Zinc in PDB 2fej: Solution Structure of Human P53 Dna Binding Domain.

The binding sites of Zinc atom in the Solution Structure of Human P53 Dna Binding Domain. (pdb code 2fej). 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 Human P53 Dna Binding Domain., PDB code: 2fej:

Zinc binding site 1 out of 1 in the Solution Structure of Human P53 Dna Binding Domain.


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 Human P53 Dna Binding Domain. within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1 b:0.0 occ:1.00 HG A:CYS242 1.7 0.0 1.0 HD1 A:HIS179 1.7 0.0 1.0 HG A:CYS238 1.9 0.0 1.0 ND1 A:HIS179 2.3 0.0 1.0 SG A:CYS176 2.4 0.0 1.0 SG A:CYS242 2.4 0.0 1.0 SG A:CYS238 2.4 0.0 1.0 HE1 A:HIS179 2.5 0.0 1.0 CE1 A:HIS179 2.7 0.0 1.0 HE2 A:HIS178 2.9 0.0 1.0 HB2 A:CYS176 3.1 0.0 1.0 CB A:CYS176 3.4 0.0 1.0 HB3 A:CYS242 3.4 0.0 1.0 H A:CYS176 3.5 0.0 1.0 CB A:CYS242 3.5 0.0 1.0 HA3 A:GLY245 3.5 0.0 1.0 CG A:HIS179 3.6 0.0 1.0 HB2 A:CYS242 3.8 0.0 1.0 NE2 A:HIS178 3.8 0.0 1.0 HB2 A:HIS179 3.9 0.0 1.0 NE2 A:HIS179 4.0 0.0 1.0 HA A:CYS238 4.1 0.0 1.0 HB3 A:CYS176 4.1 0.0 1.0 CB A:CYS238 4.1 0.0 1.0 N A:CYS176 4.3 0.0 1.0 CB A:HIS179 4.4 0.0 1.0 CD2 A:HIS179 4.4 0.0 1.0 CA A:GLY245 4.4 0.0 1.0 CA A:CYS176 4.5 0.0 1.0 HB2 A:CYS238 4.5 0.0 1.0 HD2 A:HIS178 4.5 0.0 1.0 CD2 A:HIS178 4.6 0.0 1.0 N A:GLY245 4.6 0.0 1.0 CA A:CYS238 4.7 0.0 1.0 HA2 A:GLY245 4.7 0.0 1.0 HE2 A:HIS179 4.7 0.0 1.0 CE1 A:HIS178 4.8 0.0 1.0 HB3 A:CYS238 4.8 0.0 1.0 HB3 A:HIS179 4.8 0.0 1.0 CA A:CYS242 4.9 0.0 1.0 HA A:ARG175 4.9 0.0 1.0 HE1 A:HIS178 4.9 0.0 1.0 O A:MET237 4.9 0.0 1.0 C A:GLY244 4.9 0.0 1.0 H A:GLY245 5.0 0.0 1.0 O A:GLY244 5.0 0.0 1.0

J.M.Perez-Canadillas, H.Tidow, S.M.Freund, T.J.Rutherford, H.C.Ang, A.R.Fersht. Solution Structure of P53 Core Domain: Structural Basis For Its Instability Proc.Natl.Acad.Sci.Usa V. 103 2109 2006.
ISSN: ISSN 0027-8424
PubMed: 16461916
DOI: 10.1073/PNAS.0510941103