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 |