3O1N
1.03 Angstrom Crystal Structure of Q236A Mutant Type I Dehydroquinate Dehydratase (aroD) from Salmonella typhimurium
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 | 3 |
Details | BINDING SITE FOR RESIDUE CL A 253 |
Chain | Residue |
A | ARG213 |
A | PHE225 |
A | ALA233 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG A 254 |
Chain | Residue |
A | HIS134 |
A | HOH391 |
A | HOH458 |
A | HOH627 |
A | HOH628 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG A 255 |
Chain | Residue |
A | HOH279 |
A | HOH300 |
A | HOH427 |
A | HOH690 |
A | GLU217 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG B 253 |
Chain | Residue |
B | HIS134 |
B | HOH447 |
B | HOH463 |
B | HOH481 |
B | HOH592 |
B | HOH619 |
site_id | AC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG B 254 |
Chain | Residue |
B | HOH259 |
B | HOH281 |
B | HOH379 |
B | HOH419 |
B | HOH457 |
B | HOH621 |
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 | ALA236 | |
B | GLU46 | |
B | ARG213 | |
B | ALA236 |
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 |