1UB3
Crystal Structure of Tetrameric Structure of Aldolase from thermus thermophilus HB8
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003824 | molecular_function | catalytic activity |
A | 0004139 | molecular_function | deoxyribose-phosphate aldolase activity |
A | 0005737 | cellular_component | cytoplasm |
A | 0009264 | biological_process | deoxyribonucleotide catabolic process |
A | 0016052 | biological_process | carbohydrate catabolic process |
A | 0016829 | molecular_function | lyase activity |
A | 0046386 | biological_process | deoxyribose phosphate catabolic process |
B | 0003824 | molecular_function | catalytic activity |
B | 0004139 | molecular_function | deoxyribose-phosphate aldolase activity |
B | 0005737 | cellular_component | cytoplasm |
B | 0009264 | biological_process | deoxyribonucleotide catabolic process |
B | 0016052 | biological_process | carbohydrate catabolic process |
B | 0016829 | molecular_function | lyase activity |
B | 0046386 | biological_process | deoxyribose phosphate catabolic process |
C | 0003824 | molecular_function | catalytic activity |
C | 0004139 | molecular_function | deoxyribose-phosphate aldolase activity |
C | 0005737 | cellular_component | cytoplasm |
C | 0009264 | biological_process | deoxyribonucleotide catabolic process |
C | 0016052 | biological_process | carbohydrate catabolic process |
C | 0016829 | molecular_function | lyase activity |
C | 0046386 | biological_process | deoxyribose phosphate catabolic process |
D | 0003824 | molecular_function | catalytic activity |
D | 0004139 | molecular_function | deoxyribose-phosphate aldolase activity |
D | 0005737 | cellular_component | cytoplasm |
D | 0009264 | biological_process | deoxyribonucleotide catabolic process |
D | 0016052 | biological_process | carbohydrate catabolic process |
D | 0016829 | molecular_function | lyase activity |
D | 0046386 | biological_process | deoxyribose phosphate catabolic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE HPD A 801 |
Chain | Residue |
A | LEU12 |
A | ARG186 |
A | GLY203 |
A | THR204 |
A | SER205 |
A | HOH810 |
A | HOH815 |
A | HOH834 |
A | HOH853 |
A | HOH895 |
A | CYS37 |
A | VAL60 |
A | LYS151 |
A | THR154 |
A | GLY155 |
A | ALA182 |
A | GLY183 |
A | GLY184 |
site_id | AC2 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE HPD B 802 |
Chain | Residue |
B | LEU12 |
B | CYS37 |
B | VAL60 |
B | ASP89 |
B | LYS151 |
B | THR154 |
B | ALA182 |
B | GLY183 |
B | GLY184 |
B | ARG186 |
B | GLY203 |
B | THR204 |
B | SER205 |
B | HOH815 |
B | HOH828 |
B | HOH838 |
B | HOH881 |
site_id | AC3 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE HPD C 803 |
Chain | Residue |
C | LEU12 |
C | CYS37 |
C | VAL60 |
C | LYS151 |
C | THR154 |
C | GLY155 |
C | ALA182 |
C | GLY183 |
C | GLY184 |
C | ARG186 |
C | GLY203 |
C | THR204 |
C | SER205 |
C | HOH812 |
C | HOH814 |
C | HOH837 |
C | HOH858 |
C | HOH898 |
site_id | AC4 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE HPD D 804 |
Chain | Residue |
D | LEU12 |
D | CYS37 |
D | VAL60 |
D | ASP89 |
D | LYS151 |
D | THR154 |
D | ALA182 |
D | GLY183 |
D | GLY184 |
D | ARG186 |
D | GLY203 |
D | THR204 |
D | SER205 |
D | HOH812 |
D | HOH824 |
D | HOH832 |
D | HOH840 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 8 |
Details | ACT_SITE: Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_00114, ECO:0000305|PubMed:15388928 |
Chain | Residue | Details |
A | ASP89 | |
A | LYS180 | |
B | ASP89 | |
B | LYS180 | |
C | ASP89 | |
C | LYS180 | |
D | ASP89 | |
D | LYS180 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | ACT_SITE: Schiff-base intermediate with acetaldehyde => ECO:0000255|HAMAP-Rule:MF_00114, ECO:0000305|PubMed:15388928 |
Chain | Residue | Details |
A | LYS151 | |
B | LYS151 | |
C | LYS151 | |
D | LYS151 |