3UH1
Crystal Structure of Saccharopine Dehydrogenase from Saccharomyces cerevisiae with bound saccharopine and NADH
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 | 0008652 | biological_process | amino acid biosynthetic process |
| A | 0009085 | biological_process | lysine biosynthetic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016558 | biological_process | protein import into peroxisome matrix |
| A | 0019878 | biological_process | lysine biosynthetic process via aminoadipic acid |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE NAI A 374 |
| Chain | Residue |
| A | ALA139 |
| A | CYS249 |
| A | ILE250 |
| A | TYR251 |
| A | ILE256 |
| A | VAL278 |
| A | SER279 |
| A | ILE318 |
| A | ASP319 |
| A | HIS320 |
| A | LEU321 |
| A | ILE199 |
| A | PRO322 |
| A | SHR375 |
| A | HOH380 |
| A | HOH387 |
| A | HOH392 |
| A | HOH400 |
| A | HOH412 |
| A | HOH434 |
| A | HOH506 |
| A | GLY200 |
| A | GLY203 |
| A | ARG204 |
| A | SER205 |
| A | ASP227 |
| A | ILE228 |
| A | THR231 |
| site_id | AC2 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE SHR A 375 |
| Chain | Residue |
| A | ARG18 |
| A | LYS77 |
| A | PHE94 |
| A | HIS96 |
| A | LYS99 |
| A | GLN101 |
| A | ARG131 |
| A | ALA134 |
| A | PHE135 |
| A | SER279 |
| A | ASP281 |
| A | ASP319 |
| A | PRO322 |
| A | NAI374 |
| A | HOH387 |
| A | HOH400 |
| A | HOH404 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL A 376 |
| Chain | Residue |
| A | VAL132 |
| A | ALA133 |
| A | ALA134 |
| A | ARG204 |
| A | PHE332 |
| A | ASP336 |
| A | HOH491 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"22243403","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17939687","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"22243403","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17939687","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"22243403","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17939687","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"3UH1","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 5 |
| Details | Binding site: {"evidences":[{"source":"PDB","id":"3UH1","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PDB","id":"3UHA","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"22243403","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17939687","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"3UH1","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3UHA","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"22243403","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3UH1","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3UHA","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
