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1P1X

Comparison of class I aldolase binding site architecture based on the crystal structure of 2-deoxyribose-5-phosphate aldolase determined at 0.99 Angstrom resolution

Functional Information from GO Data
ChainGOidnamespacecontents
A0004139molecular_functiondeoxyribose-phosphate aldolase activity
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006018biological_process2-deoxyribose 1-phosphate catabolic process
A0006974biological_processDNA damage response
A0009264biological_processdeoxyribonucleotide catabolic process
A0015949biological_processnucleobase-containing small molecule interconversion
A0016020cellular_componentmembrane
A0016052biological_processcarbohydrate catabolic process
A0016829molecular_functionlyase activity
A0046386biological_processdeoxyribose phosphate catabolic process
B0004139molecular_functiondeoxyribose-phosphate aldolase activity
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006018biological_process2-deoxyribose 1-phosphate catabolic process
B0006974biological_processDNA damage response
B0009264biological_processdeoxyribonucleotide catabolic process
B0015949biological_processnucleobase-containing small molecule interconversion
B0016020cellular_componentmembrane
B0016052biological_processcarbohydrate catabolic process
B0016829molecular_functionlyase activity
B0046386biological_processdeoxyribose phosphate catabolic process
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Proton donor/acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_00592","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"11598300","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsActive 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"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsActive 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"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"18723842","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues3
Detailsa catalytic site defined by CSA, PubMed 11598300
ChainResidueDetails
AASP102
ALYS201
ALYS167

site_idCSA2
Number of Residues3
Detailsa catalytic site defined by CSA, PubMed 11598300
ChainResidueDetails
BLYS1201
BASP1102
BLYS1167

site_idMCSA1
Number of Residues3
DetailsM-CSA 613
ChainResidueDetails
AASP102increase nucleophilicity, proton acceptor, proton donor, proton relay
ALYS167covalently attached, electron pair acceptor, electron pair donor, nucleofuge, nucleophile, proton acceptor, proton donor
ALYS201increase nucleophilicity, proton acceptor, proton donor, proton relay

site_idMCSA2
Number of Residues3
DetailsM-CSA 613
ChainResidueDetails
BASP1102increase nucleophilicity, proton acceptor, proton donor, proton relay
BLYS1167covalently attached, electron pair acceptor, electron pair donor, nucleofuge, nucleophile, proton acceptor, proton donor
BLYS1201increase nucleophilicity, proton acceptor, proton donor, proton relay

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PDB entries from 2026-01-21

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