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 |