1BRP

CRYSTAL STRUCTURE OF THE TRIGONAL FORM OF HUMAN PLASMA RETINOL-BINDING PROTEIN AT 2.5 ANGSTROMS RESOLUTION

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0001654	biological_process	eye development
A	0002639	biological_process	positive regulation of immunoglobulin production
A	0005501	molecular_function	retinoid binding
A	0005515	molecular_function	protein binding
A	0005576	cellular_component	extracellular region
A	0005615	cellular_component	extracellular space
A	0006094	biological_process	gluconeogenesis
A	0007507	biological_process	heart development
A	0007601	biological_process	visual perception
A	0016918	molecular_function	retinal binding
A	0019841	molecular_function	retinol binding
A	0030277	biological_process	maintenance of gastrointestinal epithelium
A	0030324	biological_process	lung development
A	0032024	biological_process	positive regulation of insulin secretion
A	0032526	biological_process	response to retinoic acid
A	0034632	molecular_function	retinol transmembrane transporter activity
A	0034633	biological_process	retinol transport
A	0042572	biological_process	retinol metabolic process
A	0042593	biological_process	glucose homeostasis
A	0048562	biological_process	embryonic organ morphogenesis
A	0048706	biological_process	embryonic skeletal system development
A	0048738	biological_process	cardiac muscle tissue development
A	0048807	biological_process	female genitalia morphogenesis
A	0050896	biological_process	response to stimulus
A	0060044	biological_process	negative regulation of cardiac muscle cell proliferation
A	0060059	biological_process	embryonic retina morphogenesis in camera-type eye
A	0060065	biological_process	uterus development
A	0060068	biological_process	vagina development
A	0060157	biological_process	urinary bladder development
A	0060347	biological_process	heart trabecula formation
A	0070062	cellular_component	extracellular exosome

Functional Information from PDB Data

site_id	AC1
Number of Residues	8
Details	BINDING SITE FOR RESIDUE RTL A 183

Chain	Residue
A	PHE36
A	LEU37
A	ALA57
A	VAL61
A	MET88
A	TYR90
A	GLN98
A	PHE135

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site_id	R1
Number of Residues	15
Details

Chain	Residue
A	ALA43
A	LEU35
A	PHE36
A	LEU37
A	VAL61
A	TYR90
A	GLN98
A	PHE45
A	ALA55
A	ALA57
A	MET73
A	MET88
A	HIS104
A	TYR133
A	PHE135

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Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	ASN14-MET27

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	BINDING: BINDING => ECO:0000250|UniProtKB:P27485

Chain	Residue	Details
A	GLY100

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site_id	SWS_FT_FI2
Number of Residues	1
Details	MOD_RES: Omega-N-methylarginine => ECO:0000250|UniProtKB:Q00724

Chain	Residue	Details
A	LEU123

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