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1USW

Crystal Structure of Ferulic Acid Esterase from Aspergillus niger

Functional Information from GO Data
ChainGOidnamespacecontents
A0000272biological_processpolysaccharide catabolic process
A0005576cellular_componentextracellular region
A0006629biological_processlipid metabolic process
A0016787molecular_functionhydrolase activity
A0016998biological_processcell wall macromolecule catabolic process
A0030245biological_processcellulose catabolic process
A0030248molecular_functioncellulose binding
A0030600molecular_functionferuloyl esterase activity
A0044347biological_processcell wall polysaccharide catabolic process
A0045490biological_processpectin catabolic process
A0045493biological_processxylan catabolic process
A0052689molecular_functioncarboxylic ester hydrolase activity
Functional Information from PROSITE/UniProt
site_idPS00120
Number of Residues10
DetailsLIPASE_SER Lipases, serine active site. LTVTGHSLGA
ChainResidueDetails
ALEU127-ALA136

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000269|PubMed:15081808
ChainResidueDetails
ASER133

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Charge relay system => ECO:0000305|PubMed:15103133
ChainResidueDetails
AASP194
AHIS247

site_idSWS_FT_FI3
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:16128806
ChainResidueDetails
AASP77
ATYR80
AHIS247

site_idSWS_FT_FI4
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:17027758
ChainResidueDetails
AASN79

237423

PDB entries from 2025-06-11

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