Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

4GHS

Crystal structure of human GLTP bound with 12:0 disulfatide (orthorombic form; two 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
Functional Information from PDB Data
site_idAC1
Number of Residues18
DetailsBINDING SITE FOR RESIDUE 0SG A 301
ChainResidue
ALEU37
ALEU136
AHIS140
ATYR207
BPRO40
BPRO44
BILE45
BPHE148
BALA151
B0SG301
AILE45
AASP48
AASN52
ALYS55
ALYS87
AALA93
ATRP96
APHE103

site_idAC2
Number of Residues21
DetailsBINDING SITE FOR RESIDUE 0SG B 301
ChainResidue
AVAL41
AILE45
AHIS140
APHE148
A0SG301
BPHE34
BPHE42
BILE45
BASP48
BASN52
BLYS55
BLYS87
BLEU92
BALA93
BTRP96
BPHE103
BLEU136
BHIS140
BILE147
BPHE148
BTYR207

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:15329726, ECO:0007744|PDB:1SX6
ChainResidueDetails
AASP48
AHIS140
ATYR207
BASP48
BHIS140
BTYR207

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: N-acetylalanine => ECO:0000250|UniProtKB:P68266
ChainResidueDetails
AALA2
BALA2

222926

PDB entries from 2024-07-24

PDB statisticsPDBj update infoContact PDBjnumon