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 | 0006018 | biological_process | 2-deoxyribose 1-phosphate catabolic process |
| A | 0009264 | biological_process | deoxyribonucleotide 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 | 0006018 | biological_process | 2-deoxyribose 1-phosphate catabolic process |
| B | 0009264 | biological_process | deoxyribonucleotide 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 | 0006018 | biological_process | 2-deoxyribose 1-phosphate catabolic process |
| C | 0009264 | biological_process | deoxyribonucleotide 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 | 0006018 | biological_process | 2-deoxyribose 1-phosphate catabolic process |
| D | 0009264 | biological_process | deoxyribonucleotide 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 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1p1x |
| Chain | Residue | Details |
| A | LYS180 | |
| A | LYS151 | |
| A | ASP89 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1p1x |
| Chain | Residue | Details |
| B | LYS180 | |
| B | LYS151 | |
| B | ASP89 |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1p1x |
| Chain | Residue | Details |
| C | LYS180 | |
| C | LYS151 | |
| C | ASP89 |
| site_id | CSA4 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1p1x |
| Chain | Residue | Details |
| D | LYS180 | |
| D | LYS151 | |
| D | ASP89 |
