3R13
Crystal structure of a Deoxyribose-phosphate aldolase (TM_1559) from THERMOTOGA MARITIMA at 1.83 A resolution
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 | 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 | 0006018 | biological_process | 2-deoxyribose 1-phosphate catabolic process |
| 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 | 3 |
| Details | BINDING SITE FOR RESIDUE ACT A 301 |
| Chain | Residue |
| A | TYR13 |
| A | ARG14 |
| A | TYR17 |
| site_id | AC2 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE ACT A 302 |
| Chain | Residue |
| A | TYR157 |
| site_id | AC3 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE ACT A 306 |
| Chain | Residue |
| A | ILE200 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL A 307 |
| Chain | Residue |
| A | SER233 |
| A | SER234 |
| A | HOH320 |
| A | HOH400 |
| A | GLY212 |
| A | ILE213 |
| A | ARG214 |
| A | THR232 |
| site_id | AC5 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE ACT B 303 |
| Chain | Residue |
| B | CYS69 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE ACT B 304 |
| Chain | Residue |
| B | ARG14 |
| B | GLU161 |
| site_id | AC7 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE ACT B 305 |
| Chain | Residue |
| B | GLY187 |
| B | GLY188 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL B 308 |
| Chain | Residue |
| B | ILE213 |
| B | ARG214 |
| B | THR232 |
| B | SER233 |
| B | SER234 |
| B | HOH331 |
| B | HOH420 |
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 |
