6Z9J
Escherichia coli D-2-deoxyribose-5-phosphate aldolase - N21K mutant
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004139 | molecular_function | deoxyribose-phosphate aldolase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006018 | biological_process | 2-deoxyribose 1-phosphate catabolic process |
| A | 0006974 | biological_process | DNA damage response |
| A | 0009264 | biological_process | deoxyribonucleotide catabolic process |
| A | 0015949 | biological_process | nucleobase-containing small molecule interconversion |
| A | 0016020 | cellular_component | membrane |
| 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 | 0005829 | cellular_component | cytosol |
| B | 0006018 | biological_process | 2-deoxyribose 1-phosphate catabolic process |
| B | 0006974 | biological_process | DNA damage response |
| B | 0009264 | biological_process | deoxyribonucleotide catabolic process |
| B | 0015949 | biological_process | nucleobase-containing small molecule interconversion |
| B | 0016020 | cellular_component | membrane |
| 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 | 6 |
| Details | binding site for residue MG A 301 |
| Chain | Residue |
| A | HIS78 |
| A | HOH518 |
| A | HOH573 |
| B | HOH514 |
| B | HOH534 |
| B | HOH538 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | binding site for residue MG A 302 |
| Chain | Residue |
| A | HOH469 |
| A | HOH605 |
| A | HOH668 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | binding site for residue MG A 303 |
| Chain | Residue |
| A | HOH515 |
| A | HOH615 |
| A | HOH686 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | binding site for residue MG A 304 |
| Chain | Residue |
| A | PHE76 |
| A | HOH452 |
| A | HOH543 |
| B | HOH410 |
| B | HOH421 |
| B | HOH604 |
| B | HOH660 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | binding site for residue MG A 305 |
| Chain | Residue |
| A | HOH425 |
| A | HOH461 |
| A | HOH483 |
| A | HOH509 |
| B | HOH436 |
| B | HOH648 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | binding site for residue MG A 306 |
| Chain | Residue |
| A | ASP22 |
| A | HOH445 |
| B | HOH415 |
| B | HOH425 |
| B | HOH616 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | binding site for residue MG B 301 |
| Chain | Residue |
| B | ASP81 |
| B | HOH441 |
| B | HOH573 |
| B | HOH576 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | binding site for residue MG B 302 |
| Chain | Residue |
| A | HOH453 |
| A | HOH476 |
| A | HOH535 |
| B | HIS78 |
| B | HOH566 |
| B | HOH581 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | binding site for residue MG B 303 |
| Chain | Residue |
| A | HOH404 |
| A | HOH412 |
| A | HOH589 |
| A | HOH660 |
| B | PHE76 |
| B | HOH411 |
| B | HOH495 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_00592","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"11598300","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Schiff-base intermediate with acetaldehyde","evidences":[{"source":"HAMAP-Rule","id":"MF_00592","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"11598300","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15476818","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_00592","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"11598300","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"15476818","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"18723842","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
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 |
