6QBA

Crystal Structure of Retinol-Binding Protein 4 (RBP4) in complex with non-retinoid ligand A1120 and engineered binding scaffold

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0001523	biological_process	retinoid metabolic process
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	0007283	biological_process	spermatogenesis
A	0007507	biological_process	heart development
A	0007601	biological_process	visual perception
A	0007603	biological_process	phototransduction, visible light
A	0008584	biological_process	male gonad development
A	0009410	biological_process	response to xenobiotic stimulus
A	0014850	biological_process	response to muscle activity
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	0032868	biological_process	response to insulin
A	0032991	cellular_component	protein-containing complex
A	0034632	molecular_function	retinol transmembrane transporter activity
A	0034633	biological_process	retinol transport
A	0042572	biological_process	retinol metabolic process
A	0042574	biological_process	retinal metabolic process
A	0042593	biological_process	glucose homeostasis
A	0044877	molecular_function	protein-containing complex binding
A	0045471	biological_process	response to ethanol
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	0050908	biological_process	detection of light stimulus involved in visual perception
A	0060041	biological_process	retina development in camera-type eye
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
A	0071939	biological_process	vitamin A import into cell
A	0140104	molecular_function	molecular carrier activity
B	0003677	molecular_function	DNA binding
B	0004518	molecular_function	nuclease activity
B	0004519	molecular_function	endonuclease activity
B	0004521	molecular_function	RNA endonuclease activity
B	0016787	molecular_function	hydrolase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	14
Details	binding site for residue 2T1 A 201

Chain	Residue
A	LEU35
A	PHE135
A	HOH336
A	HOH348
A	HOH390
B	TYR25
A	PHE36
A	LEU37
A	ALA57
A	MET73
A	MET88
A	TYR90
A	HIS104
A	ARG121

---

site_id	AC2
Number of Residues	9
Details	binding site for residue IMD A 202

Chain	Residue
A	ARG10
A	VAL11
A	GLU13
A	VAL107
A	ARG155
A	GLU158
A	IMD205
A	ZN209
B	GLU10

---

site_id	AC3
Number of Residues	6
Details	binding site for residue IMD A 203

Chain	Residue
A	ASP140
A	GLY143
A	ZN208
B	GLU59
B	HOH204
B	HOH213

---

site_id	AC4
Number of Residues	7
Details	binding site for residue IMD A 204

Chain	Residue
A	TYR25
A	HIS170
A	ASP175
A	IMD206
A	ZN210
A	HOH439
B	GLN56

---

site_id	AC5
Number of Residues	7
Details	binding site for residue IMD A 205

Chain	Residue
A	LYS12
A	GLU13
A	ASP108
A	ARG155
A	IMD202
A	ZN209
B	GLU10

---

site_id	AC6
Number of Residues	6
Details	binding site for residue IMD A 206

Chain	Residue
A	HIS170
A	GLY172
A	ASP175
A	IMD204
A	ZN210
B	GLN56

---

site_id	AC7
Number of Residues	5
Details	binding site for residue PEG A 207

Chain	Residue
A	ALA28
A	GLN156
A	TYR165
A	HOH327
B	GLU35

---

site_id	AC8
Number of Residues	6
Details	binding site for residue ZN A 208

Chain	Residue
A	ASP140
A	IMD203
B	ARG24
B	GLU59
B	HOH204
B	HOH247

---

site_id	AC9
Number of Residues	4
Details	binding site for residue ZN A 209

Chain	Residue
A	GLU13
A	IMD202
A	IMD205
B	GLU10

---

site_id	AD1
Number of Residues	4
Details	binding site for residue ZN A 210

Chain	Residue
A	HIS170
A	ASP175
A	IMD204
A	IMD206

---

site_id	AD2
Number of Residues	3
Details	binding site for residue ACT B 101

Chain	Residue
B	GLU53
B	HOH214
B	HOH227

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	ASN14-MET27

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P27485","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	1
Details	Modified residue: {"description":"Omega-N-methylarginine","evidences":[{"source":"UniProtKB","id":"Q00724","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	Modified residue: {"description":"N6-methyllysine; partial","evidences":[{"source":"PubMed","id":"8425540","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---