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6Z9H

Escherichia coli D-2-deoxyribose-5-phosphate aldolase - C47V/G204A/S239D mutant

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 PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue EDO A 301
ChainResidue
ALYS167
ASER169
ATHR170
AHOH586

site_idAC2
Number of Residues6
Detailsbinding site for residue FMT A 302
ChainResidue
AHOH625
ALYS126
AGLY162
AHOH405
AHOH448
AHOH502

site_idAC3
Number of Residues2
Detailsbinding site for residue MG B 302
ChainResidue
BHOH444
BHOH524

site_idAC4
Number of Residues12
Detailsbinding site for Di-peptide EDO B 301 and LYS B 167
ChainResidue
BASP102
BVAL138
BILE139
BILE140
BILE166
BTHR168
BSER169
BTHR170
BMET185
BLYS201
BALA203
BHOH554

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
AASP102
BASP102

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
ALYS167
BLYS167

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
ALYS201
BLYS201

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:18723842
ChainResidueDetails
ALYS167
BLYS167

Catalytic Information from CSA
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
BASP102increase nucleophilicity, proton acceptor, proton donor, proton relay
BLYS167covalently attached, electron pair acceptor, electron pair donor, nucleofuge, nucleophile, proton acceptor, proton donor
BLYS201increase nucleophilicity, proton acceptor, proton donor, proton relay

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PDB entries from 2025-06-25

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