1YP6

Van der Waals Interactions Dominate Hydrophobic Association in a Protein Binding Site Occluded From Solvent Water

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005009	molecular_function	insulin receptor activity
A	0005186	molecular_function	pheromone activity
A	0005550	molecular_function	pheromone binding
A	0005576	cellular_component	extracellular region
A	0005615	cellular_component	extracellular space
A	0005634	cellular_component	nucleus
A	0005829	cellular_component	cytosol
A	0006112	biological_process	energy reserve metabolic process
A	0007005	biological_process	mitochondrion organization
A	0007165	biological_process	signal transduction
A	0008286	biological_process	insulin receptor signaling pathway
A	0009060	biological_process	aerobic respiration
A	0009267	biological_process	cellular response to starvation
A	0010628	biological_process	positive regulation of gene expression
A	0010888	biological_process	negative regulation of lipid storage
A	0010907	biological_process	positive regulation of glucose metabolic process
A	0031649	biological_process	heat generation
A	0035634	biological_process	response to stilbenoid
A	0036094	molecular_function	small molecule binding
A	0042593	biological_process	glucose homeostasis
A	0045475	biological_process	locomotor rhythm
A	0045721	biological_process	negative regulation of gluconeogenesis
A	0045834	biological_process	positive regulation of lipid metabolic process
A	0045892	biological_process	negative regulation of DNA-templated transcription
A	0051055	biological_process	negative regulation of lipid biosynthetic process
A	0051897	biological_process	positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction
A	0061179	biological_process	negative regulation of insulin secretion involved in cellular response to glucose stimulus
A	0071240	biological_process	cellular response to food
A	0071394	biological_process	cellular response to testosterone stimulus
A	0071396	biological_process	cellular response to lipid

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CD A 200

Chain	Residue
A	GLU18
A	GLU139
A	HOH407
A	HOH418
A	HOH420

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site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CD A 201

Chain	Residue
A	HOH460
A	GLU13
A	ASP110
A	HOH406
A	HOH457

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site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CL A 202

Chain	Residue
A	LYS76
A	GLU140
A	HOH260
A	HOH284
A	HOH360

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site_id	AC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE PRZ A 203

Chain	Residue
A	PHE56
A	ALA103
A	LEU116

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Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	ASN9-ILE22

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