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5UNG

XFEL structure of human angiotensin II type 2 receptor (Orthorhombic form) in complex with compound 1 (N-benzyl-N-(2-ethyl-4-oxo-3-{[2'-(2H-tetrazol-5-yl)[1,1'-biphenyl]-4-yl] methyl}-3,4-dihydroquinazolin-6-yl)thiophene-2-carboxamide)

Functional Information from GO Data
ChainGOidnamespacecontents
B0004930molecular_functionG protein-coupled receptor activity
B0004945molecular_functionangiotensin type II receptor activity
B0005506molecular_functioniron ion binding
B0006954biological_processinflammatory response
B0007186biological_processG protein-coupled receptor signaling pathway
B0009055molecular_functionelectron transfer activity
B0016020cellular_componentmembrane
B0020037molecular_functionheme binding
B0022900biological_processelectron transport chain
B0042597cellular_componentperiplasmic space
B0042981biological_processregulation of apoptotic process
B0046872molecular_functionmetal ion binding
B0097746biological_processblood vessel diameter maintenance
Functional Information from PDB Data
site_idAC1
Number of Residues14
Detailsbinding site for residue 8ES B 1201
ChainResidue
BTYR51
BLYS215
BTRP269
BPHE272
BILE304
BPHE308
BTRP100
BTYR103
BLEU124
BTHR125
BMET128
BPHE129
BTHR178
BARG182

site_idAC2
Number of Residues6
Detailsbinding site for residue OLC B 1202
ChainResidue
BPRO48
BTYR52
BTHR102
BSER105
BALA228
BTHR229

Functional Information from PROSITE/UniProt
site_idPS00237
Number of Residues17
DetailsG_PROTEIN_RECEP_F1_1 G-protein coupled receptors family 1 signature. ASIfFITCMSVDRYQsV
ChainResidueDetails
BALA130-VAL146

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: axial binding residue
ChainResidueDetails
BTRP1007
BILE1102

site_idSWS_FT_FI2
Number of Residues24
DetailsTRANSMEM: Helical; Name=1 => ECO:0000269|PubMed:28379944, ECO:0000269|PubMed:29967536, ECO:0000269|PubMed:31899086, ECO:0000269|PubMed:32669569, ECO:0007744|PDB:5UNF, ECO:0007744|PDB:5UNG, ECO:0007744|PDB:5UNH, ECO:0007744|PDB:5XJM, ECO:0007744|PDB:6JOD, ECO:0007744|PDB:7C6A
ChainResidueDetails
BALA46-CYS70

site_idSWS_FT_FI3
Number of Residues51
DetailsTOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:28379944, ECO:0000269|PubMed:29967536, ECO:0000269|PubMed:31899086, ECO:0000269|PubMed:32669569, ECO:0007744|PDB:5UNF, ECO:0007744|PDB:5UNG, ECO:0007744|PDB:5UNH, ECO:0007744|PDB:5XJM, ECO:0007744|PDB:6JOD, ECO:0007744|PDB:7C6A
ChainResidueDetails
BCYS71-SER80
BASP141-GLN159
BGLY233-MET257

site_idSWS_FT_FI4
Number of Residues23
DetailsTRANSMEM: Helical; Name=2 => ECO:0000269|PubMed:28379944, ECO:0000269|PubMed:29967536, ECO:0000269|PubMed:31899086, ECO:0000269|PubMed:32669569, ECO:0007744|PDB:5UNF, ECO:0007744|PDB:5UNG, ECO:0007744|PDB:5UNH, ECO:0007744|PDB:5XJM, ECO:0007744|PDB:6JOD, ECO:0007744|PDB:7C6A
ChainResidueDetails
BILE81-TYR104

site_idSWS_FT_FI5
Number of Residues45
DetailsTOPO_DOM: Extracellular => ECO:0000269|PubMed:28379944, ECO:0000269|PubMed:29967536, ECO:0000269|PubMed:31899086, ECO:0000269|PubMed:32669569, ECO:0007744|PDB:5UNF, ECO:0007744|PDB:5UNG, ECO:0007744|PDB:5UNH, ECO:0007744|PDB:5XJM, ECO:0007744|PDB:6JOD, ECO:0007744|PDB:7C6A
ChainResidueDetails
BSER105-PRO114
BARG182-GLN206
BALA282-ALA294

site_idSWS_FT_FI6
Number of Residues25
DetailsTRANSMEM: Helical; Name=3 => ECO:0000269|PubMed:28379944, ECO:0000269|PubMed:29967536, ECO:0000269|PubMed:31899086, ECO:0000269|PubMed:32669569, ECO:0007744|PDB:5UNF, ECO:0007744|PDB:5UNG, ECO:0007744|PDB:5UNH, ECO:0007744|PDB:5XJM, ECO:0007744|PDB:6JOD, ECO:0007744|PDB:7C6A
ChainResidueDetails
BVAL115-VAL140

site_idSWS_FT_FI7
Number of Residues21
DetailsTRANSMEM: Helical; Name=4 => ECO:0000269|PubMed:28379944, ECO:0000269|PubMed:29967536, ECO:0000269|PubMed:31899086, ECO:0000269|PubMed:32669569, ECO:0007744|PDB:5UNF, ECO:0007744|PDB:5UNG, ECO:0007744|PDB:5UNH, ECO:0007744|PDB:5XJM, ECO:0007744|PDB:6JOD, ECO:0007744|PDB:7C6A
ChainResidueDetails
BALA160-PHE181

site_idSWS_FT_FI8
Number of Residues25
DetailsTRANSMEM: Helical; Name=5 => ECO:0000269|PubMed:28379944, ECO:0000269|PubMed:29967536, ECO:0000269|PubMed:31899086, ECO:0000269|PubMed:32669569, ECO:0007744|PDB:5UNF, ECO:0007744|PDB:5UNG, ECO:0007744|PDB:5UNH, ECO:0007744|PDB:5XJM, ECO:0007744|PDB:6JOD, ECO:0007744|PDB:7C6A
ChainResidueDetails
BTRP207-PHE232

site_idSWS_FT_FI9
Number of Residues23
DetailsTRANSMEM: Helical; Name=6 => ECO:0000269|PubMed:28379944, ECO:0000269|PubMed:29967536, ECO:0000269|PubMed:31899086, ECO:0000269|PubMed:32669569, ECO:0007744|PDB:5UNF, ECO:0007744|PDB:5UNG, ECO:0007744|PDB:5UNH, ECO:0007744|PDB:5XJM, ECO:0007744|PDB:6JOD, ECO:0007744|PDB:7C6A
ChainResidueDetails
BALA258-LEU281

site_idSWS_FT_FI10
Number of Residues25
DetailsTRANSMEM: Helical; Name=7 => ECO:0000269|PubMed:28379944, ECO:0000269|PubMed:29967536, ECO:0000269|PubMed:31899086, ECO:0000269|PubMed:32669569, ECO:0007744|PDB:5UNF, ECO:0007744|PDB:5UNG, ECO:0007744|PDB:5UNH, ECO:0007744|PDB:5XJM, ECO:0007744|PDB:6JOD, ECO:0007744|PDB:7C6A
ChainResidueDetails
BVAL295-PHE320

site_idSWS_FT_FI11
Number of Residues4
DetailsBINDING: BINDING => ECO:0000305|PubMed:31899086, ECO:0007744|PDB:6JOD
ChainResidueDetails
BTYR103
BTYR104
BARG182
BTYR204

site_idSWS_FT_FI12
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:29967536, ECO:0000305|PubMed:31899086, ECO:0007744|PDB:5XJM, ECO:0007744|PDB:6JOD
ChainResidueDetails
BLYS215
BASP279

site_idSWS_FT_FI13
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:29967536, ECO:0007744|PDB:5XJM
ChainResidueDetails
BASP297

218853

PDB entries from 2024-04-24

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