4GXG

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

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005515	molecular_function	protein binding
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006869	biological_process	lipid transport
A	0008289	molecular_function	lipid binding
A	0017089	molecular_function	glycolipid transfer activity
A	0035627	biological_process	ceramide transport
A	0035902	biological_process	response to immobilization stress
A	0042802	molecular_function	identical protein binding
A	0046836	biological_process	glycolipid transport
A	0051861	molecular_function	glycolipid binding
A	0120009	biological_process	intermembrane lipid transfer
A	0120013	molecular_function	lipid transfer activity
A	1902387	molecular_function	ceramide 1-phosphate binding
A	1902388	molecular_function	ceramide 1-phosphate transfer activity
A	1902389	biological_process	ceramide 1-phosphate transport
B	0005515	molecular_function	protein binding
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0006869	biological_process	lipid transport
B	0008289	molecular_function	lipid binding
B	0017089	molecular_function	glycolipid transfer activity
B	0035627	biological_process	ceramide transport
B	0035902	biological_process	response to immobilization stress
B	0042802	molecular_function	identical protein binding
B	0046836	biological_process	glycolipid transport
B	0051861	molecular_function	glycolipid binding
B	0120009	biological_process	intermembrane lipid transfer
B	0120013	molecular_function	lipid transfer activity
B	1902387	molecular_function	ceramide 1-phosphate binding
B	1902388	molecular_function	ceramide 1-phosphate transfer activity
B	1902389	biological_process	ceramide 1-phosphate transport
D	0005515	molecular_function	protein binding
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0006869	biological_process	lipid transport
D	0008289	molecular_function	lipid binding
D	0017089	molecular_function	glycolipid transfer activity
D	0035627	biological_process	ceramide transport
D	0035902	biological_process	response to immobilization stress
D	0042802	molecular_function	identical protein binding
D	0046836	biological_process	glycolipid transport
D	0051861	molecular_function	glycolipid binding
D	0120009	biological_process	intermembrane lipid transfer
D	0120013	molecular_function	lipid transfer activity
D	1902387	molecular_function	ceramide 1-phosphate binding
D	1902388	molecular_function	ceramide 1-phosphate transfer activity
D	1902389	biological_process	ceramide 1-phosphate transport
E	0005515	molecular_function	protein binding
E	0005737	cellular_component	cytoplasm
E	0005829	cellular_component	cytosol
E	0006869	biological_process	lipid transport
E	0008289	molecular_function	lipid binding
E	0017089	molecular_function	glycolipid transfer activity
E	0035627	biological_process	ceramide transport
E	0035902	biological_process	response to immobilization stress
E	0042802	molecular_function	identical protein binding
E	0046836	biological_process	glycolipid transport
E	0051861	molecular_function	glycolipid binding
E	0120009	biological_process	intermembrane lipid transfer
E	0120013	molecular_function	lipid transfer activity
E	1902387	molecular_function	ceramide 1-phosphate binding
E	1902388	molecular_function	ceramide 1-phosphate transfer activity
E	1902389	biological_process	ceramide 1-phosphate transport

Functional Information from PDB Data

site_id	AC1
Number of Residues	18
Details	BINDING SITE FOR RESIDUE EIS A 700

Chain	Residue
A	ILE45
A	HIS140
A	ILE147
A	PHE148
A	TYR207
A	HOH882
B	VAL41
B	TYR132
B	PHE148
B	EIS700
A	ASP48
A	ASN52
A	LYS55
A	LEU92
A	ALA93
A	TRP96
A	PHE103
A	LEU136

---

site_id	AC2
Number of Residues	19
Details	BINDING SITE FOR RESIDUE EIS B 700

Chain	Residue
A	VAL41
A	PRO44
A	HIS140
A	PHE148
A	EIS700
B	PHE42
B	ILE45
B	ASP48
B	GLY51
B	ASN52
B	LYS55
B	LEU92
B	ALA93
B	TRP96
B	PHE103
B	LEU136
B	HIS140
B	TYR207
B	VAL209

---

site_id	AC3
Number of Residues	18
Details	BINDING SITE FOR RESIDUE EIS D 700

Chain	Residue
D	PHE42
D	ILE45
D	ASP48
D	ILE49
D	ASN52
D	LYS55
D	ALA93
D	TRP96
D	PHE103
D	LEU136
D	HIS140
D	PHE148
D	TYR207
E	VAL41
E	PRO44
E	PHE148
E	ALA151
E	EIS700

---

site_id	AC4
Number of Residues	18
Details	BINDING SITE FOR RESIDUE EIS E 700

Chain	Residue
D	VAL41
D	ILE45
D	PHE148
D	EIS700
E	ILE45
E	ASP48
E	GLY51
E	ASN52
E	LYS55
E	LEU92
E	ALA93
E	TRP96
E	PHE103
E	LEU136
E	HIS140
E	TYR207
E	HOH852
E	HOH854

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	40
Details	Repeat: {"description":"1"}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	40
Details	Repeat: {"description":"2"}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	84
Details	Region: {"description":"2 X 12 AA approximate tandem repeats"}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	36
Details	Binding site: {"evidences":[{"source":"PubMed","id":"15329726","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1SX6","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	Modified residue: {"description":"N-acetylalanine","evidences":[{"source":"UniProtKB","id":"P68266","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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