2YCE
Structure of an Archaeal fructose-1,6-bisphosphate aldolase with the catalytic Lys covalently bound to the carbinolamine intermediate of the substrate.
Replaces: 1W8RFunctional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004332 | molecular_function | fructose-bisphosphate aldolase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006096 | biological_process | glycolytic process |
| A | 0016829 | molecular_function | lyase activity |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004332 | molecular_function | fructose-bisphosphate aldolase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006096 | biological_process | glycolytic process |
| B | 0016829 | molecular_function | lyase activity |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0004332 | molecular_function | fructose-bisphosphate aldolase activity |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0006096 | biological_process | glycolytic process |
| C | 0016829 | molecular_function | lyase activity |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0004332 | molecular_function | fructose-bisphosphate aldolase activity |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0006096 | biological_process | glycolytic process |
| D | 0016829 | molecular_function | lyase activity |
| E | 0003824 | molecular_function | catalytic activity |
| E | 0004332 | molecular_function | fructose-bisphosphate aldolase activity |
| E | 0005737 | cellular_component | cytoplasm |
| E | 0006096 | biological_process | glycolytic process |
| E | 0016829 | molecular_function | lyase activity |
| F | 0003824 | molecular_function | catalytic activity |
| F | 0004332 | molecular_function | fructose-bisphosphate aldolase activity |
| F | 0005737 | cellular_component | cytoplasm |
| F | 0006096 | biological_process | glycolytic process |
| F | 0016829 | molecular_function | lyase activity |
| G | 0003824 | molecular_function | catalytic activity |
| G | 0004332 | molecular_function | fructose-bisphosphate aldolase activity |
| G | 0005737 | cellular_component | cytoplasm |
| G | 0006096 | biological_process | glycolytic process |
| G | 0016829 | molecular_function | lyase activity |
| H | 0003824 | molecular_function | catalytic activity |
| H | 0004332 | molecular_function | fructose-bisphosphate aldolase activity |
| H | 0005737 | cellular_component | cytoplasm |
| H | 0006096 | biological_process | glycolytic process |
| H | 0016829 | molecular_function | lyase activity |
| I | 0003824 | molecular_function | catalytic activity |
| I | 0004332 | molecular_function | fructose-bisphosphate aldolase activity |
| I | 0005737 | cellular_component | cytoplasm |
| I | 0006096 | biological_process | glycolytic process |
| I | 0016829 | molecular_function | lyase activity |
| J | 0003824 | molecular_function | catalytic activity |
| J | 0004332 | molecular_function | fructose-bisphosphate aldolase activity |
| J | 0005737 | cellular_component | cytoplasm |
| J | 0006096 | biological_process | glycolytic process |
| J | 0016829 | molecular_function | lyase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE M2P A 270 |
| Chain | Residue |
| A | ALA22 |
| A | GLY203 |
| A | GLY204 |
| A | ALA229 |
| A | VAL230 |
| A | GLY231 |
| A | ARG232 |
| A | HOH2078 |
| A | HOH2079 |
| A | HOH2154 |
| A | HOH2155 |
| A | ASP24 |
| A | HOH2156 |
| A | HOH2157 |
| A | HOH2158 |
| A | HIS25 |
| A | HIS29 |
| A | TRP144 |
| A | ARG148 |
| A | LYS177 |
| A | LYS179 |
| A | SER202 |
| site_id | AC2 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE M2P B 270 |
| Chain | Residue |
| B | ALA22 |
| B | ASP24 |
| B | HIS25 |
| B | HIS29 |
| B | TRP144 |
| B | ARG148 |
| B | LYS177 |
| B | LYS179 |
| B | SER202 |
| B | GLY203 |
| B | GLY204 |
| B | ALA229 |
| B | VAL230 |
| B | GLY231 |
| B | ARG232 |
| B | HOH2084 |
| B | HOH2085 |
| B | HOH2170 |
| B | HOH2171 |
| B | HOH2172 |
| B | HOH2173 |
| site_id | AC3 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE M2P C 270 |
| Chain | Residue |
| C | ALA22 |
| C | ASP24 |
| C | HIS25 |
| C | HIS29 |
| C | TRP144 |
| C | ARG148 |
| C | LYS177 |
| C | LYS179 |
| C | SER202 |
| C | GLY203 |
| C | GLY204 |
| C | ALA229 |
| C | VAL230 |
| C | GLY231 |
| C | ARG232 |
| C | HOH2077 |
| C | HOH2133 |
| C | HOH2134 |
| C | HOH2135 |
| C | HOH2136 |
| site_id | AC4 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE M2P D 270 |
| Chain | Residue |
| D | ALA22 |
| D | ASP24 |
| D | HIS25 |
| D | HIS29 |
| D | TRP144 |
| D | ARG148 |
| D | LYS177 |
| D | LYS179 |
| D | SER202 |
| D | GLY203 |
| D | GLY204 |
| D | ALA229 |
| D | VAL230 |
| D | GLY231 |
| D | ARG232 |
| D | HOH2070 |
| D | HOH2071 |
| D | HOH2124 |
| D | HOH2125 |
| D | HOH2126 |
| site_id | AC5 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE M2P E 270 |
| Chain | Residue |
| E | HOH2093 |
| E | HOH2170 |
| E | HOH2171 |
| E | HOH2173 |
| E | ALA22 |
| E | ASP24 |
| E | HIS25 |
| E | HIS29 |
| E | TRP144 |
| E | ARG148 |
| E | LYS177 |
| E | LYS179 |
| E | SER202 |
| E | GLY203 |
| E | GLY204 |
| E | ALA229 |
| E | VAL230 |
| E | GLY231 |
| E | ARG232 |
| E | HOH2092 |
| site_id | AC6 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE M2P F 270 |
| Chain | Residue |
| F | ALA22 |
| F | ASP24 |
| F | HIS25 |
| F | HIS29 |
| F | TRP144 |
| F | PHE146 |
| F | ARG148 |
| F | LYS177 |
| F | LYS179 |
| F | SER202 |
| F | GLY203 |
| F | GLY204 |
| F | ALA229 |
| F | VAL230 |
| F | GLY231 |
| F | ARG232 |
| F | HOH2062 |
| F | HOH2063 |
| F | HOH2120 |
| F | HOH2121 |
| F | HOH2122 |
| site_id | AC7 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE M2P G 270 |
| Chain | Residue |
| G | ALA22 |
| G | ASP24 |
| G | HIS25 |
| G | HIS29 |
| G | TRP144 |
| G | PHE146 |
| G | ARG148 |
| G | LYS177 |
| G | LYS179 |
| G | SER202 |
| G | GLY203 |
| G | GLY204 |
| G | ALA229 |
| G | VAL230 |
| G | GLY231 |
| G | ARG232 |
| G | HOH2080 |
| G | HOH2081 |
| G | HOH2145 |
| G | HOH2146 |
| G | HOH2147 |
| G | HOH2148 |
| site_id | AC8 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE M2P H 270 |
| Chain | Residue |
| H | ALA22 |
| H | ASP24 |
| H | HIS25 |
| H | HIS29 |
| H | TRP144 |
| H | ARG148 |
| H | LYS177 |
| H | LYS179 |
| H | SER202 |
| H | GLY203 |
| H | GLY204 |
| H | ALA229 |
| H | VAL230 |
| H | GLY231 |
| H | ARG232 |
| H | HOH2073 |
| H | HOH2074 |
| H | HOH2147 |
| H | HOH2148 |
| H | HOH2149 |
| H | HOH2150 |
| site_id | AC9 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE M2P I 270 |
| Chain | Residue |
| I | ALA22 |
| I | ASP24 |
| I | HIS25 |
| I | HIS29 |
| I | TRP144 |
| I | ARG148 |
| I | LYS177 |
| I | LYS179 |
| I | SER202 |
| I | GLY203 |
| I | GLY204 |
| I | ALA229 |
| I | VAL230 |
| I | GLY231 |
| I | ARG232 |
| I | HOH2084 |
| I | HOH2085 |
| I | HOH2151 |
| I | HOH2156 |
| I | HOH2157 |
| I | HOH2158 |
| site_id | BC1 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE M2P J 270 |
| Chain | Residue |
| J | ASP24 |
| J | HIS25 |
| J | HIS29 |
| J | TRP144 |
| J | ARG148 |
| J | LYS177 |
| J | LYS179 |
| J | SER202 |
| J | GLY203 |
| J | GLY204 |
| J | ALA229 |
| J | VAL230 |
| J | GLY231 |
| J | ARG232 |
| J | HOH2087 |
| J | HOH2089 |
| J | HOH2171 |
| J | HOH2172 |
| J | HOH2173 |
| J | HOH2174 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 10 |
| Details | ACT_SITE: Proton donor |
| Chain | Residue | Details |
| A | PHE146 | |
| J | PHE146 | |
| B | PHE146 | |
| C | PHE146 | |
| D | PHE146 | |
| E | PHE146 | |
| F | PHE146 | |
| G | PHE146 | |
| H | PHE146 | |
| I | PHE146 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 10 |
| Details | ACT_SITE: Schiff-base intermediate with dihydroxyacetone-P |
| Chain | Residue | Details |
| A | LYS177 | |
| J | LYS177 | |
| B | LYS177 | |
| C | LYS177 | |
| D | LYS177 | |
| E | LYS177 | |
| F | LYS177 | |
| G | LYS177 | |
| H | LYS177 | |
| I | LYS177 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 80 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | ASP24 | |
| B | HIS29 | |
| B | ASP33 | |
| B | TRP144 | |
| B | ARG148 | |
| B | LYS177 | |
| B | SER202 | |
| B | GLY231 | |
| C | ASP24 | |
| C | HIS29 | |
| C | ASP33 | |
| A | HIS29 | |
| C | TRP144 | |
| C | ARG148 | |
| C | LYS177 | |
| C | SER202 | |
| C | GLY231 | |
| D | ASP24 | |
| D | HIS29 | |
| D | ASP33 | |
| D | TRP144 | |
| D | ARG148 | |
| A | ASP33 | |
| D | LYS177 | |
| D | SER202 | |
| D | GLY231 | |
| E | ASP24 | |
| E | HIS29 | |
| E | ASP33 | |
| E | TRP144 | |
| E | ARG148 | |
| E | LYS177 | |
| E | SER202 | |
| A | TRP144 | |
| E | GLY231 | |
| F | ASP24 | |
| F | HIS29 | |
| F | ASP33 | |
| F | TRP144 | |
| F | ARG148 | |
| F | LYS177 | |
| F | SER202 | |
| F | GLY231 | |
| G | ASP24 | |
| A | ARG148 | |
| G | HIS29 | |
| G | ASP33 | |
| G | TRP144 | |
| G | ARG148 | |
| G | LYS177 | |
| G | SER202 | |
| G | GLY231 | |
| H | ASP24 | |
| H | HIS29 | |
| H | ASP33 | |
| A | LYS177 | |
| H | TRP144 | |
| H | ARG148 | |
| H | LYS177 | |
| H | SER202 | |
| H | GLY231 | |
| I | ASP24 | |
| I | HIS29 | |
| I | ASP33 | |
| I | TRP144 | |
| I | ARG148 | |
| A | SER202 | |
| I | LYS177 | |
| I | SER202 | |
| I | GLY231 | |
| J | ASP24 | |
| J | HIS29 | |
| J | ASP33 | |
| J | TRP144 | |
| J | ARG148 | |
| J | LYS177 | |
| J | SER202 | |
| A | GLY231 | |
| J | GLY231 | |
| B | ASP24 |
