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4GXG

Crystal structure of human GLTP bound with 12:0 monosulfatide (orthorhombic form; four subunits in asymmetric unit)

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
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006869biological_processlipid transport
B0008289molecular_functionlipid binding
B0017089molecular_functionglycolipid transfer activity
B0035627biological_processceramide transport
B0035902biological_processresponse to immobilization stress
B0042802molecular_functionidentical protein binding
B0046836biological_processglycolipid transport
B0051861molecular_functionglycolipid binding
B0120009biological_processintermembrane lipid transfer
B0120013molecular_functionlipid transfer activity
B1902387molecular_functionceramide 1-phosphate binding
B1902388molecular_functionceramide 1-phosphate transfer activity
B1902389biological_processceramide 1-phosphate transport
D0005515molecular_functionprotein binding
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0006869biological_processlipid transport
D0008289molecular_functionlipid binding
D0017089molecular_functionglycolipid transfer activity
D0035627biological_processceramide transport
D0035902biological_processresponse to immobilization stress
D0042802molecular_functionidentical protein binding
D0046836biological_processglycolipid transport
D0051861molecular_functionglycolipid binding
D0120009biological_processintermembrane lipid transfer
D0120013molecular_functionlipid transfer activity
D1902387molecular_functionceramide 1-phosphate binding
D1902388molecular_functionceramide 1-phosphate transfer activity
D1902389biological_processceramide 1-phosphate transport
E0005515molecular_functionprotein binding
E0005737cellular_componentcytoplasm
E0005829cellular_componentcytosol
E0006869biological_processlipid transport
E0008289molecular_functionlipid binding
E0017089molecular_functionglycolipid transfer activity
E0035627biological_processceramide transport
E0035902biological_processresponse to immobilization stress
E0042802molecular_functionidentical protein binding
E0046836biological_processglycolipid transport
E0051861molecular_functionglycolipid binding
E0120009biological_processintermembrane lipid transfer
E0120013molecular_functionlipid transfer activity
E1902387molecular_functionceramide 1-phosphate binding
E1902388molecular_functionceramide 1-phosphate transfer activity
E1902389biological_processceramide 1-phosphate transport
Functional Information from PDB Data
site_idAC1
Number of Residues18
DetailsBINDING SITE FOR RESIDUE EIS A 700
ChainResidue
AILE45
AHIS140
AILE147
APHE148
ATYR207
AHOH882
BVAL41
BTYR132
BPHE148
BEIS700
AASP48
AASN52
ALYS55
ALEU92
AALA93
ATRP96
APHE103
ALEU136

site_idAC2
Number of Residues19
DetailsBINDING SITE FOR RESIDUE EIS B 700
ChainResidue
AVAL41
APRO44
AHIS140
APHE148
AEIS700
BPHE42
BILE45
BASP48
BGLY51
BASN52
BLYS55
BLEU92
BALA93
BTRP96
BPHE103
BLEU136
BHIS140
BTYR207
BVAL209

site_idAC3
Number of Residues18
DetailsBINDING SITE FOR RESIDUE EIS D 700
ChainResidue
DPHE42
DILE45
DASP48
DILE49
DASN52
DLYS55
DALA93
DTRP96
DPHE103
DLEU136
DHIS140
DPHE148
DTYR207
EVAL41
EPRO44
EPHE148
EALA151
EEIS700

site_idAC4
Number of Residues18
DetailsBINDING SITE FOR RESIDUE EIS E 700
ChainResidue
DVAL41
DILE45
DPHE148
DEIS700
EILE45
EASP48
EGLY51
EASN52
ELYS55
ELEU92
EALA93
ETRP96
EPHE103
ELEU136
EHIS140
ETYR207
EHOH852
EHOH854

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsBINDING: BINDING => ECO:0000269|PubMed:15329726, ECO:0007744|PDB:1SX6
ChainResidueDetails
AASP48
EASP48
EHIS140
ETYR207
AHIS140
ATYR207
BASP48
BHIS140
BTYR207
DASP48
DHIS140
DTYR207

site_idSWS_FT_FI2
Number of Residues4
DetailsMOD_RES: N-acetylalanine => ECO:0000250|UniProtKB:P68266
ChainResidueDetails
AALA2
BALA2
DALA2
EALA2

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PDB entries from 2025-06-18

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