3CLH
Crystal structure of 3-dehydroquinate synthase (DHQS)from Helicobacter pylori
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0003856 | molecular_function | 3-dehydroquinate synthase activity |
| A | 0005737 | cellular_component | cytoplasm |
| 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 | 0016838 | molecular_function | carbon-oxygen lyase activity, acting on phosphates |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0003856 | molecular_function | 3-dehydroquinate synthase activity |
| B | 0005737 | cellular_component | cytoplasm |
| 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 | 0016838 | molecular_function | carbon-oxygen lyase activity, acting on phosphates |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE ZN A 344 |
| Chain | Residue |
| A | HIS248 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE ZN B 344 |
| Chain | Residue |
| B | HIS231 |
| B | HIS248 |
| site_id | AC3 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE NAD A 400 |
| Chain | Residue |
| A | GLY94 |
| A | GLY95 |
| A | ASP99 |
| A | THR119 |
| A | THR120 |
| A | LEU122 |
| A | ASP126 |
| A | ALA127 |
| A | LYS132 |
| A | ASN142 |
| A | PHE159 |
| A | THR162 |
| A | LEU163 |
| A | GLU167 |
| A | ASP34 |
| A | ILE36 |
| A | HIS41 |
| A | SER61 |
| A | GLU63 |
| A | LYS66 |
| site_id | AC4 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE NAD B 401 |
| Chain | Residue |
| B | ASP34 |
| B | ILE36 |
| B | HIS41 |
| B | SER61 |
| B | GLU63 |
| B | LYS66 |
| B | GLY94 |
| B | GLY95 |
| B | ASP99 |
| B | THR119 |
| B | THR120 |
| B | LEU122 |
| B | ASP126 |
| B | ALA127 |
| B | LYS132 |
| B | ASN142 |
| B | PHE159 |
| B | THR162 |
| B | LEU163 |
| B | GLU167 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00110, ECO:0000269|PubMed:18503755 |
| Chain | Residue | Details |
| A | SER61 | |
| A | THR119 | |
| A | PHE159 | |
| B | SER61 | |
| B | THR119 | |
| B | PHE159 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:18503755 |
| Chain | Residue | Details |
| A | GLY95 | |
| A | ASN142 | |
| B | GLY95 | |
| B | ASN142 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 10 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00110 |
| Chain | Residue | Details |
| A | LYS132 | |
| B | HIS248 | |
| A | LYS141 | |
| A | GLU174 | |
| A | HIS231 | |
| A | HIS248 | |
| B | LYS132 | |
| B | LYS141 | |
| B | GLU174 | |
| B | HIS231 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1dqs |
| Chain | Residue | Details |
| A | HIS235 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1dqs |
| Chain | Residue | Details |
| B | HIS235 |
