3R12
Crystal structure of a Deoxyribose-phosphate aldolase (TM_1559) from THERMOTOGA MARITIMA at 1.75 A resolution
Replaces: 1O0YFunctional 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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE CIT A 249 |
| Chain | Residue |
| A | LYS41 |
| A | THR232 |
| A | SER233 |
| A | PGO250 |
| A | HOH287 |
| A | HOH294 |
| A | HOH311 |
| A | HOH313 |
| A | LYS179 |
| A | SER181 |
| A | THR182 |
| A | GLY183 |
| A | PHE184 |
| A | SER210 |
| A | GLY211 |
| A | ARG214 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE PGO A 250 |
| Chain | Residue |
| A | LYS41 |
| A | SER233 |
| A | CIT249 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL A 251 |
| Chain | Residue |
| A | HIS-1 |
| A | GLU129 |
| A | TRP130 |
| A | GLU131 |
| A | TYR132 |
| site_id | AC4 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE CIT B 249 |
| Chain | Residue |
| B | LYS179 |
| B | SER181 |
| B | THR182 |
| B | GLY183 |
| B | PHE184 |
| B | SER210 |
| B | GLY211 |
| B | ARG214 |
| B | SER233 |
| B | HOH288 |
| B | HOH300 |
| B | HOH309 |
| B | HOH402 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_00114 |
| Chain | Residue | Details |
| A | ASP117 | |
| A | LYS208 | |
| B | ASP117 | |
| B | LYS208 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | ACT_SITE: Schiff-base intermediate with acetaldehyde => ECO:0000255|HAMAP-Rule:MF_00114 |
| Chain | Residue | Details |
| A | LYS179 | |
| B | LYS179 |
