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1LN3

Structure of Human Phosphatidylcholine Transfer Protein in Complex with Palmitoyl-Linoleoyl Phosphatidylcholine (Seleno-Met Protein)

Functional Information from GO Data
ChainGOidnamespacecontents
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006869biological_processlipid transport
A0008289molecular_functionlipid binding
A0008525molecular_functionphosphatidylcholine transporter activity
A0015914biological_processphospholipid transport
A0031210molecular_functionphosphatidylcholine binding
A0120163biological_processnegative regulation of cold-induced thermogenesis
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006869biological_processlipid transport
B0008289molecular_functionlipid binding
B0008525molecular_functionphosphatidylcholine transporter activity
B0015914biological_processphospholipid transport
B0031210molecular_functionphosphatidylcholine binding
B0120163biological_processnegative regulation of cold-induced thermogenesis
Functional Information from PDB Data
site_idAC1
Number of Residues20
DetailsBINDING SITE FOR RESIDUE CPL A 300
ChainResidue
ALEU33
ATYR116
AGLN157
ALEU159
AMSE173
ATYR175
ATRP190
AALA191
AVAL196
APHE199
ALEU200
AVAL34
AHOH2013
ATYR54
ALEU68
ATYR72
AARG78
ATRP101
AVAL103
ATYR114

site_idAC2
Number of Residues19
DetailsBINDING SITE FOR RESIDUE CPL B 301
ChainResidue
BLEU33
BILE41
BTYR54
BVAL56
BTYR72
BARG78
BTYR84
BTRP101
BVAL103
BTYR105
BTYR114
BTYR116
BTYR155
BGLN157
BLEU159
BMSE173
BTYR175
BVAL196
BPHE199

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

243083

PDB entries from 2025-10-15

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