2FJK
Crystal structure of Fructose-1,6-Bisphosphate Aldolase in Thermus caldophilus
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004332 | molecular_function | fructose-bisphosphate aldolase activity |
| A | 0005975 | biological_process | carbohydrate metabolic process |
| A | 0006096 | biological_process | glycolytic process |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0016829 | molecular_function | lyase activity |
| A | 0016832 | molecular_function | aldehyde-lyase activity |
| A | 0030388 | biological_process | fructose 1,6-bisphosphate metabolic process |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0004332 | molecular_function | fructose-bisphosphate aldolase activity |
| B | 0005975 | biological_process | carbohydrate metabolic process |
| B | 0006096 | biological_process | glycolytic process |
| B | 0008270 | molecular_function | zinc ion binding |
| B | 0016829 | molecular_function | lyase activity |
| B | 0016832 | molecular_function | aldehyde-lyase activity |
| B | 0030388 | biological_process | fructose 1,6-bisphosphate metabolic process |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0004332 | molecular_function | fructose-bisphosphate aldolase activity |
| C | 0005975 | biological_process | carbohydrate metabolic process |
| C | 0006096 | biological_process | glycolytic process |
| C | 0008270 | molecular_function | zinc ion binding |
| C | 0016829 | molecular_function | lyase activity |
| C | 0016832 | molecular_function | aldehyde-lyase activity |
| C | 0030388 | biological_process | fructose 1,6-bisphosphate metabolic process |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0004332 | molecular_function | fructose-bisphosphate aldolase activity |
| D | 0005975 | biological_process | carbohydrate metabolic process |
| D | 0006096 | biological_process | glycolytic process |
| D | 0008270 | molecular_function | zinc ion binding |
| D | 0016829 | molecular_function | lyase activity |
| D | 0016832 | molecular_function | aldehyde-lyase activity |
| D | 0030388 | biological_process | fructose 1,6-bisphosphate metabolic process |
| D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE 13P A 1063 |
| Chain | Residue |
| A | ASP80 |
| A | ASN251 |
| A | ASP253 |
| A | THR254 |
| A | HIS81 |
| A | HIS178 |
| A | GLY179 |
| A | LYS182 |
| A | HIS208 |
| A | GLY209 |
| A | ALA210 |
| A | SER211 |
| site_id | AC2 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE 13P B 1073 |
| Chain | Residue |
| B | ASN23 |
| B | ASP80 |
| B | HIS81 |
| B | HIS178 |
| B | GLY179 |
| B | LYS182 |
| B | HIS208 |
| B | GLY209 |
| B | ALA210 |
| B | SER211 |
| B | ASN251 |
| B | ASP253 |
| B | THR254 |
| B | HOH1086 |
| site_id | AC3 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE 13P C 1083 |
| Chain | Residue |
| C | ASP80 |
| C | HIS81 |
| C | HIS178 |
| C | GLY179 |
| C | LYS182 |
| C | HIS208 |
| C | GLY209 |
| C | ALA210 |
| C | SER211 |
| C | ASN251 |
| C | ASP253 |
| C | THR254 |
| C | HOH1130 |
| site_id | AC4 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE 13P D 1093 |
| Chain | Residue |
| D | ASP80 |
| D | HIS81 |
| D | HIS178 |
| D | LYS182 |
| D | HIS208 |
| D | GLY209 |
| D | ALA210 |
| D | SER211 |
| D | ASN251 |
| D | THR252 |
| D | ASP253 |
| D | THR254 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton donor => ECO:0000250 |
| Chain | Residue | Details |
| A | ASP80 | |
| B | ASP80 | |
| C | ASP80 | |
| D | ASP80 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 36 |
| Details | BINDING: BINDING => ECO:0000250 |
| Chain | Residue | Details |
| A | SER49 | |
| B | SER49 | |
| B | HIS81 | |
| B | ASP102 | |
| B | GLU132 | |
| B | HIS178 | |
| B | GLY179 | |
| B | HIS208 | |
| B | GLY209 | |
| B | ASN251 | |
| C | SER49 | |
| A | HIS81 | |
| C | HIS81 | |
| C | ASP102 | |
| C | GLU132 | |
| C | HIS178 | |
| C | GLY179 | |
| C | HIS208 | |
| C | GLY209 | |
| C | ASN251 | |
| D | SER49 | |
| D | HIS81 | |
| A | ASP102 | |
| D | ASP102 | |
| D | GLU132 | |
| D | HIS178 | |
| D | GLY179 | |
| D | HIS208 | |
| D | GLY209 | |
| D | ASN251 | |
| A | GLU132 | |
| A | HIS178 | |
| A | GLY179 | |
| A | HIS208 | |
| A | GLY209 | |
| A | ASN251 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1b57 |
| Chain | Residue | Details |
| A | ASP80 | |
| A | ASN251 | |
| A | GLU140 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1b57 |
| Chain | Residue | Details |
| B | ASP80 | |
| B | ASN251 | |
| B | GLU147 |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1b57 |
| Chain | Residue | Details |
| C | ASP80 | |
| C | ASN251 | |
| C | GLU140 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1b57 |
| Chain | Residue | Details |
| D | ASP80 | |
| D | ASN251 |
