Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

8Y2N

Cryo-EM structure of the apo Lac1-Lip1 complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0005515molecular_functionprotein binding
A0005783cellular_componentendoplasmic reticulum
A0005789cellular_componentendoplasmic reticulum membrane
A0006629biological_processlipid metabolic process
A0006665biological_processsphingolipid metabolic process
A0016020cellular_componentmembrane
A0016740molecular_functiontransferase activity
A0034399cellular_componentnuclear periphery
A0046513biological_processceramide biosynthetic process
A0050291molecular_functionsphingosine N-acyltransferase activity
A0061576cellular_componentacyl-CoA ceramide synthase complex
B0005515molecular_functionprotein binding
B0005635cellular_componentnuclear envelope
B0005783cellular_componentendoplasmic reticulum
B0005789cellular_componentendoplasmic reticulum membrane
B0006629biological_processlipid metabolic process
B0046513biological_processceramide biosynthetic process
B0050291molecular_functionsphingosine N-acyltransferase activity
B0061576cellular_componentacyl-CoA ceramide synthase complex
C0005515molecular_functionprotein binding
C0005783cellular_componentendoplasmic reticulum
C0005789cellular_componentendoplasmic reticulum membrane
C0006629biological_processlipid metabolic process
C0006665biological_processsphingolipid metabolic process
C0016020cellular_componentmembrane
C0016740molecular_functiontransferase activity
C0034399cellular_componentnuclear periphery
C0046513biological_processceramide biosynthetic process
C0050291molecular_functionsphingosine N-acyltransferase activity
C0061576cellular_componentacyl-CoA ceramide synthase complex
D0005515molecular_functionprotein binding
D0005635cellular_componentnuclear envelope
D0005783cellular_componentendoplasmic reticulum
D0005789cellular_componentendoplasmic reticulum membrane
D0006629biological_processlipid metabolic process
D0046513biological_processceramide biosynthetic process
D0050291molecular_functionsphingosine N-acyltransferase activity
D0061576cellular_componentacyl-CoA ceramide synthase complex
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues364
DetailsTransmembrane: {"description":"Helical","evidences":[{"source":"PubMed","id":"37953642","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"38964337","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"39528796","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues142
DetailsTopological domain: {"description":"Lumenal","evidences":[{"source":"PubMed","id":"37953642","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"38964337","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"39528796","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues66
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"37953642","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"38964337","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"39528796","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues434
DetailsDomain: {"description":"TLC","evidences":[{"source":"PROSITE-ProRule","id":"PRU00205","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"38964337","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"39528796","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"8QTR","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"38964337","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"39528796","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"8QTR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8Y2M","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"38964337","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"8Y2M","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues50
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"37953642","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"8IZD","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"39528796","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"8QTN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8QTR","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"38964337","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"39528796","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"8QTN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8QTR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8Y2M","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"38964337","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"39528796","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"8QTN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8Y2M","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"39528796","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"8QTN","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI14
Number of Residues38
DetailsTransmembrane: {"description":"Helical; Signal-anchor for type II membrane protein","evidences":[{"evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"38964337","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI15
Number of Residues218
DetailsTopological domain: {"description":"Lumenal","evidences":[{"source":"PubMed","id":"15692566","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"38964337","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

247536

PDB entries from 2026-01-14

PDB statisticsPDBj update infoContact PDBjnumon