6OS0: PDB entry 6OS0

Structure of synthetic nanobody-stabilized angiotensin II type 1 receptor bound to angiotensin II. Determined by X-ray diffraction at 2.9 Å resolution. Released 19 Feb 2020.

Method: X-ray diffraction
Resolution: 2.9 Å
Organisms: Homo sapiens, Escherichia coli, synthetic construct
Chains: 3
Atoms: 4,139
Mol. weight: 63.57 kDa
Ligands: NAG
Released: 19 Feb 2020

Explore 6OS0 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6OS0 contains 21 α-helices and 16 β-strands across 3 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 20 helices, 3 β-strands

Element	Residues	Length	Sheet
β-strand	12-14	3	1
α-helix	30-51	22
α-helix	52-56	5
α-helix	62-79	18
α-helix	81-89	9
α-helix	97-131	35
α-helix	135-139	5
α-helix	142-159	18
α-helix	161-165	5
β-strand	167-172	6	1
β-strand	178-184	7	1
α-helix	194-200	7
α-helix	201-205	5
α-helix	206-243	38
α-helix	248-267	20
α-helix	282-306	25
α-helix	309-317	9
α-helix	318-321	4
α-helix	1228-1233	6
α-helix	1238-1267	30
α-helix	1274-1296	23
α-helix	1298-1304	7
α-helix	1307-1315	9

Chain B: 0 helices, 1 β-strand

Element	Residues	Length	Sheet
β-strand	2-4	3	1

Chain D: 1 helix, 12 β-strands

Element	Residues	Length	Sheet
β-strand	3-7	5	2
β-strand	12-13	2	3
β-strand	17-25	9	2
β-strand	33-39	7	4
β-strand	45-52	8	4
β-strand	57-59	3	4
β-strand	67-72	6	2
β-strand	77-83	7	2
α-helix	87-89	3
β-strand	91-98	8	4
β-strand	114-115	2	4
β-strand	120-122	3	4
β-strand	124-125	2	3

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Type-1 angiotensin II receptor,Soluble cytochrome b562 BRIL fusion protein	A	protein	425	Homo sapiens, Escherichia coli	P0ABE7 (AlphaFold model), P30556 (AlphaFold model)
Nanobody Nb.AT110i1	D	protein	126	synthetic construct
Angiotensinogen	B	protein	8	Homo sapiens	P01019 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>6OS0_1 Type-1 angiotensin II receptor,Soluble cytochrome b562 BRIL fusion protein (chains A)
DYKDDDDKILNSSTEDGIKRIQDDCPKAGRHNYIFVMIPTLYSIIFVVGIFGNSLVVIVI
YFYMKLKTVASVFLLNLALADLCFLLTLPLWAVYTAMEYRWPFGNYLCKIASASVSFNLY
ASVFLLTCLSIDRYLAIVHPMKSRLRRTMLVAKVTCIIIWLLAGLASLPAIIHRNVFFIE
NTNITVCAFHYESQNSTLPIGLGLTKNILGFLFPFLIILTSYTLIWKALKKAYDLEDNWE
TLNDNLKVIEKADNAAQVKDALTKMRAAALDAQKATPPKLEDKSPDSPEMKDFRHGFDIL
VGQIDDALKLANEGKVKEAQAAAEQLKTTRNAEIQKNKPRNDDIFKIIMAIVLFFFFSWI
PHQIFTFLDVLIQLGIIRDCRIADIVDTAMPITICIAYFNNCLNPLFYGFLGKKFKRYFL
QLLKY

Sequence of entity 2 (D), FASTA

>6OS0_2 Nanobody Nb.AT110i1 (chains D)
QVQLQESGGGLVQAGGSLRLSCAASGNIFDVDIMGWYRQAPGKERELVASITDGGSTDYA
DSVKGRFTISRDNAKNTVYLQMNSLKPEDTAVYYCAAVAYPDIPTYFDYDSDNFYWGQGT
QVTVSS

Sequence of entity 3 (B), FASTA

>6OS0_3 Angiotensinogen (chains B)
DRVYIHPF

Ligands and cofactors

ID	Name	Formula	Copies
NAG	2-acetamido-2-deoxy-beta-D-glucopyranose	C8 H15 N O6	1

Water and common crystallization additives (CL) are not listed.

Primary citation

Angiotensin and biased analogs induce structurally distinct active conformations within a GPCR. Wingler, L.M., Skiba, M.A., McMahon, C. et al. Science (2020) 367:888-892. DOI 10.1126/science.aay9813 · PubMed

Other PDB entries of the same protein (UniProt P0ABE7 (AlphaFold model), which also has an AlphaFold model), best resolution first:

6DYF 1.1 Å, Cu(II)-bound structure of the engineered cyt cb562 variant, CH3Y
5YO6 1.2 Å, Crystal Structure of B562RIL with engineered disulfide bond T9C-A36C
4JEA 1.22 Å, Crystal structure of an engineered Zn-RIDC1 construct with four interfacial disulfide…
7LSJ 1.26 Å, Cu-bound crystal structure of the engineered cyt cb562 variant, DiCyt2 - H63A,…
7MK4 1.27 Å, Co-bound crystal structure of the engineered cyt cb562 variant, DiCyt2
6DYC 1.33 Å, Co(II)-bound structure of the engineered cyt cb562 variant, CH3
5YO4 1.37 Å, Crystal Structure of B562RIL with engineered disulfide bond K27C-A79C
256B 1.4 Å, Improvement of the 2.5 Å resolution model of cytochrome B562 by redetermining the…
6OT4 1.4 Å, Bimetallic dodecameric cage design 2 (BMC2) from cytochrome cb562
7LRV 1.4 Å, Ni-bound crystal structure of the engineered cyt cb562 variant, DiCyt2, crystallized in…
9PQ4 1.48 Å, Bi-bound structure of the H77C variant of TriCyt2
6DYG 1.49 Å, Fe(II)-bound structure of the engineered cyt cb562 variant, CH3Y

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