3JYO
Quinate dehydrogenase from Corynebacterium glutamicum in complex with NAD
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004764 | molecular_function | shikimate 3-dehydrogenase (NADP+) 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 | 0016491 | molecular_function | oxidoreductase activity |
| A | 0019632 | biological_process | shikimate metabolic process |
| A | 0030266 | molecular_function | quinate 3-dehydrogenase (NAD+) activity |
| A | 0050661 | molecular_function | NADP binding |
| A | 0052734 | molecular_function | shikimate 3-dehydrogenase (NAD+) activity |
| A | 0070403 | molecular_function | NAD+ binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE NAD A 377 |
| Chain | Residue |
| A | VAL133 |
| A | MET206 |
| A | VAL228 |
| A | VAL229 |
| A | TYR230 |
| A | GLY251 |
| A | MET254 |
| A | ALA255 |
| A | HOH296 |
| A | HOH314 |
| A | HOH418 |
| A | GLY136 |
| A | HOH458 |
| A | HOH494 |
| A | HOH543 |
| A | HOH552 |
| A | HOH583 |
| A | HOH614 |
| A | HOH685 |
| A | HOH699 |
| A | HOH724 |
| A | GLY137 |
| A | VAL138 |
| A | ASP158 |
| A | LEU159 |
| A | ARG163 |
| A | THR202 |
| A | PRO203 |
Functional Information from PROSITE/UniProt
| site_id | PS00962 |
| Number of Residues | 12 |
| Details | RIBOSOMAL_S2_1 Ribosomal protein S2 signature 1. LkTLLDAALYLG |
| Chain | Residue | Details |
| A | LEU51-GLY62 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_00222","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"23929881","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"23929881","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3JYP","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"23929881","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3JYQ","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00222","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"23929881","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3JYO","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3JYP","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3JYQ","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 5 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"23929881","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3JYO","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3JYP","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3JYQ","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"23929881","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3JYP","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3JYQ","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
