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8GYX

Cryo-EM structure of human CEPT1

Functional Information from GO Data
ChainGOidnamespacecontents
A0004142molecular_functiondiacylglycerol cholinephosphotransferase activity
A0004307molecular_functionethanolaminephosphotransferase activity
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005783cellular_componentendoplasmic reticulum
A0005789cellular_componentendoplasmic reticulum membrane
A0005794cellular_componentGolgi apparatus
A0006629biological_processlipid metabolic process
A0006646biological_processphosphatidylethanolamine biosynthetic process
A0006656biological_processphosphatidylcholine biosynthetic process
A0006657biological_processCDP-choline pathway
A0008654biological_processphospholipid biosynthetic process
A0016020cellular_componentmembrane
A0016740molecular_functiontransferase activity
A0016780molecular_functionphosphotransferase activity, for other substituted phosphate groups
A0031965cellular_componentnuclear membrane
A0046872molecular_functionmetal ion binding
A0047359molecular_function1-alkenyl-2-acylglycerol choline phosphotransferase activity
B0004142molecular_functiondiacylglycerol cholinephosphotransferase activity
B0004307molecular_functionethanolaminephosphotransferase activity
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005783cellular_componentendoplasmic reticulum
B0005789cellular_componentendoplasmic reticulum membrane
B0005794cellular_componentGolgi apparatus
B0006629biological_processlipid metabolic process
B0006646biological_processphosphatidylethanolamine biosynthetic process
B0006656biological_processphosphatidylcholine biosynthetic process
B0006657biological_processCDP-choline pathway
B0008654biological_processphospholipid biosynthetic process
B0016020cellular_componentmembrane
B0016740molecular_functiontransferase activity
B0016780molecular_functionphosphotransferase activity, for other substituted phosphate groups
B0031965cellular_componentnuclear membrane
B0046872molecular_functionmetal ion binding
B0047359molecular_function1-alkenyl-2-acylglycerol choline phosphotransferase activity
Functional Information from PROSITE/UniProt
site_idPS00379
Number of Residues23
DetailsCDP_ALCOHOL_P_TRANSF CDP-alcohol phosphatidyltransferases signature. DGkqARrtnsssplGelfDhgcD
ChainResidueDetails
BASP136-ASP158

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues320
DetailsTRANSMEM: Helical => ECO:0000255
ChainResidueDetails
BLEU87-CYS107
APRO115-ILE135
ACYS186-LEU206
AGLY209-ILE229
AILE239-ILE259
AGLY283-ILE303
ACYS317-ALA337
ASER365-ILE385
BPRO115-ILE135
BCYS186-LEU206
BGLY209-ILE229
BILE239-ILE259
BGLY283-ILE303
BCYS317-ALA337
BSER365-ILE385
ALEU87-CYS107

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:Q4KLV1
ChainResidueDetails
BHIS155
AHIS155

site_idSWS_FT_FI3
Number of Residues12
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q4KLV1
ChainResidueDetails
BASN86
AARG141
AASP154
AASP158
BASP133
BASP136
BARG141
BASP154
BASP158
AASN86
AASP133
AASP136

site_idSWS_FT_FI4
Number of Residues2
DetailsSITE: Increases basicity of active site His => ECO:0000250|UniProtKB:Q4KLV1
ChainResidueDetails
BGLU151
AGLU151

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:23186163
ChainResidueDetails
BTHR40
ATHR40

site_idSWS_FT_FI6
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
BASN144
AASN144

219140

PDB entries from 2024-05-01

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