4H3D
1.95 Angstrom Crystal Structure of of Type I 3-Dehydroquinate Dehydratase (aroD) from Clostridium difficile with Covalent Modified Comenic Acid.
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 | 3 |
| Details | BINDING SITE FOR RESIDUE PGE A 301 |
| Chain | Residue |
| A | GLY88 |
| A | PHE146 |
| A | HOH606 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PEG A 302 |
| Chain | Residue |
| A | ILE24 |
| A | ARG49 |
| A | GLN237 |
| A | HOH602 |
| A | HOH623 |
| site_id | AC3 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE SHL A 303 |
| Chain | Residue |
| A | HIS144 |
| A | LYS171 |
| A | MET204 |
| A | ARG214 |
| A | PHE226 |
| A | GLN237 |
| A | HOH592 |
| A | HOH594 |
| A | HOH595 |
| A | HOH602 |
| A | ARG83 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE PEG B 301 |
| Chain | Residue |
| B | VAL86 |
| B | GLY88 |
| B | HOH521 |
| site_id | AC5 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SHL B 302 |
| Chain | Residue |
| B | ARG83 |
| B | HIS144 |
| B | LYS171 |
| B | MET204 |
| B | ARG214 |
| B | PHE226 |
| B | GLN237 |
| B | HOH450 |
| B | HOH574 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ACT B 303 |
| Chain | Residue |
| B | ASP145 |
| B | PHE146 |
| B | ASN147 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE PGE C 301 |
| Chain | Residue |
| C | PHE146 |
| C | HOH538 |
| C | HOH611 |
| site_id | AC8 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SHL C 302 |
| Chain | Residue |
| C | ARG83 |
| C | HIS144 |
| C | LYS171 |
| C | MET204 |
| C | ARG214 |
| C | PHE226 |
| C | GLN237 |
| C | HOH515 |
| C | HOH516 |
| site_id | AC9 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE SHL D 301 |
| Chain | Residue |
| D | ARG83 |
| D | HIS144 |
| D | LYS171 |
| D | MET204 |
| D | ARG214 |
| D | PHE226 |
| D | GLN237 |
| D | HOH437 |
| D | HOH486 |
| D | HOH525 |
| D | HOH537 |
| site_id | BC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ACT D 302 |
| Chain | Residue |
| D | GLU87 |
| D | PHE119 |
| D | ASN143 |
| site_id | BC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ACT D 303 |
| Chain | Residue |
| D | PHE146 |
| D | ASN147 |
| D | HOH461 |
| D | HOH551 |
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 |
| D | HIS144 | |
| A | HIS144 | |
| B | HIS144 | |
| C | 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 | |
| D | LYS171 | |
| B | LYS171 | |
| C | 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 |
| C | GLU47 | |
| A | GLU47 | |
| A | SER233 | |
| B | GLU47 | |
| B | SER233 | |
| 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 | |
| B | ARG214 | |
| B | GLN237 | |
| C | ARG83 | |
| C | ARG214 | |
| C | GLN237 | |
| D | ARG83 | |
| D | ARG214 | |
| D | GLN237 | |
| A | ARG214 | |
| A | GLN237 | |
| B | ARG83 |
