Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4IB4

Crystal structure of the chimeric protein of 5-HT2B-BRIL in complex with ergotamine

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004930	molecular_function	G protein-coupled receptor activity
A	0004993	molecular_function	G protein-coupled serotonin receptor activity
A	0005506	molecular_function	iron ion binding
A	0005886	cellular_component	plasma membrane
A	0007186	biological_process	G protein-coupled receptor signaling pathway
A	0009055	molecular_function	electron transfer activity
A	0016020	cellular_component	membrane
A	0020037	molecular_function	heme binding
A	0022900	biological_process	electron transport chain
A	0042597	cellular_component	periplasmic space
A	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	16
Details	BINDING SITE FOR RESIDUE ERM A 2001

Chain	Residue
A	ASP135
A	ALA225
A	TRP337
A	PHE340
A	ASN344
A	LEU347
A	GLN359
A	HOH2020
A	VAL136
A	SER139
A	THR140
A	VAL208
A	LEU209
A	THR210
A	LYS211
A	MET218

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PLM A 2002

Chain	Residue
A	ILE66
A	THR343
A	ILE395
A	THR396
A	CYS397

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CLR A 2003

Chain	Residue
A	GLY70
A	THR73
A	TYR394
A	TYR399

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE OLC A 2004

Chain	Residue
A	SER150
A	MET233
A	THR240
A	LEU326
A	HOH2017

site_id	AC5
Number of Residues	2
Details	BINDING SITE FOR RESIDUE OLB A 2005

Chain	Residue
A	PRO191
A	ILE192

site_id	AC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE OLB A 2006

Chain	Residue
A	MET360
A	TYR399
A	OLB2007

site_id	AC7
Number of Residues	3
Details	BINDING SITE FOR RESIDUE OLB A 2007

Chain	Residue
A	LEU81
A	TYR399
A	OLB2006

site_id	AC8
Number of Residues	1
Details	BINDING SITE FOR RESIDUE OLA A 2008

Chain	Residue
A	TRP56

site_id	AC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE OLA A 2009

Chain	Residue
A	GLY185
A	LYS193
A	ASP216
A	PHE217

site_id	BC1
Number of Residues	2
Details	BINDING SITE FOR RESIDUE PEG A 2010

Chain	Residue
A	TYR380
A	ASN384

site_id	BC2
Number of Residues	1
Details	BINDING SITE FOR RESIDUE PEG A 2011

Chain	Residue
A	ILE182

Functional Information from PROSITE/UniProt

site_id	PS00237
Number of Residues	17
Details	G_PROTEIN_RECEP_F1_1 G-protein coupled receptors family 1 signature. ASIwHLCAISVDRYIaI

Chain	Residue	Details
A	ALA141-ILE157

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	Binding site: {"description":"axial binding residue"}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	22
Details	Transmembrane: {"description":"Helical; Name=1","evidences":[{"source":"PubMed","id":"23519215","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24357322","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"28129538","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30127358","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"36087581","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	29
Details	Topological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"23519215","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24357322","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"28129538","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30127358","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"36087581","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	22
Details	Transmembrane: {"description":"Helical; Name=2","evidences":[{"source":"PubMed","id":"23519215","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24357322","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"28129538","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30127358","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"36087581","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	29
Details	Topological domain: {"description":"Extracellular","evidences":[{"source":"PubMed","id":"23519215","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24357322","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"28129538","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30127358","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"36087581","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	21
Details	Transmembrane: {"description":"Helical; Name=3","evidences":[{"source":"PubMed","id":"23519215","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24357322","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"28129538","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30127358","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"36087581","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	20
Details	Transmembrane: {"description":"Helical; Name=4","evidences":[{"source":"PubMed","id":"23519215","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24357322","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"28129538","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30127358","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"36087581","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	22
Details	Transmembrane: {"description":"Helical; Name=5","evidences":[{"source":"PubMed","id":"23519215","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24357322","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"28129538","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30127358","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"36087581","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	20
Details	Transmembrane: {"description":"Helical; Name=6","evidences":[{"source":"PubMed","id":"23519215","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24357322","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"28129538","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30127358","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"36087581","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	21
Details	Transmembrane: {"description":"Helical; Name=7","evidences":[{"source":"PubMed","id":"23519215","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24357322","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"28129538","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30127358","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"36087581","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	2
Details	Motif: {"description":"DRY motif; important for ligand-induced conformation changes","evidences":[{"source":"PubMed","id":"23519215","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"28129538","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	3
Details	Motif: {"description":"[DE]RFG motif; may stabilize a conformation that preferentially activates signaling via beta-arrestin family members","evidences":[{"source":"PubMed","id":"23519215","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"28129538","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI13
Number of Residues	4
Details	Motif: {"description":"NPxxY motif; important for ligand-induced conformation changes and signaling","evidences":[{"source":"PubMed","id":"23519215","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"28129538","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI14
Number of Residues	3
Details	Binding site: {"evidences":[{"source":"PubMed","id":"23519215","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4IB4","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4NC3","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI15
Number of Residues	1
Details	Site: {"description":"Hydrophobic barrier that decreases the speed of ligand binding and dissociation","evidences":[{"source":"PubMed","id":"28129538","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI16
Number of Residues	1
Details	Lipidation: {"description":"S-palmitoyl cysteine","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)