Zinc in PDB 1faq: Raf-1 Cysteine Rich Domain, uc(Nmr), 27 Structures

The binding sites of Zinc atom in the Raf-1 Cysteine Rich Domain, uc(Nmr), 27 Structures (pdb code 1faq). 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), 27 Structures, PDB code: 1faq:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Raf-1 Cysteine Rich Domain, uc(Nmr), 27 Structures


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), 27 Structures within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1 b:0.0 occ:1.00 ND1 A:HIS173 2.0 0.0 1.0 SG A:CYS152 2.3 0.0 1.0 SG A:CYS155 2.3 0.0 1.0 SG A:CYS176 2.3 0.0 1.0 H A:HIS173 2.4 0.0 1.0 CE1 A:HIS173 2.8 0.0 1.0 HE1 A:HIS173 2.9 0.0 1.0 HB A:ILE154 3.0 0.0 1.0 CG A:HIS173 3.2 0.0 1.0 CB A:CYS152 3.3 0.0 1.0 HB2 A:CYS155 3.4 0.0 1.0 HB3 A:CYS152 3.4 0.0 1.0 N A:HIS173 3.4 0.0 1.0 HB2 A:HIS173 3.4 0.0 1.0 HB2 A:CYS152 3.5 0.0 1.0 CB A:CYS155 3.5 0.0 1.0 H A:CYS155 3.5 0.0 1.0 HB2 A:PHE172 3.5 0.0 1.0 HB2 A:HIS175 3.7 0.0 1.0 HA A:PHE172 3.7 0.0 1.0 CB A:HIS173 3.7 0.0 1.0 HG23 A:ILE154 3.8 0.0 1.0 CB A:CYS176 3.9 0.0 1.0 N A:CYS155 3.9 0.0 1.0 HB3 A:CYS176 3.9 0.0 1.0 CB A:ILE154 4.0 0.0 1.0 NE2 A:HIS173 4.1 0.0 1.0 HD12 A:LEU159 4.1 0.0 1.0 CA A:HIS173 4.1 0.0 1.0 CD2 A:HIS173 4.2 0.0 1.0 HB3 A:CYS155 4.3 0.0 1.0 CA A:CYS155 4.3 0.0 1.0 HB2 A:CYS176 4.3 0.0 1.0 CA A:PHE172 4.3 0.0 1.0 H A:ILE154 4.3 0.0 1.0 H A:HIS175 4.3 0.0 1.0 C A:PHE172 4.3 0.0 1.0 HD11 A:LEU159 4.4 0.0 1.0 CB A:PHE172 4.4 0.0 1.0 CG2 A:ILE154 4.4 0.0 1.0 HD1 A:PHE172 4.4 0.0 1.0 C A:ILE154 4.5 0.0 1.0 HA A:CYS155 4.7 0.0 1.0 CB A:HIS175 4.7 0.0 1.0 CD1 A:LEU159 4.7 0.0 1.0 CA A:CYS152 4.7 0.0 1.0 HG13 A:ILE154 4.7 0.0 1.0 CA A:ILE154 4.7 0.0 1.0 HB3 A:HIS173 4.8 0.0 1.0 C A:HIS173 4.8 0.0 1.0 HG22 A:ILE154 4.8 0.0 1.0 N A:CYS176 4.8 0.0 1.0 HB3 A:HIS175 4.9 0.0 1.0 N A:ILE154 4.9 0.0 1.0 HD13 A:LEU159 4.9 0.0 1.0 C A:HIS175 4.9 0.0 1.0 HE2 A:HIS173 4.9 0.0 1.0 H A:CYS176 4.9 0.0 1.0 HA A:CYS152 4.9 0.0 1.0 N A:HIS175 5.0 0.0 1.0 CG1 A:ILE154 5.0 0.0 1.0

Zinc binding site 2 out of 2 in the Raf-1 Cysteine Rich Domain, uc(Nmr), 27 Structures


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), 27 Structures within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn2 b:0.0 occ:1.00 ND1 A:HIS139 2.0 0.0 1.0 SG A:CYS165 2.3 0.0 1.0 SG A:CYS184 2.3 0.0 1.0 SG A:CYS168 2.3 0.0 1.0 HA A:HIS139 2.6 0.0 1.0 HE1 A:HIS139 2.7 0.0 1.0 CE1 A:HIS139 2.7 0.0 1.0 HA A:CYS184 2.9 0.0 1.0 H A:CYS168 3.1 0.0 1.0 HB3 A:CYS165 3.2 0.0 1.0 CB A:CYS165 3.2 0.0 1.0 HB3 A:CYS168 3.2 0.0 1.0 HB A:THR167 3.3 0.0 1.0 CG A:HIS139 3.3 0.0 1.0 H A:ASN140 3.3 0.0 1.0 HB2 A:CYS165 3.4 0.0 1.0 CB A:CYS184 3.4 0.0 1.0 CB A:CYS168 3.4 0.0 1.0 HB2 A:CYS184 3.5 0.0 1.0 CA A:HIS139 3.6 0.0 1.0 CA A:CYS184 3.6 0.0 1.0 O A:MET183 3.6 0.0 1.0 HB2 A:TYR170 3.7 0.0 1.0 N A:CYS168 3.7 0.0 1.0 N A:ASN140 3.9 0.0 1.0 NE2 A:HIS139 3.9 0.0 1.0 CB A:HIS139 4.0 0.0 1.0 C A:HIS139 4.1 0.0 1.0 CA A:CYS168 4.2 0.0 1.0 H A:THR167 4.2 0.0 1.0 CD2 A:HIS139 4.2 0.0 1.0 HB2 A:CYS168 4.2 0.0 1.0 O A:THR138 4.3 0.0 1.0 CB A:THR167 4.3 0.0 1.0 HB3 A:CYS184 4.3 0.0 1.0 H A:GLY169 4.5 0.0 1.0 HB2 A:ASN140 4.5 0.0 1.0 C A:MET183 4.5 0.0 1.0 HB2 A:HIS139 4.6 0.0 1.0 N A:CYS184 4.6 0.0 1.0 H A:TYR170 4.6 0.0 1.0 CA A:CYS165 4.6 0.0 1.0 C A:THR167 4.7 0.0 1.0 C A:CYS184 4.7 0.0 1.0 CB A:TYR170 4.7 0.0 1.0 HE2 A:HIS139 4.7 0.0 1.0 N A:HIS139 4.8 0.0 1.0 HD1 A:TYR170 4.8 0.0 1.0 HG23 A:THR167 4.8 0.0 1.0 HB3 A:HIS139 4.9 0.0 1.0 N A:THR167 4.9 0.0 1.0 CA A:THR167 4.9 0.0 1.0 HB3 A:TYR170 4.9 0.0 1.0 O A:CYS184 4.9 0.0 1.0 C A:THR138 5.0 0.0 1.0 OG1 A:THR167 5.0 0.0 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