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4YAY

XFEL structure of human Angiotensin Receptor

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 Residues12
Detailsbinding site for residue ZD7 A 1201
ChainResidue
ATYR35
APHE182
AILE288
ATYR292
ATRP84
ATHR88
ASER105
AVAL108
ASER109
ALEU112
AALA163
AARG167

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 Residues2
DetailsBINDING: axial binding residue
ChainResidueDetails
ATRP1007
AILE1102

site_idSWS_FT_FI2
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_FI3
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_FI4
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_FI5
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_FI6
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_FI7
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_FI8
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_FI9
Number of Residues22
DetailsTOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:25913193, ECO:0000269|PubMed:26420482, ECO:0007744|PDB:4YAY, ECO:0007744|PDB:4ZUD
ChainResidueDetails
ALEU217-PHE239

site_idSWS_FT_FI10
Number of Residues28
DetailsTRANSMEM: Helical; Name=6 => ECO:0000269|PubMed:25913193, ECO:0000269|PubMed:26420482, ECO:0007744|PDB:4YAY, ECO:0007744|PDB:4ZUD
ChainResidueDetails
ALYS240-LEU268

site_idSWS_FT_FI11
Number of Residues9
DetailsTOPO_DOM: Extracellular => ECO:0000269|PubMed:25913193, ECO:0000269|PubMed:26420482, ECO:0007744|PDB:4YAY, ECO:0007744|PDB:4ZUD
ChainResidueDetails
AGLY269-ASP278

site_idSWS_FT_FI12
Number of Residues25
DetailsTRANSMEM: Helical; Name=7 => ECO:0000269|PubMed:25913193, ECO:0000269|PubMed:26420482, ECO:0007744|PDB:4YAY, ECO:0007744|PDB:4ZUD
ChainResidueDetails
AILE279-PHE304

site_idSWS_FT_FI13
Number of Residues1
DetailsBINDING: BINDING => ECO:0000305|PubMed:30639100, ECO:0007744|PDB:6DO1
ChainResidueDetails
ASER15

site_idSWS_FT_FI14
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_FI15
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:19139490
ChainResidueDetails
AASN14

site_idSWS_FT_FI16
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_FI17
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN188

218853

PDB entries from 2024-04-24

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