Zinc in PDB 2alc: Ethanol Regulon Transcriptional Activator Dna-Binding Domain From Aspergillus Nidulans

The binding sites of Zinc atom in the Ethanol Regulon Transcriptional Activator Dna-Binding Domain From Aspergillus Nidulans (pdb code 2alc). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Ethanol Regulon Transcriptional Activator Dna-Binding Domain From Aspergillus Nidulans, PDB code: 2alc:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Ethanol Regulon Transcriptional Activator Dna-Binding Domain From Aspergillus Nidulans


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Ethanol Regulon Transcriptional Activator Dna-Binding Domain From Aspergillus Nidulans within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn64 b:0.6 occ:1.00 SG A:CYS15 2.3 0.2 1.0 SG A:CYS22 2.3 0.2 1.0 SG A:CYS39 2.4 0.1 1.0 SG A:CYS12 2.4 0.1 1.0 HD21 A:ASN41 2.9 0.1 1.0 HB2 A:CYS15 2.9 0.1 1.0 H A:CYS12 3.0 0.1 1.0 HB2 A:ASN41 3.0 0.1 1.0 HB3 A:CYS22 3.0 0.2 1.0 ZN A:ZN65 3.1 1.0 1.0 CB A:CYS15 3.2 0.2 1.0 CB A:CYS22 3.2 0.1 1.0 CB A:CYS39 3.3 0.1 1.0 HB3 A:CYS39 3.3 0.1 1.0 HB2 A:CYS39 3.4 0.1 1.0 HB3 A:CYS12 3.5 0.1 1.0 CB A:CYS12 3.6 0.1 1.0 H A:CYS15 3.6 0.1 1.0 HB2 A:CYS22 3.6 0.2 1.0 HG2 A:PRO14 3.6 0.1 1.0 N A:CYS12 3.6 0.1 1.0 ND2 A:ASN41 3.8 0.1 1.0 HB3 A:CYS15 3.8 0.2 1.0 HB3 A:SER11 4.0 0.6 1.0 CB A:ASN41 4.0 0.1 1.0 CA A:CYS12 4.1 0.1 1.0 H A:CYS42 4.1 0.1 1.0 N A:CYS15 4.2 0.2 1.0 HA A:SER11 4.3 0.2 1.0 O A:CYS12 4.3 0.2 1.0 CA A:CYS15 4.3 0.2 1.0 H A:ASN41 4.4 0.2 1.0 HB2 A:ALA24 4.4 1.0 1.0 HB3 A:ASN41 4.4 0.2 1.0 CG A:ASN41 4.4 0.2 1.0 HD22 A:ASN41 4.4 0.1 1.0 HB2 A:CYS12 4.5 0.1 1.0 C A:CYS12 4.5 0.2 1.0 C A:SER11 4.6 0.2 1.0 HB3 A:ALA24 4.6 1.0 1.0 HD2 A:PRO14 4.6 0.1 1.0 CA A:CYS22 4.6 0.1 1.0 H A:CYS22 4.7 0.1 1.0 CG A:PRO14 4.7 0.2 1.0 CB A:SER11 4.7 0.2 1.0 HB2 A:SER11 4.7 0.8 1.0 CA A:CYS39 4.7 0.2 1.0 CA A:SER11 4.7 0.2 1.0 H A:CYS39 4.7 0.2 1.0 SG A:CYS42 4.8 0.2 1.0 N A:CYS22 4.8 0.1 1.0 HA A:CYS15 4.9 0.2 1.0 H A:ARG16 4.9 0.2 1.0 SG A:CYS49 4.9 0.2 1.0 N A:CYS42 5.0 0.1 1.0 CB A:ALA24 5.0 0.2 1.0

Zinc binding site 2 out of 2 in the Ethanol Regulon Transcriptional Activator Dna-Binding Domain From Aspergillus Nidulans


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Ethanol Regulon Transcriptional Activator Dna-Binding Domain From Aspergillus Nidulans within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn65 b:1.0 occ:1.00 SG A:CYS42 2.3 0.2 1.0 SG A:CYS49 2.3 0.2 1.0 SG A:CYS12 2.4 0.1 1.0 SG A:CYS39 2.4 0.1 1.0 HA A:CYS49 2.6 0.2 1.0 H A:CYS39 2.9 0.2 1.0 HB2 A:CYS42 3.0 0.2 1.0 ZN A:ZN64 3.1 0.6 1.0 HB3 A:CYS12 3.3 0.1 1.0 CB A:CYS49 3.3 0.2 1.0 CB A:CYS42 3.3 0.2 1.0 CB A:CYS12 3.3 0.1 1.0 H A:CYS42 3.3 0.1 1.0 CA A:CYS49 3.4 0.2 1.0 HG2 A:PRO14 3.4 0.1 1.0 HB3 A:CYS39 3.4 0.1 1.0 HB2 A:CYS49 3.4 0.2 1.0 CB A:CYS39 3.5 0.1 1.0 HB2 A:CYS12 3.5 0.1 1.0 N A:CYS39 3.7 0.2 1.0 HG3 A:PRO14 3.9 0.2 1.0 N A:CYS49 4.0 0.2 1.0 HB3 A:CYS42 4.0 0.2 1.0 N A:CYS42 4.0 0.1 1.0 CG A:PRO14 4.0 0.2 1.0 HD2 A:PRO14 4.1 0.1 1.0 CA A:CYS39 4.1 0.2 1.0 HB2 A:ASN41 4.1 0.1 1.0 HB2 A:SER38 4.2 0.7 1.0 CA A:CYS42 4.2 0.1 1.0 HB3 A:CYS49 4.3 0.2 1.0 HB2 A:CYS39 4.4 0.1 1.0 HH2 A:TRP36 4.4 0.3 1.0 HA A:SER38 4.4 0.3 1.0 H A:CYS49 4.4 0.2 1.0 H A:THR50 4.5 0.2 1.0 O A:CYS39 4.5 0.2 1.0 HB3 A:ALA24 4.5 1.0 1.0 H A:CYS12 4.6 0.1 1.0 C A:ASP48 4.6 0.2 1.0 HA A:CYS42 4.6 0.2 1.0 CD A:PRO14 4.6 0.2 1.0 C A:CYS49 4.6 0.2 1.0 O A:ASP48 4.7 0.3 1.0 C A:CYS39 4.7 0.2 1.0 CA A:CYS12 4.7 0.1 1.0 HZ2 A:TRP36 4.7 0.3 1.0 C A:SER38 4.7 0.3 1.0 SG A:CYS15 4.7 0.2 1.0 CB A:SER38 4.8 0.2 1.0 CA A:SER38 4.9 0.3 1.0 HB3 A:SER38 4.9 0.6 1.0 HB2 A:LYS47 4.9 0.2 1.0 N A:THR50 5.0 0.2 1.0 SG A:CYS22 5.0 0.2 1.0

R.Cerdan, B.Cahuzac, B.Felenbok, E.Guittet. uc(Nmr) Solution Structure of Alcr (1-60) Provides Insight in the Unusual Dna Binding Properties of This Zinc Binuclear Cluster Protein. J.Mol.Biol. V. 295 729 2000.
ISSN: ISSN 0022-2836
PubMed: 10656785
DOI: 10.1006/JMBI.1999.3417