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 | 0050526 | molecular_function | poly(3-hydroxybutyrate) depolymerase activity |
| A | 0052689 | molecular_function | carboxylic ester hydrolase activity |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 3 |
| Details | Active site: {"evidences":[{"source":"PubMed","id":"16405909","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PDB","id":"2D81","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PROSITE-ProRule","id":"PRU00498","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"16405909","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"1929416","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2D80","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2D81","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
