1F05
CRYSTAL STRUCTURE OF HUMAN TRANSALDOLASE
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004801 | molecular_function | transaldolase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005634 | cellular_component | nucleus |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0005975 | biological_process | carbohydrate metabolic process |
| A | 0006002 | biological_process | fructose 6-phosphate metabolic process |
| A | 0006098 | biological_process | pentose-phosphate shunt |
| A | 0009052 | biological_process | pentose-phosphate shunt, non-oxidative branch |
| A | 0016740 | molecular_function | transferase activity |
| A | 0019682 | biological_process | glyceraldehyde-3-phosphate metabolic process |
| A | 0030246 | molecular_function | carbohydrate binding |
| A | 0048029 | molecular_function | monosaccharide binding |
| A | 0070062 | cellular_component | extracellular exosome |
| B | 0004801 | molecular_function | transaldolase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005634 | cellular_component | nucleus |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0005975 | biological_process | carbohydrate metabolic process |
| B | 0006002 | biological_process | fructose 6-phosphate metabolic process |
| B | 0006098 | biological_process | pentose-phosphate shunt |
| B | 0009052 | biological_process | pentose-phosphate shunt, non-oxidative branch |
| B | 0016740 | molecular_function | transferase activity |
| B | 0019682 | biological_process | glyceraldehyde-3-phosphate metabolic process |
| B | 0030246 | molecular_function | carbohydrate binding |
| B | 0048029 | molecular_function | monosaccharide binding |
| B | 0070062 | cellular_component | extracellular exosome |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Schiff-base intermediate with substrate => ECO:0000269|PubMed:10869557 |
| Chain | Residue | Details |
| A | LYS142 | |
| B | LYS142 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q93092 |
| Chain | Residue | Details |
| A | LYS115 | |
| B | LYS115 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861 |
| Chain | Residue | Details |
| A | LYS219 | |
| A | LYS269 | |
| A | LYS286 | |
| A | LYS321 | |
| B | LYS219 | |
| B | LYS269 | |
| B | LYS286 | |
| B | LYS321 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569 |
| Chain | Residue | Details |
| A | SER237 | |
| B | SER237 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163 |
| Chain | Residue | Details |
| A | SER256 | |
| B | SER256 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1onr |
| Chain | Residue | Details |
| A | LYS142 | |
| A | GLU106 | |
| A | ASP27 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1onr |
| Chain | Residue | Details |
| B | LYS142 | |
| B | GLU106 | |
| B | ASP27 |
