9QPK
E.coli TalB mutant E96Q, F178Y, R300E
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 | 0006098 | biological_process | pentose-phosphate shunt |
| A | 0009052 | biological_process | pentose-phosphate shunt, non-oxidative branch |
| A | 0016020 | cellular_component | membrane |
| 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 | 0006098 | biological_process | pentose-phosphate shunt |
| B | 0009052 | biological_process | pentose-phosphate shunt, non-oxidative branch |
| B | 0016020 | cellular_component | membrane |
| B | 0016744 | molecular_function | transketolase or transaldolase activity |
| C | 0004801 | molecular_function | transaldolase activity |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0005829 | cellular_component | cytosol |
| C | 0006098 | biological_process | pentose-phosphate shunt |
| C | 0009052 | biological_process | pentose-phosphate shunt, non-oxidative branch |
| C | 0016020 | cellular_component | membrane |
| C | 0016744 | molecular_function | transketolase or transaldolase activity |
| D | 0004801 | molecular_function | transaldolase activity |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0005829 | cellular_component | cytosol |
| D | 0006098 | biological_process | pentose-phosphate shunt |
| D | 0009052 | biological_process | pentose-phosphate shunt, non-oxidative branch |
| D | 0016020 | cellular_component | membrane |
| D | 0016744 | molecular_function | transketolase or transaldolase activity |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_00492","evidenceCode":"ECO:0000255"},{"source":"Reference","evidenceCode":"ECO:0000305","citation":{"citationType":"journal article","publicationDate":"2015","firstPage":"3140","lastPage":"3151","volume":"7","journal":"ChemCatChem","title":"Acid Base Catalyst Discriminates between a Fructose 6-Phosphate Aldolase and a Transaldolase.","authors":["Stellmacher L.","Sandalova T.","Leptihn S.","Schneider G.","Sprenger G.A.","Samland A.K."],"citationCrossReferences":[{"database":"DOI","id":"10.1002/cctc.201500478"}]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Nucleophile; Schiff-base intermediate with substrate","evidences":[{"source":"HAMAP-Rule","id":"MF_00492","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"11298760","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"journal article","publicationDate":"2015","firstPage":"3140","lastPage":"3151","volume":"7","journal":"ChemCatChem","title":"Acid Base Catalyst Discriminates between a Fructose 6-Phosphate Aldolase and a Transaldolase.","authors":["Stellmacher L.","Sandalova T.","Leptihn S.","Schneider G.","Sprenger G.A.","Samland A.K."],"citationCrossReferences":[{"database":"DOI","id":"10.1002/cctc.201500478"}]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 32 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"27050126","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4S2C","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
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 | TYR178 | 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 | TYR178 | steric role |
| site_id | MCSA3 |
| Number of Residues | 5 |
| Details | M-CSA 148 |
| Chain | Residue | Details |
| C | ASP17 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| C | GLN96 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| C | LYS132 | covalently attached, electron pair acceptor, electron pair donor, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor |
| C | THR156 | electrostatic stabiliser, hydrogen bond donor |
| C | TYR178 | steric role |
| site_id | MCSA4 |
| Number of Residues | 5 |
| Details | M-CSA 148 |
| Chain | Residue | Details |
| D | ASP17 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| D | GLN96 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| D | LYS132 | covalently attached, electron pair acceptor, electron pair donor, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor |
| D | THR156 | electrostatic stabiliser, hydrogen bond donor |
| D | TYR178 | steric role |
