6O1V

Complex of human cystic fibrosis transmembrane conductance regulator (CFTR) and GLPG1837

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0005254	molecular_function	chloride channel activity
A	0005260	molecular_function	intracellularly ATP-gated chloride channel activity
A	0005515	molecular_function	protein binding
A	0005524	molecular_function	ATP binding
A	0005634	cellular_component	nucleus
A	0005737	cellular_component	cytoplasm
A	0005765	cellular_component	lysosomal membrane
A	0005768	cellular_component	endosome
A	0005769	cellular_component	early endosome
A	0005783	cellular_component	endoplasmic reticulum
A	0005789	cellular_component	endoplasmic reticulum membrane
A	0005829	cellular_component	cytosol
A	0005886	cellular_component	plasma membrane
A	0006695	biological_process	cholesterol biosynthetic process
A	0006811	biological_process	monoatomic ion transport
A	0006821	biological_process	chloride transport
A	0006833	biological_process	water transport
A	0006904	biological_process	vesicle docking involved in exocytosis
A	0009986	cellular_component	cell surface
A	0010008	cellular_component	endosome membrane
A	0015106	molecular_function	bicarbonate transmembrane transporter activity
A	0015108	molecular_function	chloride transmembrane transporter activity
A	0015701	biological_process	bicarbonate transport
A	0016020	cellular_component	membrane
A	0016323	cellular_component	basolateral plasma membrane
A	0016324	cellular_component	apical plasma membrane
A	0016853	molecular_function	isomerase activity
A	0016887	molecular_function	ATP hydrolysis activity
A	0017081	molecular_function	chloride channel regulator activity
A	0019869	molecular_function	chloride channel inhibitor activity
A	0019899	molecular_function	enzyme binding
A	0030165	molecular_function	PDZ domain binding
A	0030301	biological_process	cholesterol transport
A	0030660	cellular_component	Golgi-associated vesicle membrane
A	0030669	cellular_component	clathrin-coated endocytic vesicle membrane
A	0031901	cellular_component	early endosome membrane
A	0032991	cellular_component	protein-containing complex
A	0034220	biological_process	monoatomic ion transmembrane transport
A	0034707	cellular_component	chloride channel complex
A	0034976	biological_process	response to endoplasmic reticulum stress
A	0035377	biological_process	transepithelial water transport
A	0035774	biological_process	positive regulation of insulin secretion involved in cellular response to glucose stimulus
A	0043225	molecular_function	ATPase-coupled inorganic anion transmembrane transporter activity
A	0045921	biological_process	positive regulation of exocytosis
A	0048240	biological_process	sperm capacitation
A	0050891	biological_process	multicellular organismal-level water homeostasis
A	0051087	molecular_function	protein-folding chaperone binding
A	0051454	biological_process	intracellular pH elevation
A	0051649	biological_process	establishment of localization in cell
A	0055037	cellular_component	recycling endosome
A	0055038	cellular_component	recycling endosome membrane
A	0055085	biological_process	transmembrane transport
A	0060081	biological_process	membrane hyperpolarization
A	0065008	biological_process	regulation of biological quality
A	0070175	biological_process	positive regulation of enamel mineralization
A	0071320	biological_process	cellular response to cAMP
A	0071889	molecular_function	14-3-3 protein binding
A	0097186	biological_process	amelogenesis
A	0098660	biological_process	inorganic ion transmembrane transport
A	0106138	molecular_function	Sec61 translocon complex binding
A	0140359	molecular_function	ABC-type transporter activity
A	1902476	biological_process	chloride transmembrane transport
A	1902943	biological_process	positive regulation of voltage-gated chloride channel activity
A	1904322	biological_process	cellular response to forskolin

Functional Information from PDB Data

site_id	AC1
Number of Residues	7
Details	binding site for residue LJP A 2001

Chain	Residue
A	TYR304
A	PHE305
A	SER308
A	ALA309
A	PHE312
A	GLY930
A	PHE931

---

site_id	AC2
Number of Residues	3
Details	binding site for residue MG A 2002

Chain	Residue
A	ATP2004
A	THR465
A	GLN493

---

site_id	AC3
Number of Residues	4
Details	binding site for residue MG A 2003

Chain	Residue
A	SER1251
A	GLN1291
A	ASP1370
A	ATP2005

---

site_id	AC4
Number of Residues	16
Details	binding site for residue ATP A 2004

Chain	Residue
A	TRP401
A	VAL440
A	THR460
A	GLY461
A	ALA462
A	GLY463
A	LYS464
A	THR465
A	SER466
A	GLN493
A	CYS1344
A	VAL1345
A	SER1347
A	HIS1348
A	GLY1349
A	MG2002

---

site_id	AC5
Number of Residues	15
Details	binding site for residue ATP A 2005

Chain	Residue
A	PHE533
A	ILE546
A	THR547
A	SER549
A	GLY551
A	GLN552
A	TYR1219
A	THR1246
A	GLY1247
A	GLY1249
A	LYS1250
A	SER1251
A	THR1252
A	GLN1291
A	MG2003

---

site_id	AC6
Number of Residues	3
Details	binding site for residue POV A 2007

Chain	Residue
A	TRP216
A	PHE224
A	CLR2011

---

site_id	AC7
Number of Residues	2
Details	binding site for residue CLR A 2011

Chain	Residue
A	GLU217
A	POV2007

---

Functional Information from PROSITE/UniProt

site_id	PS00211
Number of Residues	15
Details	ABC_TRANSPORTER_1 ABC transporters family signature. LSGGQRARISLARAV

Chain	Residue	Details
A	LEU548-VAL562

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	76
Details	Topological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	20
Details	Transmembrane: {"description":"Helical; Name=1","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"DEC-2016","submissionDatabase":"PDB data bank","title":"Structure of human cystic fibrosis transmembrane conductance regulator (CFTR).","authors":["Liu F.","Zhang Z.","Chen J."]}}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	61
Details	Topological domain: {"description":"Extracellular","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"DEC-2016","submissionDatabase":"PDB data bank","title":"Structure of human cystic fibrosis transmembrane conductance regulator (CFTR).","authors":["Liu F.","Zhang Z.","Chen J."]}}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	23
Details	Transmembrane: {"description":"Helical; Name=2","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"DEC-2016","submissionDatabase":"PDB data bank","title":"Structure of human cystic fibrosis transmembrane conductance regulator (CFTR).","authors":["Liu F.","Zhang Z.","Chen J."]}}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	212
Details	Topological domain: {"description":"Cytoplasmic","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"DEC-2016","submissionDatabase":"PDB data bank","title":"Structure of human cystic fibrosis transmembrane conductance regulator (CFTR).","authors":["Liu F.","Zhang Z.","Chen J."]}}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	20
Details	Transmembrane: {"description":"Helical; Name=3","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"DEC-2016","submissionDatabase":"PDB data bank","title":"Structure of human cystic fibrosis transmembrane conductance regulator (CFTR).","authors":["Liu F.","Zhang Z.","Chen J."]}}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	20
Details	Transmembrane: {"description":"Helical; Name=4","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"DEC-2016","submissionDatabase":"PDB data bank","title":"Structure of human cystic fibrosis transmembrane conductance regulator (CFTR).","authors":["Liu F.","Zhang Z.","Chen J."]}}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI8
Number of Residues	20
Details	Transmembrane: {"description":"Helical; Name=5","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"DEC-2016","submissionDatabase":"PDB data bank","title":"Structure of human cystic fibrosis transmembrane conductance regulator (CFTR).","authors":["Liu F.","Zhang Z.","Chen J."]}}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI9
Number of Residues	18
Details	Transmembrane: {"description":"Helical; Name=6","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"DEC-2016","submissionDatabase":"PDB data bank","title":"Structure of human cystic fibrosis transmembrane conductance regulator (CFTR).","authors":["Liu F.","Zhang Z.","Chen J."]}}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI10
Number of Residues	20
Details	Transmembrane: {"description":"Helical; Name=7","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"DEC-2016","submissionDatabase":"PDB data bank","title":"Structure of human cystic fibrosis transmembrane conductance regulator (CFTR).","authors":["Liu F.","Zhang Z.","Chen J."]}}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI11
Number of Residues	20
Details	Transmembrane: {"description":"Discontinuously helical; Name=8","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"DEC-2016","submissionDatabase":"PDB data bank","title":"Structure of human cystic fibrosis transmembrane conductance regulator (CFTR).","authors":["Liu F.","Zhang Z.","Chen J."]}}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI12
Number of Residues	20
Details	Transmembrane: {"description":"Helical; Name=9","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"DEC-2016","submissionDatabase":"PDB data bank","title":"Structure of human cystic fibrosis transmembrane conductance regulator (CFTR).","authors":["Liu F.","Zhang Z.","Chen J."]}}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI13
Number of Residues	20
Details	Transmembrane: {"description":"Helical; Name=10","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"DEC-2016","submissionDatabase":"PDB data bank","title":"Structure of human cystic fibrosis transmembrane conductance regulator (CFTR).","authors":["Liu F.","Zhang Z.","Chen J."]}}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI14
Number of Residues	20
Details	Transmembrane: {"description":"Helical; Name=11","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"DEC-2016","submissionDatabase":"PDB data bank","title":"Structure of human cystic fibrosis transmembrane conductance regulator (CFTR).","authors":["Liu F.","Zhang Z.","Chen J."]}}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI15
Number of Residues	20
Details	Transmembrane: {"description":"Helical; Name=12","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"DEC-2016","submissionDatabase":"PDB data bank","title":"Structure of human cystic fibrosis transmembrane conductance regulator (CFTR).","authors":["Liu F.","Zhang Z.","Chen J."]}}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI16
Number of Residues	284
Details	Domain: {"description":"ABC transmembrane type-1 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00441","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI17
Number of Residues	233
Details	Domain: {"description":"ABC transporter 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00434","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI18
Number of Residues	1
Details	Binding site: {"evidences":[{"source":"PubMed","id":"15528182","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20150177","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1XMI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1XMJ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2BBO","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2BBS","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2BBT","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2PZE","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2PZF","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2PZG","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI19
Number of Residues	7
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00434","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"15528182","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1XMI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1XMJ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2BBO","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2BBS","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2BBT","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI20
Number of Residues	1
Details	Binding site: {"evidences":[{"source":"PubMed","id":"15528182","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1XMI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2BBO","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2BBS","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI21
Number of Residues	1
Details	Binding site: {"evidences":[{"source":"PDB","id":"3GD7","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI22
Number of Residues	7
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00434","evidenceCode":"ECO:0000255"},{"source":"PDB","id":"3GD7","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI23
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI24
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"22119790","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI25
Number of Residues	2
Details	Lipidation: {"description":"S-palmitoyl cysteine","evidences":[{"source":"PubMed","id":"22119790","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI26
Number of Residues	1
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"7518437","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20008117","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---