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9KWL

hCES1A contently binding with compound F-3 at the catalytic pocket.

This is a non-PDB format compatible entry.
Functional Information from GO Data
ChainGOidnamespacecontents
A0004771molecular_functionsterol ester esterase activity
A0005737cellular_componentcytoplasm
A0005783cellular_componentendoplasmic reticulum
A0005788cellular_componentendoplasmic reticulum lumen
A0005811cellular_componentlipid droplet
A0005829cellular_componentcytosol
A0006629biological_processlipid metabolic process
A0006695biological_processcholesterol biosynthetic process
A0008203biological_processcholesterol metabolic process
A0009636biological_processresponse to toxic substance
A0010875biological_processpositive regulation of cholesterol efflux
A0010887biological_processnegative regulation of cholesterol storage
A0016042biological_processlipid catabolic process
A0016787molecular_functionhydrolase activity
A0030855biological_processepithelial cell differentiation
A0042632biological_processcholesterol homeostasis
A0043691biological_processreverse cholesterol transport
A0047374molecular_functionmethylumbelliferyl-acetate deacetylase activity
A0051791biological_processmedium-chain fatty acid metabolic process
A0052689molecular_functioncarboxylic ester hydrolase activity
A0070857biological_processregulation of bile acid biosynthetic process
A0071397biological_processcellular response to cholesterol
A0071404biological_processcellular response to low-density lipoprotein particle stimulus
A0090122biological_processcholesterol ester hydrolysis involved in cholesterol transport
A0090205biological_processpositive regulation of cholesterol metabolic process
A0106435molecular_functioncarboxylesterase activity
A0120188biological_processregulation of bile acid secretion
Functional Information from PROSITE/UniProt
site_idPS00122
Number of Residues16
DetailsCARBOXYLESTERASE_B_1 Carboxylesterases type-B serine active site. FGGnpgsVtIfGeSAG
ChainResidueDetails
APHE191-GLY206

site_idPS00941
Number of Residues11
DetailsCARBOXYLESTERASE_B_2 Carboxylesterases type-B signature 2. EDCLYLNIYtP
ChainResidueDetails
AGLU97-PRO107

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Acyl-ester intermediate","evidences":[{"source":"PROSITE-ProRule","id":"PRU10039","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"12022871","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsActive site: {"description":"Charge relay system","evidences":[{"source":"PubMed","id":"12022871","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"12022871","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

238895

PDB entries from 2025-07-16

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