5EKY
Crystal structure of deoxyribose-phosphate aldolase from Escherichia coli (K58E-Y96W 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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 14 |
| Details | binding site for residue BU2 A 301 |
| Chain | Residue |
| A | THR18 |
| A | LYS201 |
| A | ALA203 |
| A | GLY204 |
| A | HOH434 |
| A | HOH483 |
| A | LEU20 |
| A | CYS47 |
| A | VAL73 |
| A | ASP102 |
| A | LYS167 |
| A | SER169 |
| A | THR170 |
| A | GLY171 |
| site_id | AC2 |
| Number of Residues | 14 |
| Details | binding site for residue EPE A 302 |
| Chain | Residue |
| A | TYR49 |
| A | PRO50 |
| A | ARG51 |
| A | PHE76 |
| A | HIS78 |
| A | GLU89 |
| A | ALA174 |
| A | HOH417 |
| A | HOH426 |
| A | HOH565 |
| A | HOH579 |
| A | HOH579 |
| A | HOH598 |
| A | HOH654 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| 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 | 1 |
| 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 | 1 |
| 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 | 1 |
| 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 |
