Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

6OS1

Structure of synthetic nanobody-stabilized angiotensin II type 1 receptor bound to TRV023

Functional Information from GO Data
ChainGOidnamespacecontents
A0004930molecular_functionG protein-coupled receptor activity
A0004945molecular_functionangiotensin type II receptor activity
A0005506molecular_functioniron ion binding
A0007186biological_processG protein-coupled receptor signaling pathway
A0009055molecular_functionelectron transfer activity
A0016020cellular_componentmembrane
A0019229biological_processregulation of vasoconstriction
A0020037molecular_functionheme binding
A0022900biological_processelectron transport chain
A0042597cellular_componentperiplasmic space
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues2
Detailsbinding site for residue OLC A 1401
ChainResidue
ACYS121
AOLC1406

site_idAC2
Number of Residues5
Detailsbinding site for residue OLC A 1402
ChainResidue
AMET1243
AALA1244
ALEU1247
AASN1294
AOLC1405

site_idAC3
Number of Residues3
Detailsbinding site for residue OLC A 1403
ChainResidue
ALYS1310
ALEU1268
APHE1304

site_idAC4
Number of Residues1
Detailsbinding site for residue OLC A 1404
ChainResidue
ATRP219

site_idAC5
Number of Residues2
Detailsbinding site for residue OLC A 1405
ChainResidue
AGLY194
AOLC1402

site_idAC6
Number of Residues3
Detailsbinding site for residue OLC A 1406
ChainResidue
ATHR120
AILE151
AOLC1401

site_idAC7
Number of Residues2
Detailsbinding site for residue CLR A 1407
ChainResidue
AILE51
ALEU1316

Functional Information from PROSITE/UniProt
site_idPS00237
Number of Residues17
DetailsG_PROTEIN_RECEP_F1_1 G-protein coupled receptors family 1 signature. ASVfLLTCLSIDRYLaI
ChainResidueDetails
AALA114-ILE130

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues29
DetailsTRANSMEM: 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
ChainResidueDetails
ATYR26-PHE55

site_idSWS_FT_FI2
Number of Residues20
DetailsTOPO_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
ChainResidueDetails
ATYR56-THR61
AARG126-THR141

site_idSWS_FT_FI3
Number of Residues27
DetailsTRANSMEM: 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
ChainResidueDetails
AVAL62-ALA89

site_idSWS_FT_FI4
Number of Residues32
DetailsTOPO_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
ChainResidueDetails
AMET90-ASN98
AHIS166-THR190

site_idSWS_FT_FI5
Number of Residues26
DetailsTRANSMEM: 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
ChainResidueDetails
ATYR99-ASP125

site_idSWS_FT_FI6
Number of Residues23
DetailsTRANSMEM: 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
ChainResidueDetails
AMET142-ILE165

site_idSWS_FT_FI7
Number of Residues25
DetailsTRANSMEM: 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
ChainResidueDetails
ALEU191-THR216

site_idSWS_FT_FI8
Number of Residues28
DetailsTRANSMEM: Helical; Name=6 => ECO:0000269|PubMed:25913193, ECO:0000269|PubMed:26420482, ECO:0007744|PDB:4YAY, ECO:0007744|PDB:4ZUD
ChainResidueDetails
ALYS1240-LEU1268

site_idSWS_FT_FI9
Number of Residues9
DetailsTOPO_DOM: Extracellular => ECO:0000269|PubMed:25913193, ECO:0000269|PubMed:26420482, ECO:0007744|PDB:4YAY, ECO:0007744|PDB:4ZUD
ChainResidueDetails
AGLY1269-ASP1278

site_idSWS_FT_FI10
Number of Residues25
DetailsTRANSMEM: Helical; Name=7 => ECO:0000269|PubMed:25913193, ECO:0000269|PubMed:26420482, ECO:0007744|PDB:4YAY, ECO:0007744|PDB:4ZUD
ChainResidueDetails
AILE1279-PHE1304

site_idSWS_FT_FI11
Number of Residues1
DetailsBINDING: BINDING => ECO:0000305|PubMed:30639100, ECO:0007744|PDB:6DO1
ChainResidueDetails
AGLN15

site_idSWS_FT_FI12
Number of Residues6
DetailsBINDING: BINDING => ECO:0000305|PubMed:30639100, ECO:0000305|PubMed:32079768, ECO:0007744|PDB:6DO1, ECO:0007744|PDB:6OS0
ChainResidueDetails
AASP17
AARG167
APHE182
AHIS183
ATYR184
ALYS199

site_idSWS_FT_FI13
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:19139490
ChainResidueDetails
AASN4

site_idSWS_FT_FI14
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:30639100, ECO:0000269|PubMed:32079768, ECO:0007744|PDB:6DO1, ECO:0007744|PDB:6OS0
ChainResidueDetails
AASN176

site_idSWS_FT_FI15
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN188

site_idSWS_FT_FI16
Number of Residues1
DetailsBINDING: axial binding residue
ChainResidueDetails
ATRP232

226707

PDB entries from 2024-10-30

PDB statisticsPDBj update infoContact PDBjnumon