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5XJM

Complex structure of angiotensin II type 2 receptor with Fab

Functional Information from GO Data
ChainGOidnamespacecontents
A0004930molecular_functionG protein-coupled receptor activity
A0004945molecular_functionangiotensin type II receptor activity
A0005506molecular_functioniron ion binding
A0006954biological_processinflammatory response
A0007186biological_processG protein-coupled receptor signaling pathway
A0009055molecular_functionelectron transfer activity
A0016020cellular_componentmembrane
A0020037molecular_functionheme binding
A0022900biological_processelectron transport chain
A0042597cellular_componentperiplasmic space
A0042981biological_processregulation of apoptotic process
A0046872molecular_functionmetal ion binding
A0097746biological_processblood vessel diameter maintenance
Functional Information from PROSITE/UniProt
site_idPS00290
Number of Residues7
DetailsIG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YTCEATH
ChainResidueDetails
LTYR191-HIS197

site_idPS00237
Number of Residues17
DetailsG_PROTEIN_RECEP_F1_1 G-protein coupled receptors family 1 signature. ASIfFITCMSVDRYQsV
ChainResidueDetails
AALA130-VAL146

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
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
AALA46-CYS70

site_idSWS_FT_FI2
Number of Residues27
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
ACYS71-SER80
AASP141-GLN159

site_idSWS_FT_FI3
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
AILE81-TYR104

site_idSWS_FT_FI4
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
ASER105-PRO114
AARG182-GLN206
AALA282-ALA294

site_idSWS_FT_FI5
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
AVAL115-VAL140

site_idSWS_FT_FI6
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
AALA160-PHE181

site_idSWS_FT_FI7
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
ATRP207-PHE232

site_idSWS_FT_FI8
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
AALA258-LEU281

site_idSWS_FT_FI9
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
AVAL295-PHE320

site_idSWS_FT_FI10
Number of Residues4
DetailsBINDING: BINDING => ECO:0000305|PubMed:31899086, ECO:0007744|PDB:6JOD
ChainResidueDetails
ATYR103
ATYR104
AARG182
ATYR204

site_idSWS_FT_FI11
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:29967536, ECO:0000305|PubMed:31899086, ECO:0007744|PDB:5XJM, ECO:0007744|PDB:6JOD
ChainResidueDetails
ALYS215
AASP279

site_idSWS_FT_FI12
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:29967536, ECO:0007744|PDB:5XJM
ChainResidueDetails
AASP297

site_idSWS_FT_FI13
Number of Residues2
DetailsBINDING: axial binding residue
ChainResidueDetails
ATRP1007
AILE1102

219140

PDB entries from 2024-05-01

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