9FD7
Re-engineered peroxygenase variant of 2-deoxy-D-ribose-5-phosphate aldolase in substrate-free state
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 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_00592, ECO:0000305|PubMed:11598300 |
| Chain | Residue | Details |
| A | ASP102 | |
| B | ASP102 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | ACT_SITE: Schiff-base intermediate with acetaldehyde => ECO:0000255|HAMAP-Rule:MF_00592, ECO:0000269|PubMed:11598300, ECO:0000305|PubMed:15476818 |
| Chain | Residue | Details |
| A | LYS167 | |
| B | LYS167 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_00592, ECO:0000305|PubMed:11598300, ECO:0000305|PubMed:15476818 |
| Chain | Residue | Details |
| A | LYS201 | |
| B | LYS201 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000269|PubMed:18723842 |
| Chain | Residue | Details |
| A | LYS167 | |
| B | LYS167 |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 3 |
| Details | M-CSA 613 |
| Chain | Residue | Details |
| A | ASP102 | increase nucleophilicity, proton acceptor, proton donor, proton relay |
| A | LYS167 | covalently attached, electron pair acceptor, electron pair donor, nucleofuge, nucleophile, proton acceptor, proton donor |
| A | LYS201 | increase nucleophilicity, proton acceptor, proton donor, proton relay |
| site_id | MCSA2 |
| Number of Residues | 3 |
| Details | M-CSA 613 |
| Chain | Residue | Details |
| B | ASP102 | increase nucleophilicity, proton acceptor, proton donor, proton relay |
| B | LYS167 | covalently attached, electron pair acceptor, electron pair donor, nucleofuge, nucleophile, proton acceptor, proton donor |
| B | LYS201 | increase nucleophilicity, proton acceptor, proton donor, proton relay |
