Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

2HL6

Structure of homologously expressed Ferrulate esterase of Aspergillus niger in complex with CAPS

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
B0000272biological_processpolysaccharide catabolic process
B0005576cellular_componentextracellular region
B0006629biological_processlipid metabolic process
B0016787molecular_functionhydrolase activity
B0016998biological_processcell wall macromolecule catabolic process
B0030245biological_processcellulose catabolic process
B0030248molecular_functioncellulose binding
B0030600molecular_functionferuloyl esterase activity
B0044347biological_processcell wall polysaccharide catabolic process
B0045490biological_processpectin catabolic process
B0045493biological_processxylan catabolic process
B0052689molecular_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 Residues2
DetailsActive site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"15081808","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsActive site: {"description":"Charge relay system","evidences":[{"source":"PubMed","id":"15103133","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"16128806","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"17027758","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

239492

PDB entries from 2025-07-30

PDB statisticsPDBj update infoContact PDBjnumon