3JS3
Crystal structure of type I 3-dehydroquinate dehydratase (aroD) from Clostridium difficile with covalent reaction intermediate
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003855 | molecular_function | 3-dehydroquinate dehydratase activity |
| A | 0008652 | biological_process | amino acid biosynthetic process |
| A | 0009073 | biological_process | aromatic amino acid family biosynthetic process |
| A | 0009423 | biological_process | chorismate biosynthetic process |
| A | 0016829 | molecular_function | lyase activity |
| A | 0046279 | biological_process | 3,4-dihydroxybenzoate biosynthetic process |
| B | 0003855 | molecular_function | 3-dehydroquinate dehydratase activity |
| B | 0008652 | biological_process | amino acid biosynthetic process |
| B | 0009073 | biological_process | aromatic amino acid family biosynthetic process |
| B | 0009423 | biological_process | chorismate biosynthetic process |
| B | 0016829 | molecular_function | lyase activity |
| B | 0046279 | biological_process | 3,4-dihydroxybenzoate biosynthetic process |
| C | 0003855 | molecular_function | 3-dehydroquinate dehydratase activity |
| C | 0008652 | biological_process | amino acid biosynthetic process |
| C | 0009073 | biological_process | aromatic amino acid family biosynthetic process |
| C | 0009423 | biological_process | chorismate biosynthetic process |
| C | 0016829 | molecular_function | lyase activity |
| C | 0046279 | biological_process | 3,4-dihydroxybenzoate biosynthetic process |
| D | 0003855 | molecular_function | 3-dehydroquinate dehydratase activity |
| D | 0008652 | biological_process | amino acid biosynthetic process |
| D | 0009073 | biological_process | aromatic amino acid family biosynthetic process |
| D | 0009423 | biological_process | chorismate biosynthetic process |
| D | 0016829 | molecular_function | lyase activity |
| D | 0046279 | biological_process | 3,4-dihydroxybenzoate biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE DHS A 301 |
| Chain | Residue |
| A | GLU47 |
| A | GLN237 |
| A | HOH282 |
| A | HOH304 |
| A | ARG49 |
| A | ARG83 |
| A | LYS171 |
| A | MET204 |
| A | ARG214 |
| A | PHE226 |
| A | SER233 |
| A | ALA234 |
| site_id | AC2 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE DHS B 301 |
| Chain | Residue |
| B | GLU47 |
| B | ARG49 |
| B | ARG83 |
| B | HIS144 |
| B | LYS171 |
| B | MET204 |
| B | ARG214 |
| B | PHE226 |
| B | SER233 |
| B | ALA234 |
| B | GLN237 |
| B | HOH321 |
| B | HOH322 |
| site_id | AC3 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE DHS C 301 |
| Chain | Residue |
| C | GLU47 |
| C | ARG49 |
| C | ARG83 |
| C | LYS171 |
| C | MET204 |
| C | ARG214 |
| C | PHE226 |
| C | SER233 |
| C | ALA234 |
| C | GLN237 |
| C | HOH278 |
| site_id | AC4 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE DHS D 301 |
| Chain | Residue |
| D | GLU47 |
| D | ARG49 |
| D | ARG83 |
| D | HIS144 |
| D | LYS171 |
| D | MET204 |
| D | ARG214 |
| D | PHE226 |
| D | SER233 |
| D | ALA234 |
| D | GLN237 |
| D | HOH320 |
Functional Information from PROSITE/UniProt
| site_id | PS01028 |
| Number of Residues | 31 |
| Details | DEHYDROQUINASE_I Dehydroquinase class I active site. DVELfmgdevidevvnfahkkevkVIiSNHD |
| Chain | Residue | Details |
| A | ASP115-ASP145 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_00214, ECO:0000269|Ref.3 |
| Chain | Residue | Details |
| A | HIS144 | |
| B | HIS144 | |
| C | HIS144 | |
| D | HIS144 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | ACT_SITE: Schiff-base intermediate with substrate => ECO:0000255|HAMAP-Rule:MF_00214, ECO:0000269|PubMed:21087925, ECO:0000269|Ref.3 |
| Chain | Residue | Details |
| A | LYS171 | |
| B | LYS171 | |
| C | LYS171 | |
| D | LYS171 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00214, ECO:0000269|PubMed:21087925 |
| Chain | Residue | Details |
| A | GLU47 | |
| A | SER233 | |
| B | GLU47 | |
| B | SER233 | |
| C | GLU47 | |
| C | SER233 | |
| D | GLU47 | |
| D | SER233 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00214, ECO:0000269|PubMed:21087925, ECO:0000269|Ref.3 |
| Chain | Residue | Details |
| A | ARG83 | |
| D | ARG83 | |
| D | ARG214 | |
| D | GLN237 | |
| A | ARG214 | |
| A | GLN237 | |
| B | ARG83 | |
| B | ARG214 | |
| B | GLN237 | |
| C | ARG83 | |
| C | ARG214 | |
| C | GLN237 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1qfe |
| Chain | Residue | Details |
| A | GLU87 | |
| A | HIS144 | |
| A | LYS171 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1qfe |
| Chain | Residue | Details |
| B | GLU87 | |
| B | HIS144 | |
| B | LYS171 |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1qfe |
| Chain | Residue | Details |
| C | GLU87 | |
| C | HIS144 | |
| C | LYS171 |
| site_id | CSA4 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1qfe |
| Chain | Residue | Details |
| D | GLU87 | |
| D | HIS144 | |
| D | LYS171 |
