Zinc in PDB 1far: Raf-1 Cysteine Rich Domain, uc(Nmr), Minimized Average Structure

The binding sites of Zinc atom in the Raf-1 Cysteine Rich Domain, uc(Nmr), Minimized Average Structure (pdb code 1far). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Raf-1 Cysteine Rich Domain, uc(Nmr), Minimized Average Structure, PDB code: 1far:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Raf-1 Cysteine Rich Domain, uc(Nmr), Minimized Average Structure


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Raf-1 Cysteine Rich Domain, uc(Nmr), Minimized Average Structure within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1 b:0.4 occ:1.00 ND1 A:HIS173 2.1 0.4 1.0 SG A:CYS152 2.4 0.3 1.0 H A:HIS173 2.4 0.4 1.0 SG A:CYS155 2.4 0.4 1.0 SG A:CYS176 2.5 0.7 1.0 CE1 A:HIS173 2.9 0.4 1.0 HB2 A:HIS175 3.0 0.6 1.0 HB A:ILE154 3.0 0.4 1.0 HE1 A:HIS173 3.1 0.4 1.0 CG A:HIS173 3.2 0.4 1.0 HB2 A:PHE172 3.2 1.0 1.0 N A:HIS173 3.3 0.3 1.0 HB2 A:HIS173 3.5 0.4 1.0 H A:CYS155 3.6 0.4 1.0 CB A:CYS152 3.7 0.3 1.0 CB A:HIS173 3.7 0.4 1.0 HG23 A:ILE154 3.8 1.1 1.0 CB A:CYS155 3.8 0.4 1.0 HB2 A:CYS155 3.8 0.3 1.0 HB3 A:CYS152 3.8 0.3 1.0 HB2 A:CYS152 3.9 0.4 1.0 NE2 A:HIS173 4.0 0.4 1.0 CB A:HIS175 4.0 0.7 1.0 CB A:ILE154 4.0 0.5 1.0 CA A:HIS173 4.0 0.4 1.0 H A:HIS175 4.0 0.6 1.0 HA A:PHE172 4.0 0.6 1.0 N A:CYS155 4.1 0.4 1.0 CD2 A:HIS173 4.1 0.4 1.0 CB A:PHE172 4.1 0.7 1.0 CB A:CYS176 4.3 0.5 1.0 HB3 A:PHE172 4.3 1.1 1.0 HB3 A:HIS175 4.3 0.7 1.0 C A:PHE172 4.3 0.4 1.0 CG2 A:ILE154 4.3 0.5 1.0 H A:CYS176 4.4 0.6 1.0 CA A:PHE172 4.4 0.4 1.0 C A:HIS173 4.5 0.5 1.0 HG13 A:ILE154 4.5 0.6 1.0 CA A:CYS155 4.5 0.4 1.0 HB2 A:CYS176 4.6 0.6 1.0 HB3 A:CYS155 4.6 0.4 1.0 N A:CYS176 4.6 0.5 1.0 HG22 A:ILE154 4.6 1.2 1.0 H A:ILE154 4.6 0.4 1.0 N A:HIS175 4.6 0.6 1.0 O A:HIS173 4.7 0.6 1.0 C A:ILE154 4.7 0.5 1.0 CA A:HIS175 4.7 0.6 1.0 HB3 A:HIS173 4.7 0.5 1.0 HA A:CYS155 4.8 0.5 1.0 C A:HIS175 4.8 0.6 1.0 HB3 A:CYS176 4.8 0.7 1.0 HE2 A:HIS173 4.8 0.4 1.0 HD23 A:LEU159 4.8 1.8 1.0 CG1 A:ILE154 4.9 0.5 1.0 CA A:ILE154 4.9 0.5 1.0 CG A:HIS175 4.9 0.8 1.0 CA A:CYS152 5.0 0.3 1.0 HA A:HIS173 5.0 0.4 1.0

Zinc binding site 2 out of 2 in the Raf-1 Cysteine Rich Domain, uc(Nmr), Minimized Average Structure


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Raf-1 Cysteine Rich Domain, uc(Nmr), Minimized Average Structure within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn2 b:0.8 occ:1.00 ND1 A:HIS139 2.2 1.1 1.0 HE1 A:HIS139 2.2 1.6 1.0 HB2 A:CYS165 2.3 1.1 1.0 SG A:CYS184 2.4 2.4 1.0 SG A:CYS165 2.4 1.2 1.0 CE1 A:HIS139 2.4 1.4 1.0 SG A:CYS168 2.5 0.7 1.0 CB A:CYS165 2.5 0.5 1.0 HB3 A:CYS165 2.5 0.8 1.0 HB2 A:TYR170 2.7 0.6 1.0 CB A:CYS184 3.0 2.9 1.0 HA A:HIS139 3.1 1.3 1.0 HB2 A:CYS184 3.1 3.3 1.0 HB3 A:CYS184 3.1 3.4 1.0 H A:ASN140 3.2 0.9 1.0 CG A:HIS139 3.5 1.1 1.0 CB A:TYR170 3.7 0.6 1.0 NE2 A:HIS139 3.7 1.6 1.0 HB3 A:TYR170 3.9 0.7 1.0 H A:CYS168 4.0 0.6 1.0 CA A:CYS165 4.0 0.4 1.0 CA A:HIS139 4.0 1.1 1.0 CB A:CYS168 4.0 0.7 1.0 N A:ASN140 4.1 0.8 1.0 H A:TYR170 4.1 0.6 1.0 HD1 A:TYR170 4.1 2.2 1.0 HB3 A:CYS168 4.1 0.8 1.0 CD2 A:TYR170 4.2 1.5 1.0 CG A:TYR170 4.2 0.7 1.0 CD2 A:HIS139 4.2 1.4 1.0 HD2 A:TYR170 4.3 2.3 1.0 HE2 A:HIS139 4.4 2.0 1.0 CB A:HIS139 4.4 1.1 1.0 HA A:CYS165 4.4 0.4 1.0 CA A:CYS184 4.5 2.9 1.0 CD1 A:TYR170 4.5 1.4 1.0 H A:GLY169 4.6 0.6 1.0 H A:CYS165 4.6 0.5 1.0 C A:HIS139 4.6 1.0 1.0 HE1 A:TYR170 4.7 2.3 1.0 HB2 A:CYS168 4.7 1.0 1.0 N A:CYS168 4.7 0.6 1.0 H A:THR167 4.7 0.6 1.0 N A:TYR170 4.7 0.5 1.0 O A:ASN140 4.8 1.0 1.0 HA A:CYS184 4.8 2.9 1.0 HB2 A:ASN140 4.8 0.8 1.0 N A:CYS165 4.8 0.4 1.0 C A:CYS165 4.8 0.5 1.0 CA A:TYR170 4.9 0.5 1.0 CE1 A:TYR170 4.9 1.5 1.0 CA A:CYS168 5.0 0.7 1.0

H.R.Mott, J.W.Carpenter, S.Zhong, S.Ghosh, R.M.Bell, S.L.Campbell. The Solution Structure of the Raf-1 Cysteine-Rich Domain: A Novel Ras and Phospholipid Binding Site. Proc.Natl.Acad.Sci.Usa V. 93 8312 1996.
ISSN: ISSN 0027-8424
PubMed: 8710867
DOI: 10.1073/PNAS.93.16.8312