1QGD
TRANSKETOLASE FROM ESCHERICHIA COLI
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004802 | molecular_function | transketolase activity |
| A | 0005829 | cellular_component | cytosol |
| A | 0006098 | biological_process | pentose-phosphate shunt |
| A | 0009052 | biological_process | pentose-phosphate shunt, non-oxidative branch |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016744 | molecular_function | transketolase or transaldolase activity |
| A | 0030145 | molecular_function | manganese ion binding |
| A | 0030976 | molecular_function | thiamine pyrophosphate binding |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004802 | molecular_function | transketolase activity |
| B | 0005829 | cellular_component | cytosol |
| B | 0006098 | biological_process | pentose-phosphate shunt |
| B | 0009052 | biological_process | pentose-phosphate shunt, non-oxidative branch |
| B | 0016740 | molecular_function | transferase activity |
| B | 0016744 | molecular_function | transketolase or transaldolase activity |
| B | 0030145 | molecular_function | manganese ion binding |
| B | 0030976 | molecular_function | thiamine pyrophosphate binding |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA A 675 |
| Chain | Residue |
| A | ASP155 |
| A | ASN185 |
| A | ILE187 |
| A | TPP670 |
| A | HOH706 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 B 680 |
| Chain | Residue |
| B | ARG358 |
| B | SER385 |
| B | HIS461 |
| B | ARG520 |
| B | HOH954 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA B 675 |
| Chain | Residue |
| B | ASP155 |
| B | ASN185 |
| B | ILE187 |
| B | TPP670 |
| B | HOH712 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 A 680 |
| Chain | Residue |
| A | ARG358 |
| A | SER385 |
| A | HIS461 |
| A | ARG520 |
| A | HOH1174 |
| A | HOH1215 |
| site_id | AC5 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE TPP A 670 |
| Chain | Residue |
| A | ALA29 |
| A | HIS66 |
| A | GLY114 |
| A | LEU116 |
| A | ASP155 |
| A | GLY156 |
| A | GLU160 |
| A | ASN185 |
| A | ILE187 |
| A | ILE189 |
| A | ILE247 |
| A | HIS261 |
| A | CA675 |
| A | HOH706 |
| A | HOH754 |
| A | HOH767 |
| B | ASP381 |
| B | GLU411 |
| B | PHE437 |
| B | TYR440 |
| B | HOH1103 |
| site_id | AC6 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE TPP B 670 |
| Chain | Residue |
| A | ASP381 |
| A | GLU411 |
| A | PHE437 |
| A | TYR440 |
| A | HOH1085 |
| B | ALA29 |
| B | HIS66 |
| B | GLY114 |
| B | LEU116 |
| B | ASP155 |
| B | GLY156 |
| B | GLU160 |
| B | ASN185 |
| B | ILE187 |
| B | ILE189 |
| B | ILE247 |
| B | HIS261 |
| B | CA675 |
| B | HOH712 |
| B | HOH800 |
| B | HOH876 |
| site_id | TPA |
| Number of Residues | 14 |
| Details | COFACTOR BINDING |
| Chain | Residue |
| A | HIS66 |
| A | HIS261 |
| B | ASP381 |
| B | GLU411 |
| B | PHE437 |
| B | TYR440 |
| A | GLY114 |
| A | LEU116 |
| A | ASP155 |
| A | GLY156 |
| A | ASN185 |
| A | ILE187 |
| A | SER188 |
| A | ILE189 |
| site_id | TPB |
| Number of Residues | 14 |
| Details | COFACTOR BINDING |
| Chain | Residue |
| B | HIS66 |
| B | GLY114 |
| B | LEU116 |
| B | ASP155 |
| B | GLY156 |
| B | ASN185 |
| B | ILE187 |
| B | SER188 |
| B | ILE189 |
| B | HIS261 |
| A | ASP381 |
| A | GLU411 |
| A | PHE437 |
| A | TYR440 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton donor => ECO:0000305 |
| Chain | Residue | Details |
| A | GLU411 | |
| B | GLU411 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 14 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:17914867 |
| Chain | Residue | Details |
| A | HIS26 | |
| B | SER385 | |
| B | HIS461 | |
| B | ASP469 | |
| B | HIS473 | |
| B | ARG520 | |
| A | ARG358 | |
| A | SER385 | |
| A | HIS461 | |
| A | ASP469 | |
| A | HIS473 | |
| A | ARG520 | |
| B | HIS26 | |
| B | ARG358 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:17914867, ECO:0000269|Ref.9, ECO:0007744|PDB:1QGD, ECO:0007744|PDB:2R5N |
| Chain | Residue | Details |
| A | HIS66 | |
| A | GLY114 | |
| A | ASN185 | |
| A | HIS261 | |
| B | HIS66 | |
| B | GLY114 | |
| B | ASN185 | |
| B | HIS261 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:17914867, ECO:0000305|Ref.9 |
| Chain | Residue | Details |
| A | ASP155 | |
| A | ILE187 | |
| B | ASP155 | |
| B | ILE187 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|Ref.9, ECO:0007744|PDB:1QGD |
| Chain | Residue | Details |
| A | GLY156 | |
| B | GLY156 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:17914867, ECO:0000269|Ref.9 |
| Chain | Residue | Details |
| A | PHE437 | |
| B | PHE437 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 4 |
| Details | SITE: Important for catalytic activity |
| Chain | Residue | Details |
| A | HIS26 | |
| A | HIS261 | |
| B | HIS26 | |
| B | HIS261 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000269|PubMed:18723842 |
| Chain | Residue | Details |
| A | LYS46 | |
| B | LYS46 |
