9LXP

A Cryo-EM structure of LA-PTH-PTH1R-Beta-arrestin1 complex (state 2 conformation)

Functional Information from GO Data

Chain	GOid	namespace	contents
B	0007165	biological_process	signal transduction
L	0005179	molecular_function	hormone activity
L	0005576	cellular_component	extracellular region
L	0030282	biological_process	bone mineralization
R	0004888	molecular_function	transmembrane signaling receptor activity
R	0004930	molecular_function	G protein-coupled receptor activity
R	0004991	molecular_function	parathyroid hormone receptor activity
R	0007166	biological_process	cell surface receptor signaling pathway
R	0007186	biological_process	G protein-coupled receptor signaling pathway
R	0016020	cellular_component	membrane

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
C	TYR204-HIS210
E	TYR193-HIS199

---

site_id	PS00295
Number of Residues	19
Details	ARRESTINS Arrestins signature. FRYGrEDlDVLGLtFrKDL

Chain	Residue	Details
B	PHE61-LEU79

---

site_id	PS00649
Number of Residues	25
Details	G_PROTEIN_RECEP_F2_1 G-protein coupled receptors family 2 signature 1. ClpeWDhil.CWplGapgevvavpCP

Chain	Residue	Details
R	CYS108-PRO132

---

site_id	PS00650
Number of Residues	16
Details	G_PROTEIN_RECEP_F2_2 G-protein coupled receptors family 2 signature 2. QGFFVaIIYCFcNgeV

Chain	Residue	Details
R	GLN451-VAL466

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	41
Details	Region: {"description":"Interaction with CHRM2","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	11
Details	Compositional bias: {"description":"Basic and acidic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"Q8BWG8","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	24
Details	Transmembrane: {"description":"Helical; Name=1","evidences":[{"source":"PubMed","id":"30975883","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6NBF","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6NBH","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6NBI","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	19
Details	Topological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"30975883","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6NBF","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6NBH","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6NBI","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	21
Details	Transmembrane: {"description":"Helical; Name=2","evidences":[{"source":"PubMed","id":"30975883","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6NBF","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6NBH","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6NBI","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI8
Number of Residues	24
Details	Transmembrane: {"description":"Helical; Name=3","evidences":[{"source":"PubMed","id":"30975883","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6NBF","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6NBH","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6NBI","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI9
Number of Residues	21
Details	Transmembrane: {"description":"Helical; Name=4","evidences":[{"source":"PubMed","id":"30975883","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6NBF","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6NBH","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6NBI","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI10
Number of Residues	21
Details	Topological domain: {"description":"Extracellular","evidences":[{"source":"PubMed","id":"30975883","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6NBF","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6NBH","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6NBI","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI11
Number of Residues	24
Details	Transmembrane: {"description":"Helical; Name=5","evidences":[{"source":"PubMed","id":"30975883","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6NBF","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6NBH","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6NBI","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI12
Number of Residues	19
Details	Transmembrane: {"description":"Helical; Name=6","evidences":[{"source":"PubMed","id":"30975883","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6NBF","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6NBH","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6NBI","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI13
Number of Residues	27
Details	Transmembrane: {"description":"Helical; Name=7","evidences":[{"source":"PubMed","id":"30975883","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6NBF","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6NBH","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6NBI","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI14
Number of Residues	2
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---