1USW

Crystal Structure of Ferulic Acid Esterase from Aspergillus niger

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000272	biological_process	polysaccharide catabolic process
A	0005576	cellular_component	extracellular region
A	0006629	biological_process	lipid metabolic process
A	0016787	molecular_function	hydrolase activity
A	0016998	biological_process	cell wall macromolecule catabolic process
A	0030245	biological_process	cellulose catabolic process
A	0030248	molecular_function	cellulose binding
A	0030600	molecular_function	feruloyl esterase activity
A	0045490	biological_process	pectin catabolic process
A	0045493	biological_process	xylan catabolic process
A	0052689	molecular_function	carboxylic ester hydrolase activity

Functional Information from PROSITE/UniProt

site_id	PS00120
Number of Residues	10
Details	LIPASE_SER Lipases, serine active site. LTVTGHSLGA

Chain	Residue	Details
A	LEU127-ALA136

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	Active site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"15081808","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	2
Details	Active site: {"description":"Charge relay system","evidences":[{"source":"PubMed","id":"15103133","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	3
Details	Binding site: {"evidences":[{"source":"PubMed","id":"16128806","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI4
Number of Residues	1
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"17027758","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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