Structure of PDB 6os2 Chain A Binding Site BS01
Receptor Information
>6os2 Chain A (length=380) Species:
562,9606
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IKRIQDDCPKAGRHNYIFVMIPTLYSIIFVVGIFGNSLVVIVIYFYMKLK
TVASVFLLNLALADLCFLLTLPLWAVYTAMEYRWPFGNYLCKIASASVSF
NLYASVFLLTCLSIDRYLAIVHPMKSRLRRTMLVAKVTCIIIWLLAGLAS
LPAIIHRNVFFIENTNITVCAFHYESQNSTLPIGLGLTKNILGFLFPFLI
ILTSYTLIWKALKKAYDLEDNWETLNDNLKVIEKADNAAQVKDALTKMRA
AALDAQKAHGFDILVGQIDDALKLANEGKVKEAQAAAEQLKKNKPRNDDI
FKIIMAIVLFFFFSWIPHQIFTFLDVLIQLGIIRDCRIADIVDTAMPITI
CIAYFNNCLNPLFYGFLGKKFKRYFLQLLK
Ligand information
>6os2 Chain B (length=7) Species:
32630
(synthetic construct) [
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GRVYYHP
Receptor-Ligand Complex Structure
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PDB
6os2
Angiotensin and biased analogs induce structurally distinct active conformations within a GPCR.
Resolution
2.7 Å
Binding residue
(original residue number in PDB)
Q15 D16 D17 A21 G22 R23 W84 Y87 Y92 R167 A181 F182 H183 Y184 D1263 I1266 D1281 M1284
Binding residue
(residue number reindexed from 1)
Q5 D6 D7 A11 G12 R13 W74 Y77 Y82 R157 A171 F172 H173 Y174 D325 I328 D343 M346
Enzymatic activity
Enzyme Commision number
?
Gene Ontology
Molecular Function
GO:0004930
G protein-coupled receptor activity
GO:0004945
angiotensin type II receptor activity
GO:0005506
iron ion binding
GO:0009055
electron transfer activity
GO:0020037
heme binding
GO:0046872
metal ion binding
Biological Process
GO:0007186
G protein-coupled receptor signaling pathway
GO:0019229
regulation of vasoconstriction
GO:0022900
electron transport chain
Cellular Component
GO:0016020
membrane
GO:0042597
periplasmic space
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Molecular Function
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Cellular Component
External links
PDB
RCSB:6os2
,
PDBe:6os2
,
PDBj:6os2
PDBsum
6os2
PubMed
32079768
UniProt
P0ABE7
|C562_ECOLX Soluble cytochrome b562 (Gene Name=cybC);
P30556
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