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5A7H

Comparison of the structure and activity of glycosylated and aglycosylated Human Carboxylesterase 1

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 PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE IOD A 1554
ChainResidue
ASER98
AILE108
ALEU110
ASER150
ATHR151
AHOH2047

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE IOD A 1555
ChainResidue
AGLN95
ALEU110

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE IOD A 1557
ChainResidue
APRO46
AALA48
AALA125
AHOH2061
AGLN45

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE IOD A 1558
ChainResidue
ASER75
AIOD1559

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE IOD A 1559
ChainResidue
ASER75
AASP182
AGLU183
AIOD1558

site_idAC6
Number of Residues1
DetailsBINDING SITE FOR RESIDUE IOD A 1560
ChainResidue
AMET326

Functional Information from PROSITE/UniProt
site_idPS00122
Number of Residues16
DetailsCARBOXYLESTERASE_B_1 Carboxylesterases type-B serine active site. FGGnpgsVtIfGeSAG
ChainResidueDetails
APHE208-GLY223

site_idPS00941
Number of Residues11
DetailsCARBOXYLESTERASE_B_2 Carboxylesterases type-B signature 2. EDCLYLNIYtP
ChainResidueDetails
AGLU114-PRO124

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Acyl-ester intermediate => ECO:0000255|PROSITE-ProRule:PRU10039, ECO:0000269|PubMed:12022871
ChainResidueDetails
ASER221

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Charge relay system => ECO:0000269|PubMed:12022871
ChainResidueDetails
AGLU354
AGLY468

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569
ChainResidueDetails
ALEU380

site_idSWS_FT_FI4
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12022871
ChainResidueDetails
AGLN79

237735

PDB entries from 2025-06-18

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