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Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4LDL

Structure of beta2 adrenoceptor bound to hydroxybenzylisoproterenol and an engineered nanobody

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003796	molecular_function	lysozyme activity
A	0003824	molecular_function	catalytic activity
A	0004930	molecular_function	G protein-coupled receptor activity
A	0004941	molecular_function	beta2-adrenergic receptor activity
A	0006940	biological_process	regulation of smooth muscle contraction
A	0007186	biological_process	G protein-coupled receptor signaling pathway
A	0007189	biological_process	adenylate cyclase-activating G protein-coupled receptor signaling pathway
A	0008152	biological_process	metabolic process
A	0009253	biological_process	peptidoglycan catabolic process
A	0016020	cellular_component	membrane
A	0016787	molecular_function	hydrolase activity
A	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
A	0016998	biological_process	cell wall macromolecule catabolic process
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
A	0097746	biological_process	blood vessel diameter maintenance

Functional Information from PDB Data

site_id	AC1
Number of Residues	11
Details	BINDING SITE FOR RESIDUE XQC A 1401

Chain	Residue
A	ASP1113
A	ASN1312
A	TYR1316
A	CYS1191
A	ASP1192
A	PHE1193
A	SER1203
A	SER1207
A	PHE1289
A	ASN1293
A	ILE1309

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE NA A 1402

Chain	Residue
A	ASN1103
A	CYS1184
A	TYR1185
A	GLU1187
A	CYS1190
A	HOH1501

site_id	AC3
Number of Residues	2
Details	BINDING SITE FOR RESIDUE 1WV A 1403

Chain	Residue
A	GLU1306
A	TRP1313

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	ALA1119-ILE1135

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
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	GLU876

site_id	SWS_FT_FI2
Number of Residues	1
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	ASP885

site_id	SWS_FT_FI3
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269\|PubMed:8266098

Chain	Residue	Details
A	LEU897
A	PHE969

site_id	SWS_FT_FI4
Number of Residues	2
Details	BINDING: BINDING => ECO:0000303\|PubMed:7831309

Chain	Residue	Details
A	SER982
A	ASN997

site_id	SWS_FT_FI5
Number of Residues	23
Details	TRANSMEM: Helical; Name=1

Chain	Residue	Details
A	GLY1035-ILE1058

site_id	SWS_FT_FI6
Number of Residues	85
Details	TOPO_DOM: Cytoplasmic

Chain	Residue	Details
A	ALA1059-PHE1071
A	ASP1130-ALA1150
A	ARG1221-LEU1302

site_id	SWS_FT_FI7
Number of Residues	23
Details	TRANSMEM: Helical; Name=2

Chain	Residue	Details
A	ILE1072-LEU1095

site_id	SWS_FT_FI8
Number of Residues	37
Details	TOPO_DOM: Extracellular

Chain	Residue	Details
A	THR1096-CYS1106
A	ARG1175-ASN1196
A	GLN1299-LYS1305

site_id	SWS_FT_FI9
Number of Residues	22
Details	TRANSMEM: Helical; Name=3

Chain	Residue	Details
A	GLU1107-VAL1129

site_id	SWS_FT_FI10
Number of Residues	23
Details	TRANSMEM: Helical; Name=4

Chain	Residue	Details
A	ARG1151-TYR1174

site_id	SWS_FT_FI11
Number of Residues	23
Details	TRANSMEM: Helical; Name=5

Chain	Residue	Details
A	GLN1197-SER1220

site_id	SWS_FT_FI12
Number of Residues	23
Details	TRANSMEM: Helical; Name=6

Chain	Residue	Details
A	LEU1275-ILE1298

site_id	SWS_FT_FI13
Number of Residues	23
Details	TRANSMEM: Helical; Name=7

Chain	Residue	Details
A	GLU1306-SER1329

site_id	SWS_FT_FI14
Number of Residues	5
Details	BINDING: BINDING => ECO:0000269\|PubMed:18547522, ECO:0007744\|PDB:3D4S

Chain	Residue	Details
A	ASP1113
A	THR1118
A	ASN1293
A	ASN1312
A	TYR1316

site_id	SWS_FT_FI15
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269\|PubMed:17952055, ECO:0000269\|PubMed:17962520, ECO:0007744\|PDB:2RH1

Chain	Residue	Details
A	SER1203

site_id	SWS_FT_FI16
Number of Residues	1
Details	MOD_RES: Phosphotyrosine => ECO:0000269\|PubMed:8521811

Chain	Residue	Details
A	TYR1141

site_id	SWS_FT_FI17
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:17525332

Chain	Residue	Details
A	THR1274

site_id	SWS_FT_FI18
Number of Residues	2
Details	MOD_RES: Phosphoserine; by PKA => ECO:0000255

Chain	Residue	Details
A	PHE1289
A	PHE1290

site_id	SWS_FT_FI19
Number of Residues	2
Details	MOD_RES: Phosphoserine; by PKA => ECO:0000269\|PubMed:11146000

Chain	Residue	Details
A	SER1345
A	SER1346

site_id	SWS_FT_FI20
Number of Residues	1
Details	LIPID: S-palmitoyl cysteine => ECO:0000269\|PubMed:27481942

Chain	Residue	Details
A	ALA1265

site_id	SWS_FT_FI21
Number of Residues	1
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	CYS1341

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	2
Details	M-CSA 921

Chain	Residue	Details
A	GLU876	proton shuttle (general acid/base)
A	ASP885	covalent catalysis

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PDB entries from 2024-04-24

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