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9EVV

His579Leu variant of L-arabinonate dehydratase co-crystallized with 2-oxobutyrate

Functional Information from GO Data
ChainGOidnamespacecontents
A0008869molecular_functiongalactonate dehydratase activity
A0016829molecular_functionlyase activity
A0019568biological_processarabinose catabolic process
A0046872molecular_functionmetal ion binding
A0047818molecular_functionD-fuconate dehydratase activity
A0050020molecular_functionL-arabinonate dehydratase activity
A0051537molecular_function2 iron, 2 sulfur cluster binding
B0008869molecular_functiongalactonate dehydratase activity
B0016829molecular_functionlyase activity
B0019568biological_processarabinose catabolic process
B0046872molecular_functionmetal ion binding
B0047818molecular_functionD-fuconate dehydratase activity
B0050020molecular_functionL-arabinonate dehydratase activity
B0051537molecular_function2 iron, 2 sulfur cluster binding
C0008869molecular_functiongalactonate dehydratase activity
C0016829molecular_functionlyase activity
C0019568biological_processarabinose catabolic process
C0046872molecular_functionmetal ion binding
C0047818molecular_functionD-fuconate dehydratase activity
C0050020molecular_functionL-arabinonate dehydratase activity
C0051537molecular_function2 iron, 2 sulfur cluster binding
D0008869molecular_functiongalactonate dehydratase activity
D0016829molecular_functionlyase activity
D0019568biological_processarabinose catabolic process
D0046872molecular_functionmetal ion binding
D0047818molecular_functionD-fuconate dehydratase activity
D0050020molecular_functionL-arabinonate dehydratase activity
D0051537molecular_function2 iron, 2 sulfur cluster binding
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues24
DetailsBINDING: BINDING => ECO:0000269|PubMed:28574691
ChainResidueDetails
ACYS59
BASP128
BCYS200
BGLU453
CCYS59
CGLU91
CCYS127
CASP128
CCYS200
CGLU453
DCYS59
AGLU91
DGLU91
DCYS127
DASP128
DCYS200
DGLU453
ACYS127
AASP128
ACYS200
AGLU453
BCYS59
BGLU91
BCYS127

227344

PDB entries from 2024-11-13

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