1NPD
X-RAY STRUCTURE OF SHIKIMATE DEHYDROGENASE COMPLEXED WITH NAD+ FROM E.COLI (YDIB) NORTHEAST STRUCTURAL GENOMICS RESEARCH CONSORTIUM (NESG) TARGET ER24
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004764 | molecular_function | shikimate 3-dehydrogenase (NADP+) activity |
| A | 0005515 | molecular_function | protein binding |
| 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 | 0042803 | molecular_function | protein homodimerization activity |
| A | 0052733 | molecular_function | quinate 3-dehydrogenase (NADP+) activity |
| A | 0052734 | molecular_function | shikimate 3-dehydrogenase (NAD+) activity |
| B | 0004764 | molecular_function | shikimate 3-dehydrogenase (NADP+) activity |
| B | 0005515 | molecular_function | protein binding |
| 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 | 0016491 | molecular_function | oxidoreductase activity |
| B | 0019632 | biological_process | shikimate metabolic process |
| B | 0030266 | molecular_function | quinate 3-dehydrogenase (NAD+) activity |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0052733 | molecular_function | quinate 3-dehydrogenase (NADP+) activity |
| B | 0052734 | molecular_function | shikimate 3-dehydrogenase (NAD+) activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE NAD A 300 |
| Chain | Residue |
| A | ASP107 |
| A | PHE160 |
| A | LEU184 |
| A | GLY203 |
| A | THR204 |
| A | LYS205 |
| A | VAL206 |
| A | MSE208 |
| A | CYS232 |
| A | VAL233 |
| A | TYR234 |
| A | GLY131 |
| A | ASN235 |
| A | GLY255 |
| A | MSE258 |
| A | LEU259 |
| A | HOH3013 |
| A | HOH3320 |
| A | HOH3321 |
| A | ALA132 |
| A | GLY133 |
| A | GLY134 |
| A | ALA135 |
| A | ASN155 |
| A | ARG156 |
| A | ASP158 |
| site_id | AC2 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE NAD B 300 |
| Chain | Residue |
| B | ASP107 |
| B | ALA132 |
| B | GLY133 |
| B | GLY134 |
| B | ALA135 |
| B | ASN155 |
| B | ARG156 |
| B | ASP158 |
| B | PHE160 |
| B | GLY203 |
| B | THR204 |
| B | LYS205 |
| B | VAL206 |
| B | MSE208 |
| B | CYS232 |
| B | TYR234 |
| B | GLY255 |
| B | MSE258 |
| B | LEU259 |
| B | HOH3014 |
| B | HOH3106 |
| B | HOH3111 |
| B | HOH3127 |
| B | HOH3271 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01578","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 20 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01578","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"12624088","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12637497","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16021622","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1nvt |
| Chain | Residue | Details |
| A | ASP98 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1nvt |
| Chain | Residue | Details |
| B | ASP98 |
