3S42
Crystal Structure of the 3-Dehydroquinate Dehydratase (aroD) from Salmonella enterica Typhimurium LT2 with Malonate and Boric Acid at the Active Site
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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE MLA B 583 |
| Chain | Residue |
| B | HIS143 |
| B | HOH409 |
| B | LYS170 |
| B | ALA172 |
| B | MET203 |
| B | MET205 |
| B | ARG213 |
| B | PHE225 |
| B | ALA233 |
| B | GLN236 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE DMS B 591 |
| Chain | Residue |
| A | LYS207 |
| A | VAL210 |
| A | HOH348 |
| B | VAL218 |
| B | LEU249 |
| B | ALA252 |
| B | HOH308 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE DMS A 592 |
| Chain | Residue |
| A | GLU217 |
| A | VAL218 |
| A | LEU249 |
| A | HOH277 |
| A | HOH300 |
| B | LYS207 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE DMS B 593 |
| Chain | Residue |
| B | SER83 |
| B | ALA84 |
| B | LEU92 |
| B | TYR97 |
| B | GLU116 |
| B | HOH378 |
| B | HOH398 |
| B | HOH455 |
| B | HOH474 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE DMS B 594 |
| Chain | Residue |
| B | ASN-1 |
| B | ALA0 |
| B | LYS85 |
| B | HIS143 |
| B | ASP144 |
| B | PHE145 |
| B | HIS146 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NI B 589 |
| Chain | Residue |
| A | HIS134 |
| A | HOH547 |
| B | HIS-22 |
| B | HIS-20 |
| B | HIS134 |
| B | IMD253 |
| site_id | AC7 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE IMD B 253 |
| Chain | Residue |
| A | GLN133 |
| A | HIS134 |
| A | HOH547 |
| B | HIS-20 |
| B | ASP106 |
| B | HIS134 |
| B | HOH466 |
| B | NI589 |
| site_id | AC8 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE MLA A 586 |
| Chain | Residue |
| A | HIS143 |
| A | LYS170 |
| A | ALA172 |
| A | MET203 |
| A | MET205 |
| A | ARG213 |
| A | PHE225 |
| A | ALA233 |
| A | GLN236 |
| A | BO3253 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE DMS A 590 |
| Chain | Residue |
| A | SER83 |
| A | ALA84 |
| A | ALA91 |
| A | LEU92 |
| A | TYR97 |
| A | GLU116 |
| A | HOH520 |
| site_id | BC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE DMS A 595 |
| Chain | Residue |
| A | LYS2 |
| A | HIS146 |
| A | GLN156 |
| A | GLU193 |
| A | ARG194 |
| A | TYR195 |
| A | ALA196 |
| site_id | BC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE BO3 A 253 |
| Chain | Residue |
| A | SER21 |
| A | GLU46 |
| A | ARG48 |
| A | ARG82 |
| A | LYS170 |
| A | HOH307 |
| A | HOH374 |
| A | HOH404 |
| A | MLA586 |
Functional Information from PROSITE/UniProt
| site_id | PS01028 |
| Number of Residues | 31 |
| Details | DEHYDROQUINASE_I Dehydroquinase class I active site. DLELftgddevkatvgyahqhnvaVImSNHD |
| Chain | Residue | Details |
| B | 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 |
| B | HIS143 | |
| A | 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 |
| B | LYS170 | |
| A | 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 |
| B | SER21 | |
| A | 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 |
| B | GLU46 | |
| B | ARG213 | |
| B | GLN236 | |
| A | GLU46 | |
| A | ARG213 | |
| A | 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 |
| B | ARG82 | |
| A | 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 |
| B | SER232 | |
| A | SER232 |
