5TUD

Structural Insights into the Extracellular Recognition of the Human Serotonin 2B Receptor by an Antibody

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	0006939	biological_process	smooth muscle contraction
A	0007186	biological_process	G protein-coupled receptor signaling pathway
A	0007507	biological_process	heart development
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	0042310	biological_process	vasoconstriction
A	0042597	cellular_component	periplasmic space
A	0046872	molecular_function	metal ion binding
A	0050795	biological_process	regulation of behavior
D	0004930	molecular_function	G protein-coupled receptor activity
D	0004993	molecular_function	G protein-coupled serotonin receptor activity
D	0005506	molecular_function	iron ion binding
D	0005886	cellular_component	plasma membrane
D	0006939	biological_process	smooth muscle contraction
D	0007186	biological_process	G protein-coupled receptor signaling pathway
D	0007507	biological_process	heart development
D	0009055	molecular_function	electron transfer activity
D	0016020	cellular_component	membrane
D	0020037	molecular_function	heme binding
D	0022900	biological_process	electron transport chain
D	0042310	biological_process	vasoconstriction
D	0042597	cellular_component	periplasmic space
D	0046872	molecular_function	metal ion binding
D	0050795	biological_process	regulation of behavior

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	PHE340
A	PHE341
A	LEU347
A	GLN359
A	LEU362
A	GLU363
A	VAL366
A	VAL136
A	SER139
A	THR140
A	VAL208
A	LEU209
A	LYS211
A	MET218
A	ALA225

---

site_id	AC2
Number of Residues	17
Details	binding site for residue ERM D 1201

Chain	Residue
D	ASP135
D	SER139
D	THR140
D	VAL208
D	LEU209
D	THR210
D	MET218
D	ALA225
D	PHE340
D	PHE341
D	ASN344
D	VAL348
D	GLN359
D	LEU362
D	GLU363
D	VAL366
D	TYR370

---

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

---

site_id	PS00290
Number of Residues	7
Details	IG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YACEVTH

Chain	Residue	Details
B	TYR191-HIS197
C	TYR208-HIS214

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	44
Details	TRANSMEM: Helical; Name=1 => ECO:0000269|PubMed:23519215, ECO:0000269|PubMed:24357322, ECO:0000269|PubMed:28129538

Chain	Residue	Details
A	ALA57-VAL79
D	ALA57-VAL79

---

site_id	SWS_FT_FI2
Number of Residues	58
Details	TOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:23519215, ECO:0000269|PubMed:24357322, ECO:0000269|PubMed:28129538

Chain	Residue	Details
A	SER80-ASN90
A	ASP152-THR171
D	SER80-ASN90
D	ASP152-THR171

---

site_id	SWS_FT_FI3
Number of Residues	44
Details	TRANSMEM: Helical; Name=2 => ECO:0000269|PubMed:23519215, ECO:0000269|PubMed:24357322, ECO:0000269|PubMed:28129538

Chain	Residue	Details
A	TYR91-LEU113
D	TYR91-LEU113

---

site_id	SWS_FT_FI4
Number of Residues	104
Details	TOPO_DOM: Extracellular => ECO:0000269|PubMed:23519215, ECO:0000269|PubMed:24357322, ECO:0000269|PubMed:28129538

Chain	Residue	Details
A	THR114-PRO129
A	LYS193-ASP216
A	THR346-MET360
D	THR114-PRO129
D	LYS193-ASP216
D	THR346-MET360

---

site_id	SWS_FT_FI5
Number of Residues	42
Details	TRANSMEM: Helical; Name=3 => ECO:0000269|PubMed:23519215, ECO:0000269|PubMed:24357322, ECO:0000269|PubMed:28129538

Chain	Residue	Details
A	ALA130-VAL151
D	ALA130-VAL151

---

site_id	SWS_FT_FI6
Number of Residues	40
Details	TRANSMEM: Helical; Name=4 => ECO:0000269|PubMed:23519215, ECO:0000269|PubMed:24357322, ECO:0000269|PubMed:28129538

Chain	Residue	Details
A	ALA172-ILE192
D	ALA172-ILE192

---

site_id	SWS_FT_FI7
Number of Residues	44
Details	TRANSMEM: Helical; Name=5 => ECO:0000269|PubMed:23519215, ECO:0000269|PubMed:24357322, ECO:0000269|PubMed:28129538

Chain	Residue	Details
A	PHE217-LEU239
D	PHE217-LEU239

---

site_id	SWS_FT_FI8
Number of Residues	40
Details	TRANSMEM: Helical; Name=6 => ECO:0000269|PubMed:23519215, ECO:0000269|PubMed:24357322, ECO:0000269|PubMed:28129538

Chain	Residue	Details
A	VAL325-ILE345
D	VAL325-ILE345

---

site_id	SWS_FT_FI9
Number of Residues	42
Details	TRANSMEM: Helical; Name=7 => ECO:0000269|PubMed:23519215, ECO:0000269|PubMed:24357322, ECO:0000269|PubMed:28129538

Chain	Residue	Details
A	LEU361-LEU382
D	LEU361-LEU382

---

site_id	SWS_FT_FI10
Number of Residues	6
Details	BINDING: BINDING => ECO:0000269|PubMed:23519215, ECO:0007744|PDB:4IB4, ECO:0007744|PDB:4NC3

Chain	Residue	Details
A	ASP135
A	THR140
A	LEU209
D	ASP135
D	THR140
D	LEU209

---

site_id	SWS_FT_FI11
Number of Residues	2
Details	SITE: Hydrophobic barrier that decreases the speed of ligand binding and dissociation => ECO:0000269|PubMed:28129538

Chain	Residue	Details
A	LEU209
D	LEU209

---

site_id	SWS_FT_FI12
Number of Residues	2
Details	LIPID: S-palmitoyl cysteine => ECO:0000255

Chain	Residue	Details
A	CYS397
D	CYS397

---

site_id	SWS_FT_FI13
Number of Residues	4
Details	BINDING: axial binding residue

Chain	Residue	Details
A	TRP1007
A	ILE1102
D	TRP1007
D	ILE1102

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