4RZ5
Transaldolase B E96Q from E.coli
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004801 | molecular_function | transaldolase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0005975 | biological_process | carbohydrate metabolic process |
| A | 0006098 | biological_process | pentose-phosphate shunt |
| A | 0009052 | biological_process | pentose-phosphate shunt, non-oxidative branch |
| A | 0016020 | cellular_component | membrane |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016744 | molecular_function | transketolase or transaldolase activity |
| B | 0004801 | molecular_function | transaldolase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0005975 | biological_process | carbohydrate metabolic process |
| B | 0006098 | biological_process | pentose-phosphate shunt |
| B | 0009052 | biological_process | pentose-phosphate shunt, non-oxidative branch |
| B | 0016020 | cellular_component | membrane |
| B | 0016740 | molecular_function | transferase activity |
| B | 0016744 | molecular_function | transketolase or transaldolase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 401 |
| Chain | Residue |
| A | ARG181 |
| A | SER226 |
| A | ARG228 |
| A | HOH680 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 A 402 |
| Chain | Residue |
| A | HOH539 |
| B | LYS50 |
| A | ARG92 |
| A | PHE173 |
| A | ARG241 |
| A | HOH526 |
| A | HOH530 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 B 401 |
| Chain | Residue |
| A | LYS50 |
| A | HOH690 |
| B | ARG92 |
| B | PHE173 |
| B | ARG241 |
| B | HOH563 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 B 402 |
| Chain | Residue |
| B | ARG181 |
| B | SER226 |
| B | ARG228 |
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:11298760 |
| Chain | Residue | Details |
| A | LYS132 | |
| B | LYS132 |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 5 |
| Details | M-CSA 148 |
| Chain | Residue | Details |
| A | ASP17 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | GLN96 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | LYS132 | covalently attached, electron pair acceptor, electron pair donor, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor |
| A | THR156 | electrostatic stabiliser, hydrogen bond donor |
| A | PHE178 | steric role |
| site_id | MCSA2 |
| Number of Residues | 5 |
| Details | M-CSA 148 |
| Chain | Residue | Details |
| B | ASP17 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| B | GLN96 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| B | LYS132 | covalently attached, electron pair acceptor, electron pair donor, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor |
| B | THR156 | electrostatic stabiliser, hydrogen bond donor |
| B | PHE178 | steric role |
