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Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

8W1V

The beta2 adrenergic receptor bound to a bitopic ligand

This is a non-PDB format compatible entry.

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003796	molecular_function	lysozyme activity
A	0009253	biological_process	peptidoglycan catabolic process
A	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
A	0030430	cellular_component	host cell cytoplasm
A	0031640	biological_process	killing of cells of another organism
A	0042742	biological_process	defense response to bacterium
A	0044659	biological_process	viral release from host cell by cytolysis
B	0003796	molecular_function	lysozyme activity
B	0009253	biological_process	peptidoglycan catabolic process
B	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
B	0030430	cellular_component	host cell cytoplasm
B	0031640	biological_process	killing of cells of another organism
B	0042742	biological_process	defense response to bacterium
B	0044659	biological_process	viral release from host cell by cytolysis

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. ASIeTLCVIAVDRYFaI

Chain	Residue	Details
A	ALA119-ILE135

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	140
Details	TOPO_DOM: Extracellular

Chain	Residue	Details
A	MET1-VAL34
A	MET96-CYS106
A	ARG175-ASN196
A	GLN299-LYS305
B	MET1-VAL34
B	MET96-CYS106
B	ARG175-ASN196
B	GLN299-LYS305

site_id	SWS_FT_FI2
Number of Residues	46
Details	TRANSMEM: Helical; Name=1

Chain	Residue	Details
A	GLY35-ILE58
B	GLY35-ILE58

site_id	SWS_FT_FI3
Number of Residues	170
Details	TOPO_DOM: Cytoplasmic

Chain	Residue	Details
A	ALA59-PHE71
A	ASP130-ALA150
A	ARG221-THR274
B	ALA59-PHE71
B	ASP130-ALA150
B	ARG221-THR274

site_id	SWS_FT_FI4
Number of Residues	46
Details	TRANSMEM: Helical; Name=2

Chain	Residue	Details
A	ILE72-LEU95
B	ILE72-LEU95

site_id	SWS_FT_FI5
Number of Residues	44
Details	TRANSMEM: Helical; Name=3

Chain	Residue	Details
A	GLU107-VAL129
B	GLU107-VAL129

site_id	SWS_FT_FI6
Number of Residues	46
Details	TRANSMEM: Helical; Name=4

Chain	Residue	Details
A	ARG151-TYR174
B	ARG151-TYR174

site_id	SWS_FT_FI7
Number of Residues	46
Details	TRANSMEM: Helical; Name=5

Chain	Residue	Details
A	GLN197-SER220
B	GLN197-SER220

site_id	SWS_FT_FI8
Number of Residues	46
Details	TRANSMEM: Helical; Name=6

Chain	Residue	Details
A	LEU275-ILE298
B	LEU275-ILE298

site_id	SWS_FT_FI9
Number of Residues	46
Details	TRANSMEM: Helical; Name=7

Chain	Residue	Details
A	GLU306-SER329
B	GLU306-SER329

site_id	SWS_FT_FI10
Number of Residues	10
Details	BINDING: BINDING => ECO:0000269\|PubMed:18547522, ECO:0007744\|PDB:3D4S

Chain	Residue	Details
A	ASP113
B	TYR316
A	THR118
A	ASN293
A	ASN312
A	TYR316
B	ASP113
B	THR118
B	ASN293
B	ASN312

site_id	SWS_FT_FI11
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269\|PubMed:17952055, ECO:0000269\|PubMed:17962520, ECO:0007744\|PDB:2RH1

Chain	Residue	Details
A	SER203
B	SER203

site_id	SWS_FT_FI12
Number of Residues	2
Details	MOD_RES: Phosphotyrosine => ECO:0000269\|PubMed:8521811

Chain	Residue	Details
A	TYR141
B	TYR141

site_id	SWS_FT_FI13
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:17525332

Chain	Residue	Details
A	SER246
B	SER246

site_id	SWS_FT_FI14
Number of Residues	4
Details	MOD_RES: Phosphoserine; by PKA => ECO:0000255

Chain	Residue	Details
A	SER261
A	SER262
B	SER261
B	SER262

site_id	SWS_FT_FI15
Number of Residues	4
Details	MOD_RES: Phosphoserine; by PKA => ECO:0000269\|PubMed:11146000

Chain	Residue	Details
A	SER981
A	SER982
B	SER981
B	SER982

site_id	SWS_FT_FI16
Number of Residues	4
Details	MOD_RES: Phosphoserine; by BARK => ECO:0000305

Chain	Residue	Details
A	SER991
A	SER992
B	SER991
B	SER992

site_id	SWS_FT_FI17
Number of Residues	2
Details	LIPID: S-palmitoyl cysteine => ECO:0000269\|PubMed:27481942

Chain	Residue	Details
A	CYS265
B	CYS265

site_id	SWS_FT_FI18
Number of Residues	2
Details	LIPID: S-palmitoyl cysteine => ECO:0000269\|PubMed:17962520, ECO:0000269\|PubMed:18547522, ECO:0000269\|PubMed:2540197, ECO:0000269\|PubMed:27481942

Chain	Residue	Details
A	CYS341
B	CYS341

site_id	SWS_FT_FI19
Number of Residues	4
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000305

Chain	Residue	Details
A	ASN6
A	ASN15
B	ASN6
B	ASN15

site_id	SWS_FT_FI20
Number of Residues	2
Details	ACT_SITE: Proton donor/acceptor => ECO:0000255\|HAMAP-Rule:MF_04110, ECO:0000269\|PubMed:3382407, ECO:0000269\|PubMed:7831309, ECO:0000269\|PubMed:8266098

Chain	Residue	Details
A	GLU1011
B	GLU1011

site_id	SWS_FT_FI21
Number of Residues	2
Details	ACT_SITE: Proton donor/acceptor => ECO:0000255\|HAMAP-Rule:MF_04110, ECO:0000269\|PubMed:1892846, ECO:0000269\|PubMed:3382407, ECO:0000269\|PubMed:7831309, ECO:0000269\|PubMed:8266098

Chain	Residue	Details
A	ASP1020
B	ASP1020

site_id	SWS_FT_FI22
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269\|PubMed:8266098

Chain	Residue	Details
A	LEU1032
A	PHE1104
B	LEU1032
B	PHE1104

site_id	SWS_FT_FI23
Number of Residues	4
Details	BINDING: BINDING => ECO:0000303\|PubMed:7831309

Chain	Residue	Details
A	SER1117
A	ASN1132
B	SER1117
B	ASN1132

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	2
Details	M-CSA 921

Chain	Residue	Details
A	GLU1011	proton shuttle (general acid/base)
A	ASP1020	covalent catalysis

site_id	MCSA2
Number of Residues	2
Details	M-CSA 921

Chain	Residue	Details
B	GLU1011	proton shuttle (general acid/base)
B	ASP1020	covalent catalysis

225158

PDB entries from 2024-09-18

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