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3S0K

Crystal Structure of Human Glycolipid Transfer Protein complexed with glucosylceramide containing oleoyl acyl chain (18:1)

Functional Information from GO Data
ChainGOidnamespacecontents
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006869biological_processlipid transport
A0008289molecular_functionlipid binding
A0017089molecular_functionglycolipid transfer activity
A0035627biological_processceramide transport
A0035902biological_processresponse to immobilization stress
A0042802molecular_functionidentical protein binding
A0046836biological_processglycolipid transport
A0051861molecular_functionglycolipid binding
A0120009biological_processintermembrane lipid transfer
A0120013molecular_functionlipid transfer activity
A1902387molecular_functionceramide 1-phosphate binding
A1902388molecular_functionceramide 1-phosphate transfer activity
A1902389biological_processceramide 1-phosphate transport
Functional Information from PDB Data
site_idAC1
Number of Residues24
DetailsBINDING SITE FOR RESIDUE 03F A 210
ChainResidue
ALEU30
ATRP96
AGLY100
APHE107
ALEU108
ALEU136
AHIS140
AALA151
ATYR207
AVAL209
AHOH215
APHE33
AHOH273
AHOH379
AHOH397
AHOH422
AHOH468
APHE34
ALEU37
APHE42
AILE45
AASP48
AASN52
ALEU92

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE NI A 240
ChainResidue
AHIS7
AGLU25
AHIS29
AHIS120

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:15329726, ECO:0007744|PDB:1SX6
ChainResidueDetails
AASP48
AHIS140
ATYR207

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: N-acetylalanine => ECO:0000250|UniProtKB:P68266
ChainResidueDetails
AALA2

226707

PDB entries from 2024-10-30

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