4GUI
1.78 Angstrom Crystal Structure of the Salmonella enterica 3-Dehydroquinate Dehydratase (aroD) in Complex with Quinate
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003855 | molecular_function | 3-dehydroquinate dehydratase activity |
| A | 0005829 | cellular_component | cytosol |
| 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 | 0005829 | cellular_component | cytosol |
| 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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE QIC A 301 |
| Chain | Residue |
| A | SER21 |
| A | SER232 |
| A | ALA233 |
| A | GLN236 |
| A | HOH447 |
| A | GLU46 |
| A | ARG48 |
| A | ARG82 |
| A | HIS143 |
| A | LYS170 |
| A | MET205 |
| A | ARG213 |
| A | PHE225 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NI A 302 |
| Chain | Residue |
| A | HIS250 |
| A | HOH483 |
| A | HOH484 |
| A | HOH485 |
| A | HOH486 |
| A | HOH487 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NI A 303 |
| Chain | Residue |
| A | ASP106 |
| A | HIS134 |
| A | HOH489 |
| A | HOH490 |
| A | HOH491 |
| B | GLU59 |
| site_id | AC4 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE QIC B 301 |
| Chain | Residue |
| B | LYS170 |
| B | MET203 |
| B | MET205 |
| B | ARG213 |
| B | PHE225 |
| B | GLN236 |
| B | HOH423 |
| B | HOH480 |
| B | HOH503 |
| B | HOH543 |
| B | HOH545 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NI B 302 |
| Chain | Residue |
| B | HIS250 |
| B | HOH504 |
| B | HOH505 |
| B | HOH506 |
| B | HOH507 |
| B | HOH508 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NI B 303 |
| Chain | Residue |
| B | HIS134 |
| B | HOH509 |
| B | HOH510 |
| B | HOH511 |
| B | HOH512 |
| B | HOH533 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE NI B 304 |
| Chain | Residue |
| B | HIS132 |
| B | HOH513 |
| B | HOH514 |
| B | HOH519 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NI B 305 |
| Chain | Residue |
| A | HIS146 |
| B | HIS146 |
| B | HOH515 |
| B | HOH516 |
| B | HOH517 |
Functional Information from PROSITE/UniProt
| site_id | PS01028 |
| Number of Residues | 31 |
| Details | DEHYDROQUINASE_I Dehydroquinase class I active site. DLELftgddevkatvgyahqhnvaVImSNHD |
| Chain | Residue | Details |
| A | ASP114-ASP144 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_00214, ECO:0000269|PubMed:21087925, ECO:0000269|PubMed:23341204, ECO:0000269|PubMed:24437575, ECO:0000269|Ref.4, ECO:0000269|Ref.8 |
| Chain | Residue | Details |
| A | HIS143 | |
| B | HIS143 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | ACT_SITE: Schiff-base intermediate with substrate => ECO:0000255|HAMAP-Rule:MF_00214, ECO:0000269|PubMed:21087925, ECO:0000269|PubMed:23341204, ECO:0000269|Ref.4, ECO:0000269|Ref.7, ECO:0000269|Ref.8 |
| Chain | Residue | Details |
| A | LYS170 | |
| B | LYS170 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00214, ECO:0000269|PubMed:21087925, ECO:0000269|PubMed:24437575, ECO:0000269|Ref.4, ECO:0000269|Ref.7 |
| Chain | Residue | Details |
| A | SER21 | |
| B | SER21 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00214, ECO:0000269|PubMed:21087925, ECO:0000269|PubMed:23341204, ECO:0000269|PubMed:24437575, ECO:0000269|Ref.4, ECO:0000269|Ref.7 |
| Chain | Residue | Details |
| A | GLU46 | |
| A | ARG213 | |
| A | GLN236 | |
| B | GLU46 | |
| B | ARG213 | |
| B | GLN236 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00214, ECO:0000269|PubMed:21087925, ECO:0000269|PubMed:23341204, ECO:0000269|PubMed:24437575, ECO:0000269|Ref.4, ECO:0000269|Ref.7, ECO:0000269|Ref.8 |
| Chain | Residue | Details |
| A | ARG82 | |
| B | ARG82 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00214, ECO:0000269|PubMed:21087925, ECO:0000269|PubMed:24437575, ECO:0000269|Ref.4 |
| Chain | Residue | Details |
| A | SER232 | |
| B | SER232 |
