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2OBD

Crystal Structure of Cholesteryl Ester Transfer Protein

Functional Information from GO Data
ChainGOidnamespacecontents
A0005548molecular_functionphospholipid transporter activity
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0006641biological_processtriglyceride metabolic process
A0006869biological_processlipid transport
A0008203biological_processcholesterol metabolic process
A0008289molecular_functionlipid binding
A0010745biological_processnegative regulation of macrophage derived foam cell differentiation
A0010874biological_processregulation of cholesterol efflux
A0015485molecular_functioncholesterol binding
A0015914biological_processphospholipid transport
A0017129molecular_functiontriglyceride binding
A0030301biological_processcholesterol transport
A0031210molecular_functionphosphatidylcholine binding
A0031982cellular_componentvesicle
A0032376biological_processpositive regulation of cholesterol transport
A0034197biological_processtriglyceride transport
A0034364cellular_componenthigh-density lipoprotein particle
A0034372biological_processvery-low-density lipoprotein particle remodeling
A0034374biological_processlow-density lipoprotein particle remodeling
A0034375biological_processhigh-density lipoprotein particle remodeling
A0042632biological_processcholesterol homeostasis
A0043691biological_processreverse cholesterol transport
A0046470biological_processphosphatidylcholine metabolic process
A0055088biological_processlipid homeostasis
A0055091biological_processphospholipid homeostasis
A0070062cellular_componentextracellular exosome
A0070328biological_processtriglyceride homeostasis
A0120020molecular_functioncholesterol transfer activity
A2001140biological_processpositive regulation of phospholipid transport
Functional Information from PROSITE/UniProt
site_idPS00400
Number of Residues33
DetailsLBP_BPI_CETP LBP / BPI / CETP family signature. AGIvcRITkpaLlvlnhEtakvIQtafqrasyP
ChainResidueDetails
AALA9-PRO41

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:19139490
ChainResidueDetails
AASP88

site_idSWS_FT_FI2
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952
ChainResidueDetails
AASP240
AASP341

site_idSWS_FT_FI3
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN396

223166

PDB entries from 2024-07-31

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