3R2Q
Crystal Structure Analysis of yibF from E. Coli
Functional Information from GO Data
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE GSH A 301 |
| Chain | Residue |
| A | SER9 |
| A | PRO64 |
| A | LEU105 |
| A | ARG125 |
| A | LYS129 |
| A | HOH1009 |
| A | HOH1010 |
| A | HOH1028 |
| A | HOH1030 |
| A | HOH1051 |
| A | HOH1096 |
| A | PHE11 |
| A | HOH1099 |
| A | HOH1116 |
| A | HOH1234 |
| A | PRO33 |
| A | TYR34 |
| A | LYS48 |
| A | VAL49 |
| A | PRO50 |
| A | ASP62 |
| A | SER63 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE PO4 A 305 |
| Chain | Residue |
| A | ARG127 |
| A | ASN131 |
| A | ALA171 |
| A | PRO172 |
| A | GLY173 |
| A | HOH1136 |
| A | HOH1147 |
| A | HOH1253 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO A 309 |
| Chain | Residue |
| A | ARG13 |
| A | PHE189 |
| A | GLU198 |
| A | HOH1069 |
| A | HOH1077 |
| A | HOH1130 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO A 310 |
| Chain | Residue |
| A | PHE167 |
| A | ARG168 |
| A | ARG169 |
| A | HOH1057 |
| A | HOH1082 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 77 |
| Details | Domain: {"description":"GST N-terminal"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAR-2012","submissionDatabase":"PDB data bank","title":"Structural and functional genomics of YibF, a glutathione transferase homologue from Escherichia coli.","authors":["Ladner J.E.","Stournan N.V.","Branch M.C.","Harp J.","Schaab M.","Brown D.W.","Armstrong R.N."]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Binding site: {} |
| Chain | Residue | Details |
