5A7H
Comparison of the structure and activity of glycosylated and aglycosylated Human Carboxylesterase 1
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004771 | molecular_function | sterol ester esterase activity |
A | 0005737 | cellular_component | cytoplasm |
A | 0005783 | cellular_component | endoplasmic reticulum |
A | 0005788 | cellular_component | endoplasmic reticulum lumen |
A | 0005811 | cellular_component | lipid droplet |
A | 0005829 | cellular_component | cytosol |
A | 0006629 | biological_process | lipid metabolic process |
A | 0006695 | biological_process | cholesterol biosynthetic process |
A | 0008203 | biological_process | cholesterol metabolic process |
A | 0009636 | biological_process | response to toxic substance |
A | 0010875 | biological_process | positive regulation of cholesterol efflux |
A | 0010887 | biological_process | negative regulation of cholesterol storage |
A | 0016042 | biological_process | lipid catabolic process |
A | 0016787 | molecular_function | hydrolase activity |
A | 0030855 | biological_process | epithelial cell differentiation |
A | 0042632 | biological_process | cholesterol homeostasis |
A | 0043691 | biological_process | reverse cholesterol transport |
A | 0047374 | molecular_function | methylumbelliferyl-acetate deacetylase activity |
A | 0051791 | biological_process | medium-chain fatty acid metabolic process |
A | 0052689 | molecular_function | carboxylic ester hydrolase activity |
A | 0070857 | biological_process | regulation of bile acid biosynthetic process |
A | 0071397 | biological_process | cellular response to cholesterol |
A | 0071404 | biological_process | cellular response to low-density lipoprotein particle stimulus |
A | 0090122 | biological_process | cholesterol ester hydrolysis involved in cholesterol transport |
A | 0090205 | biological_process | positive regulation of cholesterol metabolic process |
A | 0106435 | molecular_function | carboxylesterase activity |
A | 0120188 | biological_process | regulation of bile acid secretion |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE IOD A 1554 |
Chain | Residue |
A | SER98 |
A | ILE108 |
A | LEU110 |
A | SER150 |
A | THR151 |
A | HOH2047 |
site_id | AC2 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE IOD A 1555 |
Chain | Residue |
A | GLN95 |
A | LEU110 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE IOD A 1557 |
Chain | Residue |
A | PRO46 |
A | ALA48 |
A | ALA125 |
A | HOH2061 |
A | GLN45 |
site_id | AC4 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE IOD A 1558 |
Chain | Residue |
A | SER75 |
A | IOD1559 |
site_id | AC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE IOD A 1559 |
Chain | Residue |
A | SER75 |
A | ASP182 |
A | GLU183 |
A | IOD1558 |
site_id | AC6 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE IOD A 1560 |
Chain | Residue |
A | MET326 |
Functional Information from PROSITE/UniProt
site_id | PS00122 |
Number of Residues | 16 |
Details | CARBOXYLESTERASE_B_1 Carboxylesterases type-B serine active site. FGGnpgsVtIfGeSAG |
Chain | Residue | Details |
A | PHE208-GLY223 |
site_id | PS00941 |
Number of Residues | 11 |
Details | CARBOXYLESTERASE_B_2 Carboxylesterases type-B signature 2. EDCLYLNIYtP |
Chain | Residue | Details |
A | GLU114-PRO124 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | ACT_SITE: Acyl-ester intermediate => ECO:0000255|PROSITE-ProRule:PRU10039, ECO:0000269|PubMed:12022871 |
Chain | Residue | Details |
A | SER221 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | ACT_SITE: Charge relay system => ECO:0000269|PubMed:12022871 |
Chain | Residue | Details |
A | GLU354 | |
A | GLY468 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569 |
Chain | Residue | Details |
A | LEU380 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12022871 |
Chain | Residue | Details |
A | GLN79 |