRP140 4.7 0.0 1.0 H A:CYS144 4.7 0.0 1.0 CA A:CYS144 4.7 0.0 1.0 O A:ASP125 4.8 0.0 1.0 O A:CYS120 4.8 0.0 1.0 C A:CYS120 4.9 0.0 1.0 C A:ALA122 4.9 0.0 1.0 HG12 A:VAL127 4.9 0.0 1.0

Zinc binding site 2 out of 2 in the Mutant R122A of Quail Cysteine and Glycine-Rich Protein, uc(Nmr), Minimized Structure


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Mutant R122A of Quail Cysteine and Glycine-Rich Protein, uc(Nmr), Minimized Structure within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn2 b:0.0 occ:1.00 SG A:CYS171 2.3 0.0 1.0 SG A:CYS147 2.3 0.0 1.0 SG A:CYS168 2.3 0.0 1.0 SG A:CYS150 2.3 0.0 1.0 H A:CYS150 2.7 0.0 1.0 HB2 A:CYS171 3.1 0.0 1.0 HB2 A:LYS149 3.2 0.0 1.0 H A:CYS168 3.2 0.0 1.0 CB A:CYS147 3.3 0.0 1.0 HB2 A:CYS147 3.3 0.0 1.0 CB A:CYS171 3.3 0.0 1.0 HB3 A:CYS150 3.3 0.0 1.0 HB3 A:CYS147 3.4 0.0 1.0 HB3 A:CYS168 3.4 0.0 1.0 CB A:CYS150 3.4 0.0 1.0 CB A:CYS168 3.4 0.0 1.0 H A:GLY151 3.4 0.0 1.0 HG2 A:LYS152 3.6 0.0 1.0 N A:CYS150 3.6 0.0 1.0 HE3 A:LYS152 3.6 0.0 1.0 H A:CYS171 3.8 0.0 1.0 N A:CYS168 4.0 0.0 1.0 H A:LYS149 4.0 0.0 1.0 CA A:CYS150 4.1 0.0 1.0 HB3 A:CYS171 4.1 0.0 1.0 CA A:CYS171 4.2 0.0 1.0 CA A:CYS168 4.2 0.0 1.0 CB A:LYS149 4.2 0.0 1.0 H A:LYS152 4.2 0.0 1.0 HZ1 A:LYS174 4.2 0.0 1.0 HA A:CYS171 4.3 0.0 1.0 N A:CYS171 4.3 0.0 1.0 HB2 A:CYS150 4.3 0.0 1.0 HB2 A:CYS168 4.3 0.0 1.0 N A:GLY151 4.3 0.0 1.0 O A:CYS168 4.3 0.0 1.0 HB3 A:LYS149 4.5 0.0 1.0 HB3 A:TYR167 4.5 0.0 1.0 CG A:LYS152 4.6 0.0 1.0 CE A:LYS152 4.6 0.0 1.0 C A:CYS168 4.7 0.0 1.0 C A:LYS149 4.7 0.0 1.0 CA A:CYS147 4.7 0.0 1.0 N A:LYS149 4.8 0.0 1.0 C A:CYS150 4.8 0.0 1.0 HG3 A:LYS149 4.8 0.0 1.0 CA A:LYS149 4.8 0.0 1.0 HA A:TYR167 4.8 0.0 1.0 HZ3 A:LYS152 4.9 0.0 1.0 HG3 A:LYS152 4.9 0.0 1.0 H A:ALA148 5.0 0.0 1.0 HA A:CYS150 5.0 0.0 1.0 HA A:CYS147 5.0 0.0 1.0

K.Kloiber, R.Weiskirchen, B.Krautler, K.Bister, R.Konrat. Mutational Analysis and uc(Nmr) Spectroscopy of Quail Cysteine and Glycine-Rich Protein CRP2 Reveal An Intrinsic Segmental Flexibility of Lim Domains. J.Mol.Biol. V. 292 893 1999.
ISSN: ISSN 0022-2836
PubMed: 10525413
DOI: 10.1006/JMBI.1999.3118