6NNX

Crystal Structure of the All-Trans Retinal-Bound R111K:Y134F:T54V:R132Q:P39Y:R59Y:L121M Mutant of Human Cellular Retinoic Acid Binding Protein II in the Dark at 1.87 Angstrom Resolution

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0001972	molecular_function	retinoic acid binding
A	0005501	molecular_function	retinoid binding
A	0005504	molecular_function	fatty acid binding
A	0005515	molecular_function	protein binding
A	0005634	cellular_component	nucleus
A	0005654	cellular_component	nucleoplasm
A	0005737	cellular_component	cytoplasm
A	0005783	cellular_component	endoplasmic reticulum
A	0005829	cellular_component	cytosol
A	0006355	biological_process	regulation of DNA-templated transcription
A	0007165	biological_process	signal transduction
A	0008289	molecular_function	lipid binding
A	0008544	biological_process	epidermis development
A	0015908	biological_process	fatty acid transport
A	0016918	molecular_function	retinal binding
A	0019841	molecular_function	retinol binding
A	0030332	molecular_function	cyclin binding
A	0035115	biological_process	embryonic forelimb morphogenesis
A	0042573	biological_process	retinoic acid metabolic process
A	0048672	biological_process	positive regulation of collateral sprouting
A	0070062	cellular_component	extracellular exosome

Functional Information from PDB Data

site_id	AC1
Number of Residues	9
Details	binding site for residue RET A 201

Functional Information from PROSITE/UniProt

site_id	PS00214
Number of Residues	18
Details	FABP Cytosolic fatty-acid binding proteins signature. GNWkIirSeNFEeLLKVL

Chain	Residue	Details
A	GLY5-LEU22

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269\|PubMed:16979656, ECO:0007744\|PDB:2FR3

Chain	Residue	Details
A	GLN132

site_id	SWS_FT_FI2
Number of Residues	2
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) => ECO:0000269\|PubMed:21998312

Chain	Residue	Details
A	LYS101