5U5I
The dimeric crystal structure of the selenomethionine derivative of HTPA Reductase from Sellaginella moellendorffii
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0008652 | biological_process | amino acid biosynthetic process |
| A | 0008839 | molecular_function | 4-hydroxy-tetrahydrodipicolinate reductase activity |
| A | 0009085 | biological_process | L-lysine biosynthetic process |
| A | 0009089 | biological_process | L-lysine biosynthetic process via diaminopimelate |
| A | 0009570 | cellular_component | chloroplast stroma |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0019877 | biological_process | diaminopimelate biosynthetic process |
| A | 0070402 | molecular_function | NADPH binding |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0008652 | biological_process | amino acid biosynthetic process |
| B | 0008839 | molecular_function | 4-hydroxy-tetrahydrodipicolinate reductase activity |
| B | 0009085 | biological_process | L-lysine biosynthetic process |
| B | 0009089 | biological_process | L-lysine biosynthetic process via diaminopimelate |
| B | 0009570 | cellular_component | chloroplast stroma |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0019877 | biological_process | diaminopimelate biosynthetic process |
| B | 0070402 | molecular_function | NADPH binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 30 |
| Details | binding site for residue NAD A 301 |
| Chain | Residue |
| A | ASP20 |
| A | VAL67 |
| A | TYR89 |
| A | THR90 |
| A | LEU91 |
| A | ALA94 |
| A | GLY112 |
| A | THR113 |
| A | THR114 |
| A | ALA135 |
| A | PRO136 |
| A | GLY23 |
| A | GLN137 |
| A | MSE138 |
| A | TYR252 |
| A | HOH406 |
| A | HOH410 |
| A | HOH428 |
| A | HOH431 |
| A | HOH432 |
| A | HOH448 |
| A | HOH458 |
| A | LYS24 |
| B | ARG50 |
| A | VAL25 |
| A | LEU45 |
| A | THR46 |
| A | GLY47 |
| A | PRO48 |
| A | ARG50 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue CA A 302 |
| Chain | Residue |
| A | THR22 |
| A | ARG50 |
| A | LYS53 |
| B | THR22 |
| B | ARG50 |
| B | LYS53 |
| site_id | AC3 |
| Number of Residues | 31 |
| Details | binding site for residue NAD B 301 |
| Chain | Residue |
| A | ARG50 |
| B | ASP20 |
| B | GLY23 |
| B | LYS24 |
| B | VAL25 |
| B | LEU45 |
| B | THR46 |
| B | GLY47 |
| B | ARG50 |
| B | VAL67 |
| B | TYR89 |
| B | THR90 |
| B | ALA94 |
| B | ASN98 |
| B | GLY112 |
| B | THR113 |
| B | THR114 |
| B | ALA135 |
| B | PRO136 |
| B | GLN137 |
| B | MSE138 |
| B | TYR252 |
| B | HOH418 |
| B | HOH425 |
| B | HOH433 |
| B | HOH437 |
| B | HOH454 |
| B | HOH459 |
| B | HOH470 |
| B | HOH478 |
| B | HOH479 |
