Structure of PDB 6os2 Chain A

Receptor sequence
>6os2A (length=380) Species: 562,9606 [Search protein sequence]
IKRIQDDCPKAGRHNYIFVMIPTLYSIIFVVGIFGNSLVVIVIYFYMKLK
TVASVFLLNLALADLCFLLTLPLWAVYTAMEYRWPFGNYLCKIASASVSF
NLYASVFLLTCLSIDRYLAIVHPMKSRLRRTMLVAKVTCIIIWLLAGLAS
LPAIIHRNVFFIENTNITVCAFHYESQNSTLPIGLGLTKNILGFLFPFLI
ILTSYTLIWKALKKAYDLEDNWETLNDNLKVIEKADNAAQVKDALTKMRA
AALDAQKAHGFDILVGQIDDALKLANEGKVKEAQAAAEQLKKNKPRNDDI
FKIIMAIVLFFFFSWIPHQIFTFLDVLIQLGIIRDCRIADIVDTAMPITI
CIAYFNNCLNPLFYGFLGKKFKRYFLQLLK
3D structure
PDB6os2 Angiotensin and biased analogs induce structurally distinct active conformations within a GPCR.
ChainA
Resolution2.7 Å
3D
structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Enzyme Commision number ?
Interaction with ligand
Site
#
Ligand Ligand
chain
Binding residues on receptor
(original residue number in PDB)
Binding residues on receptor
(residue number reindexed from 1)
Binding affinity
BS01 peptide A Q15 D16 D17 A21 G22 R23 W84 Y87 Y92 R167 A181 F182 H183 Y184 D1263 I1266 D1281 M1284 Q5 D6 D7 A11 G12 R13 W74 Y77 Y82 R157 A171 F172 H173 Y174 D325 I328 D343 M346
BS02 CLR A I43 L1316 I33 L378
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

View graph for
Molecular Function

View graph for
Biological Process

View graph for
Cellular Component
External links
PDB RCSB:6os2, PDBe:6os2, PDBj:6os2
PDBsum6os2
PubMed32079768
UniProtP0ABE7|C562_ECOLX Soluble cytochrome b562 (Gene Name=cybC);
P30556

[Back to BioLiP]