1TCC
THE SEQUENCE, CRYSTAL STRUCTURE DETERMINATION AND REFINEMENT OF TWO CRYSTAL FORMS OF LIPASE B FROM CANDIDA ANTARCTICA
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004806 | molecular_function | triacylglycerol lipase activity |
A | 0006629 | biological_process | lipid metabolic process |
A | 0016042 | biological_process | lipid catabolic process |
A | 0016787 | molecular_function | hydrolase activity |
B | 0004806 | molecular_function | triacylglycerol lipase activity |
B | 0006629 | biological_process | lipid metabolic process |
B | 0016042 | biological_process | lipid catabolic process |
B | 0016787 | molecular_function | hydrolase activity |
Functional Information from PDB Data
site_id | CTA |
Number of Residues | 3 |
Details |
Chain | Residue |
A | SER105 |
A | ASP187 |
A | HIS224 |
site_id | CTB |
Number of Residues | 3 |
Details |
Chain | Residue |
B | SER105 |
B | ASP187 |
B | HIS224 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | Active site: {"evidences":[{"source":"PubMed","id":"8527460","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | Active site: {} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"8087556","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8527460","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |