1VI2
Crystal structure of shikimate-5-dehydrogenase with NAD
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 | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 A 299 |
| Chain | Residue |
| A | SER67 |
| A | MSE68 |
| A | PRO69 |
| A | ASN70 |
| A | LYS71 |
| A | GLN72 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 B 299 |
| Chain | Residue |
| B | LYS71 |
| B | GLN72 |
| B | HOH316 |
| B | HOH356 |
| B | MSE68 |
| B | PRO69 |
| B | ASN70 |
| site_id | AC3 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE NAD A 300 |
| Chain | Residue |
| A | GLY131 |
| A | ALA132 |
| A | GLY133 |
| A | GLY134 |
| A | ALA135 |
| A | ASN155 |
| A | ARG156 |
| A | ASP158 |
| A | PHE160 |
| A | GLY203 |
| A | THR204 |
| A | LYS205 |
| A | VAL206 |
| A | MSE208 |
| A | CYS232 |
| A | VAL233 |
| A | TYR234 |
| A | GLY255 |
| A | MSE258 |
| A | LEU259 |
| A | HOH313 |
| A | HOH327 |
| A | HOH328 |
| A | HOH329 |
| A | HOH334 |
| A | HOH398 |
| A | HOH399 |
| A | HOH402 |
| site_id | AC4 |
| Number of Residues | 29 |
| 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 | VAL233 |
| B | TYR234 |
| B | GLY255 |
| B | MSE258 |
| B | LEU259 |
| B | HOH304 |
| B | HOH309 |
| B | HOH315 |
| B | HOH335 |
| B | HOH351 |
| B | HOH394 |
| B | HOH400 |
| B | HOH409 |
| B | HOH425 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01578 |
| Chain | Residue | Details |
| A | LYS71 | |
| A | ASP107 | |
| B | LYS71 | |
| B | ASP107 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 10 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01578, ECO:0000269|PubMed:12624088, ECO:0000269|PubMed:12637497, ECO:0000269|PubMed:16021622 |
| Chain | Residue | Details |
| A | GLY255 | |
| B | ALA132 | |
| B | ASN155 | |
| B | LYS205 | |
| B | CYS232 | |
| B | GLY255 | |
| A | ALA132 | |
| A | ASN155 | |
| A | LYS205 | |
| A | CYS232 |
