6D33
Crystal structure of BH1352 2-deoxyribose-5-phosphate from Bacillus halodurans
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| 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 | 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 |
| 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 | 0016052 | biological_process | carbohydrate catabolic process |
| C | 0016829 | molecular_function | lyase activity |
| C | 0046386 | biological_process | deoxyribose phosphate catabolic process |
| 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 | 0016052 | biological_process | carbohydrate catabolic process |
| D | 0016829 | molecular_function | lyase activity |
| D | 0046386 | biological_process | deoxyribose phosphate catabolic process |
| E | 0004139 | molecular_function | deoxyribose-phosphate aldolase activity |
| E | 0005737 | cellular_component | cytoplasm |
| E | 0006018 | biological_process | 2-deoxyribose 1-phosphate catabolic process |
| E | 0009264 | biological_process | deoxyribonucleotide catabolic process |
| E | 0016052 | biological_process | carbohydrate catabolic process |
| E | 0016829 | molecular_function | lyase activity |
| E | 0046386 | biological_process | deoxyribose phosphate catabolic process |
| F | 0004139 | molecular_function | deoxyribose-phosphate aldolase activity |
| F | 0005737 | cellular_component | cytoplasm |
| F | 0006018 | biological_process | 2-deoxyribose 1-phosphate catabolic process |
| F | 0009264 | biological_process | deoxyribonucleotide catabolic process |
| F | 0016052 | biological_process | carbohydrate catabolic process |
| F | 0016829 | molecular_function | lyase activity |
| F | 0046386 | biological_process | deoxyribose phosphate catabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | binding site for residue GOL A 301 |
| Chain | Residue |
| A | GLN113 |
| A | LYS148 |
| C | VAL147 |
| C | LYS148 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | binding site for residue GOL A 302 |
| Chain | Residue |
| A | GLU144 |
| A | VAL176 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue TRS B 301 |
| Chain | Residue |
| E | VAL147 |
| E | LYS148 |
| B | GLN113 |
| B | LYS148 |
| B | GOL304 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | binding site for residue GOL B 302 |
| Chain | Residue |
| B | ALA141 |
| B | GLU144 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | binding site for residue GOL B 303 |
| Chain | Residue |
| B | ASP191 |
| B | ASP194 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | binding site for residue GOL B 304 |
| Chain | Residue |
| B | VAL147 |
| B | LYS148 |
| B | TRS301 |
| E | HOH408 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | binding site for residue GOL B 305 |
| Chain | Residue |
| A | GLU20 |
| B | GLN104 |
| B | GOL306 |
| site_id | AC8 |
| Number of Residues | 2 |
| Details | binding site for residue GOL B 306 |
| Chain | Residue |
| B | ASP102 |
| B | GOL305 |
| site_id | AC9 |
| Number of Residues | 13 |
| Details | binding site for residue TRS C 301 |
| Chain | Residue |
| A | GLY150 |
| A | ALA151 |
| A | ASP152 |
| A | ASN180 |
| A | LEU181 |
| A | HOH430 |
| C | GLY150 |
| C | ALA151 |
| C | ASP152 |
| C | ASN180 |
| C | HOH402 |
| C | HOH405 |
| C | HOH410 |
| site_id | AD1 |
| Number of Residues | 2 |
| Details | binding site for residue GOL C 302 |
| Chain | Residue |
| C | GLN113 |
| C | GLU120 |
| site_id | AD2 |
| Number of Residues | 14 |
| Details | binding site for residue TRS D 301 |
| Chain | Residue |
| D | GLY150 |
| D | ALA151 |
| D | ASP152 |
| D | ASN180 |
| D | HOH403 |
| D | HOH408 |
| D | HOH416 |
| D | HOH426 |
| F | GLY150 |
| F | ALA151 |
| F | ASP152 |
| F | ASN180 |
| F | LEU181 |
| F | HOH415 |
| site_id | AD3 |
| Number of Residues | 6 |
| Details | binding site for residue GOL D 302 |
| Chain | Residue |
| D | GLN113 |
| D | GLU120 |
| D | LYS148 |
| D | ALA149 |
| D | GOL303 |
| F | LYS148 |
| site_id | AD4 |
| Number of Residues | 5 |
| Details | binding site for residue GOL D 303 |
| Chain | Residue |
| D | VAL147 |
| D | LYS148 |
| D | GOL302 |
| F | GLU120 |
| F | LYS148 |
| site_id | AD5 |
| Number of Residues | 11 |
| Details | binding site for residue TRS E 301 |
| Chain | Residue |
| B | GLY150 |
| B | ALA151 |
| B | ASP152 |
| B | ASN180 |
| E | GLY150 |
| E | ALA151 |
| E | ASP152 |
| E | ASN180 |
| E | HOH405 |
| E | HOH406 |
| E | HOH407 |
| site_id | AD6 |
| Number of Residues | 4 |
| Details | binding site for residue GOL E 302 |
| Chain | Residue |
| E | GLU32 |
| E | GLN104 |
| E | GOL303 |
| F | GLU20 |
| site_id | AD7 |
| Number of Residues | 2 |
| Details | binding site for residue GOL E 303 |
| Chain | Residue |
| E | GOL302 |
| F | GLU20 |
| site_id | AD8 |
| Number of Residues | 1 |
| Details | binding site for residue GOL E 304 |
| Chain | Residue |
| E | GLU144 |
| site_id | AD9 |
| Number of Residues | 2 |
| Details | binding site for residue GOL F 301 |
| Chain | Residue |
| F | TYR105 |
| F | GLU144 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 12 |
| Details | Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_00114","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | Active site: {"description":"Schiff-base intermediate with acetaldehyde","evidences":[{"source":"HAMAP-Rule","id":"MF_00114","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |






