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1KCM

Crystal Structure of Mouse PITP Alpha Void of Bound Phospholipid at 2.0 Angstroms Resolution

Functional Information from GO Data
ChainGOidnamespacecontents
A0000062molecular_functionfatty-acyl-CoA binding
A0005543molecular_functionphospholipid binding
A0005548molecular_functionphospholipid transporter activity
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006869biological_processlipid transport
A0007409biological_processaxonogenesis
A0008289molecular_functionlipid binding
A0008525molecular_functionphosphatidylcholine transporter activity
A0008526molecular_functionphosphatidylinositol transfer activity
A0015914biological_processphospholipid transport
A0016020cellular_componentmembrane
A0031210molecular_functionphosphatidylcholine binding
A0035091molecular_functionphosphatidylinositol binding
A0043209cellular_componentmyelin sheath
A0070540molecular_functionstearic acid binding
A0120009biological_processintermembrane lipid transfer
A0120019molecular_functionphosphatidylcholine transfer activity
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"Q00169","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q00169","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

247536

PDB entries from 2026-01-14

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