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5OYN

Crystal structure of D-xylonate dehydratase in holo-form

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0016829molecular_functionlyase activity
A0016836molecular_functionhydro-lyase activity
A0042732biological_processD-xylose metabolic process
A0042843biological_processD-xylose catabolic process
A0046872molecular_functionmetal ion binding
A0047929molecular_functiongluconate dehydratase activity
A0050401molecular_functionxylonate dehydratase activity
A0051536molecular_functioniron-sulfur cluster binding
A0051537molecular_function2 iron, 2 sulfur cluster binding
B0003824molecular_functioncatalytic activity
B0016829molecular_functionlyase activity
B0016836molecular_functionhydro-lyase activity
B0042732biological_processD-xylose metabolic process
B0042843biological_processD-xylose catabolic process
B0046872molecular_functionmetal ion binding
B0047929molecular_functiongluconate dehydratase activity
B0050401molecular_functionxylonate dehydratase activity
B0051536molecular_functioniron-sulfur cluster binding
B0051537molecular_function2 iron, 2 sulfur cluster binding
C0003824molecular_functioncatalytic activity
C0016829molecular_functionlyase activity
C0016836molecular_functionhydro-lyase activity
C0042732biological_processD-xylose metabolic process
C0042843biological_processD-xylose catabolic process
C0046872molecular_functionmetal ion binding
C0047929molecular_functiongluconate dehydratase activity
C0050401molecular_functionxylonate dehydratase activity
C0051536molecular_functioniron-sulfur cluster binding
C0051537molecular_function2 iron, 2 sulfur cluster binding
D0003824molecular_functioncatalytic activity
D0016829molecular_functionlyase activity
D0016836molecular_functionhydro-lyase activity
D0042732biological_processD-xylose metabolic process
D0042843biological_processD-xylose catabolic process
D0046872molecular_functionmetal ion binding
D0047929molecular_functiongluconate dehydratase activity
D0050401molecular_functionxylonate dehydratase activity
D0051536molecular_functioniron-sulfur cluster binding
D0051537molecular_function2 iron, 2 sulfur cluster binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue MG A 601
ChainResidue
AGLU92
AASP129
AKCX130
AGLU463
AHOH718

site_idAC2
Number of Residues5
Detailsbinding site for residue FES A 602
ChainResidue
BARG30
ACYS60
AASN93
ACYS128
ACYS201

site_idAC3
Number of Residues6
Detailsbinding site for residue MG B 601
ChainResidue
BGLU92
BASP129
BKCX130
BTHR206
BGLU463
BHOH714

site_idAC4
Number of Residues7
Detailsbinding site for residue FES B 602
ChainResidue
AARG30
BCYS60
BASN93
BCYS128
BASP129
BHIS200
BCYS201

site_idAC5
Number of Residues5
Detailsbinding site for residue MG C 601
ChainResidue
CGLU92
CASP129
CKCX130
CGLU463
CHOH726

site_idAC6
Number of Residues5
Detailsbinding site for residue FES C 602
ChainResidue
CCYS60
CCYS128
CASP129
CHIS200
CCYS201

site_idAC7
Number of Residues5
Detailsbinding site for residue MG D 601
ChainResidue
DGLU92
DASP129
DKCX130
DGLU463
DHOH711

site_idAC8
Number of Residues7
Detailsbinding site for residue FES D 602
ChainResidue
CARG30
DCYS60
DASN93
DCYS128
DASP129
DCYS201
DHOH764

Functional Information from PROSITE/UniProt
site_idPS00886
Number of Residues11
DetailsILVD_EDD_1 Dihydroxy-acid and 6-phosphogluconate dehydratases signature 1. CDKttPAgimA
ChainResidueDetails
ACYS128-ALA138

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues24
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"29339766","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

247947

PDB entries from 2026-01-21

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