3UHA
Crystal Structure of Saccharopine Dehydrogenase from Saccharomyces cervisiae complexed with NAD.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003729 | molecular_function | mRNA binding |
| A | 0004753 | molecular_function | saccharopine dehydrogenase activity |
| A | 0004754 | molecular_function | saccharopine dehydrogenase (NAD+, L-lysine-forming) activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005777 | cellular_component | peroxisome |
| A | 0006553 | biological_process | lysine metabolic process |
| A | 0008652 | biological_process | amino acid biosynthetic process |
| A | 0009085 | biological_process | lysine biosynthetic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0019878 | biological_process | lysine biosynthetic process via aminoadipic acid |
| B | 0003729 | molecular_function | mRNA binding |
| B | 0004753 | molecular_function | saccharopine dehydrogenase activity |
| B | 0004754 | molecular_function | saccharopine dehydrogenase (NAD+, L-lysine-forming) activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005777 | cellular_component | peroxisome |
| B | 0006553 | biological_process | lysine metabolic process |
| B | 0008652 | biological_process | amino acid biosynthetic process |
| B | 0009085 | biological_process | lysine biosynthetic process |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0019878 | biological_process | lysine biosynthetic process via aminoadipic acid |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE NAD A 374 |
| Chain | Residue |
| A | ARG130 |
| A | THR231 |
| A | ILE250 |
| A | TYR251 |
| A | ILE256 |
| A | VAL278 |
| A | ILE318 |
| A | ASP319 |
| A | HIS320 |
| A | LEU321 |
| A | PRO322 |
| A | ALA139 |
| A | ILE199 |
| A | GLY200 |
| A | GLY203 |
| A | ARG204 |
| A | SER205 |
| A | ASP227 |
| A | ILE228 |
| site_id | AC2 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE NAD B 374 |
| Chain | Residue |
| B | ARG130 |
| B | ALA139 |
| B | ILE199 |
| B | GLY200 |
| B | GLY203 |
| B | ARG204 |
| B | SER205 |
| B | ASP227 |
| B | ILE228 |
| B | THR231 |
| B | CYS249 |
| B | ILE250 |
| B | TYR251 |
| B | ILE256 |
| B | VAL278 |
| B | ILE318 |
| B | ASP319 |
| B | HIS320 |
| B | LEU321 |
| B | PRO322 |
| B | HOH377 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL A 375 |
| Chain | Residue |
| A | LYS193 |
| B | LYS193 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton acceptor => ECO:0000269|PubMed:22243403, ECO:0000305|PubMed:17939687 |
| Chain | Residue | Details |
| A | LYS77 | |
| B | LYS77 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton donor => ECO:0000269|PubMed:22243403, ECO:0000305|PubMed:17939687 |
| Chain | Residue | Details |
| A | HIS96 | |
| B | HIS96 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:22243403, ECO:0000305|PubMed:17939687, ECO:0007744|PDB:3UH1 |
| Chain | Residue | Details |
| A | ARG18 | |
| A | LYS77 | |
| A | ARG131 | |
| B | ARG18 | |
| B | LYS77 | |
| B | ARG131 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0007744|PDB:3UH1 |
| Chain | Residue | Details |
| A | GLN101 | |
| A | PHE135 | |
| A | TYR251 | |
| A | SER279 | |
| B | GLN101 | |
| B | PHE135 | |
| B | TYR251 | |
| B | SER279 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0007744|PDB:3UHA |
| Chain | Residue | Details |
| A | ARG130 | |
| B | ARG130 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:22243403, ECO:0000305|PubMed:17939687, ECO:0007744|PDB:3UH1, ECO:0007744|PDB:3UHA |
| Chain | Residue | Details |
| A | GLY203 | |
| A | ASP227 | |
| A | THR231 | |
| B | GLY203 | |
| B | ASP227 | |
| B | THR231 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:22243403, ECO:0007744|PDB:3UH1, ECO:0007744|PDB:3UHA |
| Chain | Residue | Details |
| A | VAL278 | |
| A | ILE318 | |
| B | VAL278 | |
| B | ILE318 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | MOD_RES: N-acetylalanine; partial => ECO:0000269|Ref.4 |
| Chain | Residue | Details |
| A | ALA2 | |
| B | ALA2 |
