2D80
Crystal structure of PHB depolymerase from Penicillium funiculosum
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005576 | cellular_component | extracellular region |
A | 0006508 | biological_process | proteolysis |
A | 0006629 | biological_process | lipid metabolic process |
A | 0008236 | molecular_function | serine-type peptidase activity |
A | 0016042 | biological_process | lipid catabolic process |
A | 0016787 | molecular_function | hydrolase activity |
A | 0052689 | molecular_function | carboxylic ester hydrolase activity |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 3 |
Details | ACT_SITE: ACT_SITE => ECO:0000269|PubMed:16405909 |
Chain | Residue | Details |
A | SER39 | |
A | ASP121 | |
A | HIS155 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0007744|PDB:2D81 |
Chain | Residue | Details |
A | TRP307 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498, ECO:0000269|PubMed:16405909, ECO:0000269|PubMed:1929416, ECO:0007744|PDB:2D80, ECO:0007744|PDB:2D81 |
Chain | Residue | Details |
A | ASN144 |