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3WMT

Crystal structure of feruloyl esterase B from Aspergillus oryzae

Functional Information from GO Data
ChainGOidnamespacecontents
A0005575cellular_componentcellular_component
A0005576cellular_componentextracellular region
A0030600molecular_functionferuloyl esterase activity
A0045493biological_processxylan catabolic process
A0046872molecular_functionmetal ion binding
A0052689molecular_functioncarboxylic ester hydrolase activity
B0005575cellular_componentcellular_component
B0005576cellular_componentextracellular region
B0030600molecular_functionferuloyl esterase activity
B0045493biological_processxylan catabolic process
B0046872molecular_functionmetal ion binding
B0052689molecular_functioncarboxylic ester hydrolase activity
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Acyl-ester intermediate => ECO:0000305|PubMed:25066066
ChainResidueDetails
ASER203
BSER203

site_idSWS_FT_FI2
Number of Residues4
DetailsACT_SITE: Charge relay system => ECO:0000305|PubMed:25066066
ChainResidueDetails
AASP417
AHIS457
BASP417
BHIS457

site_idSWS_FT_FI3
Number of Residues10
DetailsBINDING: BINDING => ECO:0000269|PubMed:25066066, ECO:0007744|PDB:3WMT
ChainResidueDetails
AASP272
BILE281
AASP275
AALA277
AASP279
AILE281
BASP272
BASP275
BALA277
BASP279

site_idSWS_FT_FI4
Number of Residues12
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN28
BASN195
BASN328
BASN506
AASN66
AASN113
AASN195
AASN328
AASN506
BASN28
BASN66
BASN113

site_idSWS_FT_FI5
Number of Residues10
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:25066066, ECO:0007744|PDB:3WMT
ChainResidueDetails
AASN49
BASN367
AASN95
AASN234
AASN298
AASN367
BASN49
BASN95
BASN234
BASN298

222036

PDB entries from 2024-07-03

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