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7P75

Re-engineered 2-deoxy-D-ribose-5-phosphate aldolase catalysing asymmetric Michael addition reactions in substrate-free state

This is a non-PDB format compatible entry.
Functional Information from GO Data
ChainGOidnamespacecontents
AAA0003824molecular_functioncatalytic activity
AAA0004139molecular_functiondeoxyribose-phosphate aldolase activity
AAA0005737cellular_componentcytoplasm
AAA0005829cellular_componentcytosol
AAA0006018biological_process2-deoxyribose 1-phosphate catabolic process
AAA0006974biological_processDNA damage response
AAA0009264biological_processdeoxyribonucleotide catabolic process
AAA0015949biological_processnucleobase-containing small molecule interconversion
AAA0016020cellular_componentmembrane
AAA0016052biological_processcarbohydrate catabolic process
AAA0016829molecular_functionlyase activity
AAA0046386biological_processdeoxyribose phosphate catabolic process
BBB0003824molecular_functioncatalytic activity
BBB0004139molecular_functiondeoxyribose-phosphate aldolase activity
BBB0005737cellular_componentcytoplasm
BBB0005829cellular_componentcytosol
BBB0006018biological_process2-deoxyribose 1-phosphate catabolic process
BBB0006974biological_processDNA damage response
BBB0009264biological_processdeoxyribonucleotide catabolic process
BBB0015949biological_processnucleobase-containing small molecule interconversion
BBB0016020cellular_componentmembrane
BBB0016052biological_processcarbohydrate catabolic process
BBB0016829molecular_functionlyase activity
BBB0046386biological_processdeoxyribose phosphate catabolic process
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_00592, ECO:0000305|PubMed:11598300
ChainResidueDetails
AAAASP102
BBBASP102

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Schiff-base intermediate with acetaldehyde => ECO:0000255|HAMAP-Rule:MF_00592, ECO:0000269|PubMed:11598300, ECO:0000305|PubMed:15476818
ChainResidueDetails
AAALYS167
BBBLYS167

site_idSWS_FT_FI3
Number of Residues2
DetailsACT_SITE: Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_00592, ECO:0000305|PubMed:11598300, ECO:0000305|PubMed:15476818
ChainResidueDetails
AAALYS201
BBBLYS201

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:18723842
ChainResidueDetails
AAALYS167
BBBLYS167

Catalytic Information from CSA
site_idMCSA1
Number of Residues3
DetailsM-CSA 613
ChainResidueDetails
AAAASP102increase nucleophilicity, proton acceptor, proton donor, proton relay
AAALYS167covalently attached, electron pair acceptor, electron pair donor, nucleofuge, nucleophile, proton acceptor, proton donor
AAALYS201increase nucleophilicity, proton acceptor, proton donor, proton relay

site_idMCSA2
Number of Residues3
DetailsM-CSA 613
ChainResidueDetails
BBBASP102increase nucleophilicity, proton acceptor, proton donor, proton relay
BBBLYS167covalently attached, electron pair acceptor, electron pair donor, nucleofuge, nucleophile, proton acceptor, proton donor
BBBLYS201increase nucleophilicity, proton acceptor, proton donor, proton relay

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PDB entries from 2024-10-02

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