6Z9H
Escherichia coli D-2-deoxyribose-5-phosphate aldolase - C47V/G204A/S239D 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 | 4 |
Details | binding site for residue EDO A 301 |
Chain | Residue |
A | LYS167 |
A | SER169 |
A | THR170 |
A | HOH586 |
site_id | AC2 |
Number of Residues | 6 |
Details | binding site for residue FMT A 302 |
Chain | Residue |
A | HOH625 |
A | LYS126 |
A | GLY162 |
A | HOH405 |
A | HOH448 |
A | HOH502 |
site_id | AC3 |
Number of Residues | 2 |
Details | binding site for residue MG B 302 |
Chain | Residue |
B | HOH444 |
B | HOH524 |
site_id | AC4 |
Number of Residues | 12 |
Details | binding site for Di-peptide EDO B 301 and LYS B 167 |
Chain | Residue |
B | ASP102 |
B | VAL138 |
B | ILE139 |
B | ILE140 |
B | ILE166 |
B | THR168 |
B | SER169 |
B | THR170 |
B | MET185 |
B | LYS201 |
B | ALA203 |
B | HOH554 |
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 |