Zinc in PDB 1p4q: Solution Structure of the CITED2 Transactivation Domain in Complex with the P300 CH1 Domain

All present enzymatic activity of Solution Structure of the CITED2 Transactivation Domain in Complex with the P300 CH1 Domain:
2.3.1.48;

The binding sites of Zinc atom in the Solution Structure of the CITED2 Transactivation Domain in Complex with the P300 CH1 Domain (pdb code 1p4q). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 3 binding sites of Zinc where determined in the Solution Structure of the CITED2 Transactivation Domain in Complex with the P300 CH1 Domain, PDB code: 1p4q:
Jump to Zinc binding site number: 1; 2; 3;

Zinc binding site 1 out of 3 in the Solution Structure of the CITED2 Transactivation Domain in Complex with the P300 CH1 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 the CITED2 Transactivation Domain in Complex with the P300 CH1 Domain within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn301 b:0.0 occ:1.00 NE2 B:HIS125 2.0 0.0 1.0 SG B:CYS142 2.3 0.0 1.0 SG B:CYS147 2.3 0.0 1.0 SG B:CYS129 2.4 0.0 1.0 HB3 B:CYS147 2.8 0.0 1.0 CB B:CYS147 3.0 0.0 1.0 HB3 B:CYS142 3.0 0.0 1.0 CE1 B:HIS125 3.0 0.0 1.0 HB2 B:CYS147 3.1 0.0 1.0 CD2 B:HIS125 3.1 0.0 1.0 HE1 B:HIS125 3.2 0.0 1.0 CB B:CYS142 3.3 0.0 1.0 HE3 B:LYS151 3.3 0.0 1.0 HD2 B:HIS125 3.3 0.0 1.0 HB2 B:CYS129 3.6 0.0 1.0 CB B:CYS129 3.6 0.0 1.0 HB2 B:CYS142 3.7 0.0 1.0 HG B:LEU144 3.8 0.0 1.0 HE2 B:LYS151 3.8 0.0 1.0 HB3 B:CYS129 3.8 0.0 1.0 O B:LEU144 4.1 0.0 1.0 CE B:LYS151 4.1 0.0 1.0 ND1 B:HIS125 4.2 0.0 1.0 CG B:HIS125 4.2 0.0 1.0 HD13 B:LEU144 4.2 0.0 1.0 HA B:ALA126 4.3 0.0 1.0 CA B:CYS147 4.5 0.0 1.0 HD21 B:LEU144 4.5 0.0 1.0 H B:CYS147 4.5 0.0 1.0 CA B:CYS142 4.6 0.0 1.0 HA B:CYS142 4.7 0.0 1.0 CG B:LEU144 4.7 0.0 1.0 HZ3 B:LYS151 4.8 0.0 1.0 HD2 B:LYS151 4.8 0.0 1.0 HE2 A:MET22 4.9 0.0 1.0 H B:LEU144 4.9 0.0 1.0 H B:ASN143 4.9 0.0 1.0 CA B:CYS129 4.9 0.0 1.0 CD1 B:LEU144 5.0 0.0 1.0 N B:CYS147 5.0 0.0 1.0

Zinc binding site 2 out of 3 in the Solution Structure of the CITED2 Transactivation Domain in Complex with the P300 CH1 Domain


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Solution Structure of the CITED2 Transactivation Domain in Complex with the P300 CH1 Domain within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn302 b:0.0 occ:1.00 NE2 B:HIS156 2.0 0.0 1.0 HE1 B:HIS156 2.2 0.0 1.0 CE1 B:HIS156 2.2 0.0 1.0 HB2 B:CYS160 2.2 0.0 1.0 SG B:CYS160 2.3 0.0 1.0 SG B:CYS166 2.3 0.0 1.0 SG B:CYS171 2.4 0.0 1.0 CB B:CYS160 2.6 0.0 1.0 HA B:CYS160 2.8 0.0 1.0 HB B:VAL168 3.2 0.0 1.0 CD2 B:HIS156 3.2 0.0 1.0 CA B:CYS160 3.2 0.0 1.0 ND1 B:HIS156 3.3 0.0 1.0 CB B:CYS166 3.4 0.0 1.0 HB2 B:CYS166 3.4 0.0 1.0 HB3 B:CYS166 3.4 0.0 1.0 HB2 B:CYS171 3.5 0.0 1.0 CB B:CYS171 3.6 0.0 1.0 HB3 B:CYS160 3.6 0.0 1.0 CG B:HIS156 3.8 0.0 1.0 HG21 B:VAL168 3.8 0.0 1.0 HD2 B:HIS156 3.8 0.0 1.0 HB3 B:CYS171 3.9 0.0 1.0 HD1 B:HIS156 4.0 0.0 1.0 N B:CYS160 4.1 0.0 1.0 CB B:VAL168 4.2 0.0 1.0 HA B:MET157 4.2 0.0 1.0 H B:VAL168 4.2 0.0 1.0 O B:HIS156 4.2 0.0 1.0 C B:CYS160 4.4 0.0 1.0 H B:CYS160 4.4 0.0 1.0 CG2 B:VAL168 4.5 0.0 1.0 H B:GLY163 4.5 0.0 1.0 H B:GLN161 4.6 0.0 1.0 HG11 B:VAL168 4.7 0.0 1.0 H B:SER162 4.7 0.0 1.0 HG12 B:VAL168 4.7 0.0 1.0 CG1 B:VAL168 4.8 0.0 1.0 C B:HIS156 4.8 0.0 1.0 CA B:CYS166 4.8 0.0 1.0 C B:HIS159 4.9 0.0 1.0 HG22 B:VAL168 4.9 0.0 1.0 HA2 B:GLY163 4.9 0.0 1.0 CA B:CYS171 4.9 0.0 1.0 N B:GLN161 4.9 0.0 1.0 HA B:CYS171 5.0 0.0 1.0

Zinc binding site 3 out of 3 in the Solution Structure of the CITED2 Transactivation Domain in Complex with the P300 CH1 Domain


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Solution Structure of the CITED2 Transactivation Domain in Complex with the P300 CH1 Domain within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn303 b:0.0 occ:1.00 NE2 B:HIS180 2.1 0.0 1.0 SG B:CYS184 2.4 0.0 1.0 SG B:CYS192 2.4 0.0 1.0 SG B:CYS189 2.4 0.0 1.0 HB B:VAL191 2.5 0.0 1.0 HB3 B:CYS184 2.6 0.0 1.0 H B:CYS192 2.8 0.0 1.0 CE1 B:HIS180 2.8 0.0 1.0 CB B:CYS184 2.8 0.0 1.0 CD2 B:HIS180 2.9 0.0 1.0 HB2 B:CYS184 3.0 0.0 1.0 HE1 B:HIS180 3.1 0.0 1.0 HG22 B:VAL191 3.2 0.0 1.0 HG21 B:VAL191 3.2 0.0 1.0 HA B:TRP181 3.3 0.0 1.0 HD2 B:HIS180 3.3 0.0 1.0 CB B:VAL191 3.4 0.0 1.0 CG2 B:VAL191 3.4 0.0 1.0 N B:CYS192 3.7 0.0 1.0 ND1 B:HIS180 3.7 0.0 1.0 CG B:HIS180 3.8 0.0 1.0 CB B:CYS192 3.9 0.0 1.0 H B:VAL191 4.0 0.0 1.0 HG12 B:VAL191 4.1 0.0 1.0 CB B:CYS189 4.1 0.0 1.0 HB2 B:CYS192 4.2 0.0 1.0 CA B:TRP181 4.3 0.0 1.0 O B:HIS180 4.3 0.0 1.0 CA B:CYS184 4.3 0.0 1.0 HD1 B:TRP181 4.3 0.0 1.0 CG1 B:VAL191 4.3 0.0 1.0 CA B:VAL191 4.4 0.0 1.0 CA B:CYS192 4.4 0.0 1.0 HB2 B:CYS189 4.4 0.0 1.0 CD1 B:TRP181 4.4 0.0 1.0 C B:VAL191 4.5 0.0 1.0 HG23 B:VAL191 4.5 0.0 1.0 C B:HIS180 4.5 0.0 1.0 N B:TRP181 4.6 0.0 1.0 HD1 B:HIS180 4.6 0.0 1.0 HB3 B:CYS189 4.6 0.0 1.0 N B:VAL191 4.6 0.0 1.0 HB3 B:CYS192 4.7 0.0 1.0 H B:LEU193 4.8 0.0 1.0 C B:CYS184 4.8 0.0 1.0 CG B:TRP181 4.8 0.0 1.0 HA B:CYS184 4.8 0.0 1.0 NE1 B:TRP181 4.9 0.0 1.0 HG13 B:VAL191 4.9 0.0 1.0 H B:CYS184 4.9 0.0 1.0

S.J.Freedman, Z.Y.Sun, A.L.Kung, D.S.France, G.Wagner, M.J.Eck. Structural Basis For Negative Regulation of Hypoxia-Inducible Factor-1ALPHA By CITED2. Nat.Struct.Biol. V. 10 504 2003.
ISSN: ISSN 1072-8368
PubMed: 12778114
DOI: 10.1038/NSB936