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1T27

THE STRUCTURE OF PITP COMPLEXED TO PHOSPHATIDYLCHOLINE

Replaces:  1FVZ
Functional Information from GO Data
ChainGOidnamespacecontents
A0000062molecular_functionfatty-acyl-CoA binding
A0005543molecular_functionphospholipid binding
A0005548molecular_functionphospholipid transporter activity
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0006869biological_processlipid transport
A0007409biological_processaxonogenesis
A0008289molecular_functionlipid binding
A0008525molecular_functionphosphatidylcholine transporter activity
A0008526molecular_functionphosphatidylinositol transfer activity
A0015914biological_processphospholipid transport
A0031210molecular_functionphosphatidylcholine binding
A0035091molecular_functionphosphatidylinositol binding
A0070540molecular_functionstearic acid binding
A0120009biological_processintermembrane lipid transfer
A0120019molecular_functionphosphatidylcholine transfer activity
Functional Information from PDB Data
site_idAC1
Number of Residues22
DetailsBINDING SITE FOR RESIDUE PCW A 501
ChainResidue
AGLN22
AASN101
ATYR103
AMET104
ALYS195
ATRP203
APHE213
AGLN217
AGLU218
APHE222
AMET267
ATYR63
AASP270
AHOH503
AHOH628
ALYS68
AALA77
ALEU82
AGLU86
AASN90
ATHR97
AILE99

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsBINDING: BINDING => ECO:0000305|PubMed:7568025
ChainResidueDetails
AHIS60

site_idSWS_FT_FI2
Number of Residues5
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q00169
ChainResidueDetails
AILE62
ALYS87
AALA91
AVAL98
ALEU196

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q00169
ChainResidueDetails
AGLN217

222415

PDB entries from 2024-07-10

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