3RWV

Crystal Structure of apo-form of Human Glycolipid Transfer Protein at 1.5 A resolution

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	0035621	biological_process	ER to Golgi ceramide transport
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	0035621	biological_process	ER to Golgi ceramide transport
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

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 B 301

Chain	Residue
B	LEU205
B	ASN206
B	TYR207
B	HOH540
B	HOH675

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	BINDING: BINDING => ECO:0000269|PubMed:15329726, ECO:0007744|PDB:1SX6

Chain	Residue	Details
A	ASP48
A	HIS140
A	TYR207
B	ASP48
B	HIS140
B	TYR207

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site_id	SWS_FT_FI2
Number of Residues	2
Details	MOD_RES: N-acetylalanine => ECO:0000250|UniProtKB:P68266

Chain	Residue	Details
A	ALA2
B	ALA2

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