7MFZ

The Crystal Structure of Domain-Swapped Trimer Q108K:K40D:T53A:R58L:Q38F:Q4F Mutant of HCRBPII Bound with LizFluor3 Chromophore Showing Excited State Intermolecular Proton Transfer

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005501	molecular_function	retinoid binding
A	0005504	molecular_function	fatty acid binding
A	0005634	cellular_component	nucleus
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006776	biological_process	vitamin A metabolic process
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
B	0005501	molecular_function	retinoid binding
B	0005504	molecular_function	fatty acid binding
B	0005634	cellular_component	nucleus
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0006776	biological_process	vitamin A metabolic process
B	0008289	molecular_function	lipid binding
B	0008544	biological_process	epidermis development
B	0015908	biological_process	fatty acid transport
B	0016918	molecular_function	retinal binding
B	0019841	molecular_function	retinol binding
C	0005501	molecular_function	retinoid binding
C	0005504	molecular_function	fatty acid binding
C	0005634	cellular_component	nucleus
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0006776	biological_process	vitamin A metabolic process
C	0008289	molecular_function	lipid binding
C	0008544	biological_process	epidermis development
C	0015908	biological_process	fatty acid transport
C	0016918	molecular_function	retinal binding
C	0019841	molecular_function	retinol binding

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	GLY6-LEU23

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	BINDING: BINDING => ECO:0000269|PubMed:18076076

Chain	Residue	Details
A	ASP40
A	LYS108
B	ASP40
B	LYS108
C	ASP40
C	LYS108

---