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Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

9EAH

Structure of nanobody AT209 in complex with the olmesartan-bound angiotensin II type I receptor (AT1R)

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0042597	cellular_component	periplasmic space
A	0046872	molecular_function	metal ion binding
B	0042597	cellular_component	periplasmic space
B	0046872	molecular_function	metal ion binding

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. ASVfLLTCLSIDRYLaI

Chain	Residue	Details
A	ALA114-ILE130

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

Chain	Residue	Details
C	TYR208-HIS214
D	TYR194-HIS200

site_id	PS00324
Number of Residues	9
Details	ASPARTOKINASE Aspartokinase signature. LlKYGGSSL

Chain	Residue	Details
A	LEU1316-LEU1324

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	58
Details	TRANSMEM: Helical; Name=1 => ECO:0000269\|PubMed:25913193, ECO:0000269\|PubMed:26420482, ECO:0000269\|PubMed:30639100, ECO:0000269\|PubMed:32079768, ECO:0007744\|PDB:4YAY, ECO:0007744\|PDB:4ZUD, ECO:0007744\|PDB:6DO1, ECO:0007744\|PDB:6OS0, ECO:0007744\|PDB:6OS1, ECO:0007744\|PDB:6OS2

Chain	Residue	Details
A	TYR26-PHE55
B	TYR159-PHE188

site_id	SWS_FT_FI2
Number of Residues	40
Details	TOPO_DOM: Cytoplasmic => ECO:0000269\|PubMed:25913193, ECO:0000269\|PubMed:26420482, ECO:0000269\|PubMed:30639100, ECO:0000269\|PubMed:32079768, ECO:0007744\|PDB:4YAY, ECO:0007744\|PDB:4ZUD, ECO:0007744\|PDB:6DO1, ECO:0007744\|PDB:6OS0, ECO:0007744\|PDB:6OS1, ECO:0007744\|PDB:6OS2

Chain	Residue	Details
A	TYR56-THR61
A	ARG126-THR141
B	TYR189-THR194
B	ARG259-THR274

site_id	SWS_FT_FI3
Number of Residues	54
Details	TRANSMEM: Helical; Name=2 => ECO:0000269\|PubMed:25913193, ECO:0000269\|PubMed:26420482, ECO:0000269\|PubMed:30639100, ECO:0000269\|PubMed:32079768, ECO:0007744\|PDB:4YAY, ECO:0007744\|PDB:4ZUD, ECO:0007744\|PDB:6DO1, ECO:0007744\|PDB:6OS0, ECO:0007744\|PDB:6OS1, ECO:0007744\|PDB:6OS2

Chain	Residue	Details
A	VAL62-ALA89
B	VAL195-ALA222

site_id	SWS_FT_FI4
Number of Residues	64
Details	TOPO_DOM: Extracellular => ECO:0000269\|PubMed:25913193, ECO:0000269\|PubMed:26420482, ECO:0000269\|PubMed:30639100, ECO:0000269\|PubMed:32079768, ECO:0007744\|PDB:4YAY, ECO:0007744\|PDB:4ZUD, ECO:0007744\|PDB:6DO1, ECO:0007744\|PDB:6OS0, ECO:0007744\|PDB:6OS1, ECO:0007744\|PDB:6OS2

Chain	Residue	Details
A	MET90-ASN98
A	HIS166-THR190
B	MET223-ASN231
B	HIS299-THR323

site_id	SWS_FT_FI5
Number of Residues	52
Details	TRANSMEM: Helical; Name=3 => ECO:0000269\|PubMed:25913193, ECO:0000269\|PubMed:26420482, ECO:0000269\|PubMed:30639100, ECO:0000269\|PubMed:32079768, ECO:0007744\|PDB:4YAY, ECO:0007744\|PDB:4ZUD, ECO:0007744\|PDB:6DO1, ECO:0007744\|PDB:6OS0, ECO:0007744\|PDB:6OS1, ECO:0007744\|PDB:6OS2

Chain	Residue	Details
A	TYR99-ASP125
B	TYR232-ASP258

site_id	SWS_FT_FI6
Number of Residues	46
Details	TRANSMEM: Helical; Name=4 => ECO:0000269\|PubMed:25913193, ECO:0000269\|PubMed:26420482, ECO:0000269\|PubMed:30639100, ECO:0000269\|PubMed:32079768, ECO:0007744\|PDB:4YAY, ECO:0007744\|PDB:4ZUD, ECO:0007744\|PDB:6DO1, ECO:0007744\|PDB:6OS0, ECO:0007744\|PDB:6OS1, ECO:0007744\|PDB:6OS2

Chain	Residue	Details
A	MET142-ILE165
B	MET275-ILE298

site_id	SWS_FT_FI7
Number of Residues	50
Details	TRANSMEM: Helical; Name=5 => ECO:0000269\|PubMed:25913193, ECO:0000269\|PubMed:26420482, ECO:0000269\|PubMed:30639100, ECO:0000269\|PubMed:32079768, ECO:0007744\|PDB:4YAY, ECO:0007744\|PDB:4ZUD, ECO:0007744\|PDB:6DO1, ECO:0007744\|PDB:6OS0, ECO:0007744\|PDB:6OS1, ECO:0007744\|PDB:6OS2

Chain	Residue	Details
A	LEU191-THR216
B	LEU324-THR349

site_id	SWS_FT_FI8
Number of Residues	56
Details	TRANSMEM: Helical; Name=6 => ECO:0000269\|PubMed:25913193, ECO:0000269\|PubMed:26420482, ECO:0007744\|PDB:4YAY, ECO:0007744\|PDB:4ZUD

Chain	Residue	Details
A	LYS1240-LEU1268
B	LYS480-LEU508

site_id	SWS_FT_FI9
Number of Residues	18
Details	TOPO_DOM: Extracellular => ECO:0000269\|PubMed:25913193, ECO:0000269\|PubMed:26420482, ECO:0007744\|PDB:4YAY, ECO:0007744\|PDB:4ZUD

Chain	Residue	Details
A	GLY1269-ASP1278
B	GLY509-ASP518

site_id	SWS_FT_FI10
Number of Residues	50
Details	TRANSMEM: Helical; Name=7 => ECO:0000269\|PubMed:25913193, ECO:0000269\|PubMed:26420482, ECO:0007744\|PDB:4YAY, ECO:0007744\|PDB:4ZUD

Chain	Residue	Details
A	ILE1279-PHE1304
B	ILE519-PHE544

site_id	SWS_FT_FI11
Number of Residues	2
Details	BINDING: BINDING => ECO:0000305\|PubMed:30639100, ECO:0007744\|PDB:6DO1

Chain	Residue	Details
A	GLN15
B	GLN148

site_id	SWS_FT_FI12
Number of Residues	12
Details	BINDING: BINDING => ECO:0000305\|PubMed:30639100, ECO:0000305\|PubMed:32079768, ECO:0007744\|PDB:6DO1, ECO:0007744\|PDB:6OS0

Chain	Residue	Details
A	ASP17
B	HIS316
B	TYR317
B	LYS332
A	ARG167
A	PHE182
A	HIS183
A	TYR184
A	LYS199
B	ASP150
B	ARG300
B	PHE315

site_id	SWS_FT_FI13
Number of Residues	2
Details	CARBOHYD: N-linked (GlcNAc...) (complex) asparagine => ECO:0000269\|PubMed:19139490

Chain	Residue	Details
A	ASN4
B	ASN137

site_id	SWS_FT_FI14
Number of Residues	2
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269\|PubMed:30639100, ECO:0000269\|PubMed:32079768, ECO:0007744\|PDB:6DO1, ECO:0007744\|PDB:6OS0

Chain	Residue	Details
A	ASN176
B	ASN309

site_id	SWS_FT_FI15
Number of Residues	2
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255

Chain	Residue	Details
A	ASN188
B	ASN321

site_id	SWS_FT_FI16
Number of Residues	4
Details	BINDING: axial binding residue

Chain	Residue	Details
A	TRP232
A	ILE327
B	TRP365
B	ILE460

237735

PDB entries from 2025-06-18

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