Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1QAB

The structure of human retinol binding protein with its carrier protein transthyretin reveals interaction with the carboxy terminus of RBP

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005179	molecular_function	hormone activity
A	0005515	molecular_function	protein binding
A	0005576	cellular_component	extracellular region
A	0005615	cellular_component	extracellular space
A	0005737	cellular_component	cytoplasm
A	0006144	biological_process	purine nucleobase metabolic process
A	0007165	biological_process	signal transduction
A	0035578	cellular_component	azurophil granule lumen
A	0042802	molecular_function	identical protein binding
A	0070062	cellular_component	extracellular exosome
A	0070324	molecular_function	thyroid hormone binding
B	0005179	molecular_function	hormone activity
B	0005515	molecular_function	protein binding
B	0005576	cellular_component	extracellular region
B	0005615	cellular_component	extracellular space
B	0005737	cellular_component	cytoplasm
B	0006144	biological_process	purine nucleobase metabolic process
B	0007165	biological_process	signal transduction
B	0035578	cellular_component	azurophil granule lumen
B	0042802	molecular_function	identical protein binding
B	0070062	cellular_component	extracellular exosome
B	0070324	molecular_function	thyroid hormone binding
C	0005179	molecular_function	hormone activity
C	0005515	molecular_function	protein binding
C	0005576	cellular_component	extracellular region
C	0005615	cellular_component	extracellular space
C	0005737	cellular_component	cytoplasm
C	0006144	biological_process	purine nucleobase metabolic process
C	0007165	biological_process	signal transduction
C	0035578	cellular_component	azurophil granule lumen
C	0042802	molecular_function	identical protein binding
C	0070062	cellular_component	extracellular exosome
C	0070324	molecular_function	thyroid hormone binding
D	0005179	molecular_function	hormone activity
D	0005515	molecular_function	protein binding
D	0005576	cellular_component	extracellular region
D	0005615	cellular_component	extracellular space
D	0005737	cellular_component	cytoplasm
D	0006144	biological_process	purine nucleobase metabolic process
D	0007165	biological_process	signal transduction
D	0035578	cellular_component	azurophil granule lumen
D	0042802	molecular_function	identical protein binding
D	0070062	cellular_component	extracellular exosome
D	0070324	molecular_function	thyroid hormone binding
E	0001654	biological_process	eye development
E	0002639	biological_process	positive regulation of immunoglobulin production
E	0005501	molecular_function	retinoid binding
E	0005515	molecular_function	protein binding
E	0005576	cellular_component	extracellular region
E	0005615	cellular_component	extracellular space
E	0006094	biological_process	gluconeogenesis
E	0007507	biological_process	heart development
E	0007601	biological_process	visual perception
E	0016918	molecular_function	retinal binding
E	0019841	molecular_function	retinol binding
E	0030277	biological_process	maintenance of gastrointestinal epithelium
E	0030324	biological_process	lung development
E	0032024	biological_process	positive regulation of insulin secretion
E	0032526	biological_process	response to retinoic acid
E	0034632	molecular_function	retinol transmembrane transporter activity
E	0034633	biological_process	retinol transport
E	0042572	biological_process	retinol metabolic process
E	0042593	biological_process	glucose homeostasis
E	0048562	biological_process	embryonic organ morphogenesis
E	0048706	biological_process	embryonic skeletal system development
E	0048738	biological_process	cardiac muscle tissue development
E	0048807	biological_process	female genitalia morphogenesis
E	0060044	biological_process	negative regulation of cardiac muscle cell proliferation
E	0060059	biological_process	embryonic retina morphogenesis in camera-type eye
E	0060065	biological_process	uterus development
E	0060068	biological_process	vagina development
E	0060157	biological_process	urinary bladder development
E	0060347	biological_process	heart trabecula formation
E	0070062	cellular_component	extracellular exosome
F	0001654	biological_process	eye development
F	0002639	biological_process	positive regulation of immunoglobulin production
F	0005501	molecular_function	retinoid binding
F	0005515	molecular_function	protein binding
F	0005576	cellular_component	extracellular region
F	0005615	cellular_component	extracellular space
F	0006094	biological_process	gluconeogenesis
F	0007507	biological_process	heart development
F	0007601	biological_process	visual perception
F	0016918	molecular_function	retinal binding
F	0019841	molecular_function	retinol binding
F	0030277	biological_process	maintenance of gastrointestinal epithelium
F	0030324	biological_process	lung development
F	0032024	biological_process	positive regulation of insulin secretion
F	0032526	biological_process	response to retinoic acid
F	0034632	molecular_function	retinol transmembrane transporter activity
F	0034633	biological_process	retinol transport
F	0042572	biological_process	retinol metabolic process
F	0042593	biological_process	glucose homeostasis
F	0048562	biological_process	embryonic organ morphogenesis
F	0048706	biological_process	embryonic skeletal system development
F	0048738	biological_process	cardiac muscle tissue development
F	0048807	biological_process	female genitalia morphogenesis
F	0060044	biological_process	negative regulation of cardiac muscle cell proliferation
F	0060059	biological_process	embryonic retina morphogenesis in camera-type eye
F	0060065	biological_process	uterus development
F	0060068	biological_process	vagina development
F	0060157	biological_process	urinary bladder development
F	0060347	biological_process	heart trabecula formation
F	0070062	cellular_component	extracellular exosome

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE RTL E 1

Chain	Residue
D	GLY83
E	PHE36
E	ALA57
E	MET73
E	TYR90
E	LEU97

site_id	AC2
Number of Residues	11
Details	BINDING SITE FOR RESIDUE RTL F 2

Chain	Residue
F	ALA55
F	ALA57
F	MET73
F	VAL74
F	MET88
F	TYR90
F	LEU97
F	GLN98
B	GLY83
F	LEU35
F	PHE36

Functional Information from PROSITE/UniProt

site_id	PS00213
Number of Residues	14
Details	LIPOCALIN Lipocalin signature. NFDkaRFSGTWYAM

Chain	Residue	Details
E	ASN14-MET27

site_id	PS00768
Number of Residues	16
Details	TRANSTHYRETIN_1 Transthyretin signature 1. KVLDavrGsPAinVaV

Chain	Residue	Details
A	LYS15-VAL30

site_id	PS00769
Number of Residues	13
Details	TRANSTHYRETIN_2 Transthyretin signature 2. YTIAalLSPYSYS

Chain	Residue	Details
A	TYR105-SER117

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	BINDING: BINDING => ECO:0000250\|UniProtKB:P27485

Chain	Residue	Details
E	GLN98
D	LYS15
D	GLU54
D	SER117
F	GLN98
A	SER117
B	LYS15
B	GLU54
B	SER117
C	LYS15
C	GLU54
C	SER117

site_id	SWS_FT_FI2
Number of Residues	2
Details	MOD_RES: Omega-N-methylarginine => ECO:0000250\|UniProtKB:Q00724

Chain	Residue	Details
E	ARG121
F	ARG121
C	CYS10
D	CYS10

site_id	SWS_FT_FI3
Number of Residues	4
Details	MOD_RES: 4-carboxyglutamate; in a patient with Moyamoya disease => ECO:0000269\|PubMed:18221012

Chain	Residue	Details
A	GLU42
B	GLU42
C	GLU42
D	GLU42

site_id	SWS_FT_FI4
Number of Residues	4
Details	MOD_RES: Phosphoserine => ECO:0000250\|UniProtKB:P02767

Chain	Residue	Details
A	SER52
B	SER52
C	SER52
D	SER52

site_id	SWS_FT_FI5
Number of Residues	4
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269\|PubMed:16335952, ECO:0000269\|PubMed:19167329

Chain	Residue	Details
A	ASN98
B	ASN98
C	ASN98
D	ASN98

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)