5UNH: PDB entry 5UNH

Synchrotron structure of human angiotensin II type 2 receptor in complex with compound 2 (N-[(furan-2-yl)methyl]-N-(4-oxo-2-propyl-3-{[2'-(2H-tetrazol-5-yl)[1,1'- biphenyl]-4-yl]methyl}-3,4-dihydroquinazolin-6-yl)benzamide). Determined by X-ray diffraction at 2.9 Å resolution. Released 5 Apr 2017.

Method: X-ray diffraction
Resolution: 2.9 Å
Organisms: Escherichia coli, Homo sapiens
Chains: 2
Atoms: 5,877
Mol. weight: 94.26 kDa
Ligands: 8EM
Released: 5 Apr 2017

Explore 5UNH in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5UNH contains 37 α-helices and 4 β-strands across 2 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, 2 β-strands

Element	Residues	Length	Sheet
α-helix	1004-1019	16
α-helix	1023-1041	19
α-helix	1056-1080	25
α-helix	1084-1105	22
α-helix	40-42	3
α-helix	46-72	27
α-helix	78-94	17
α-helix	97-103	7
α-helix	104-106	3
α-helix	114-147	34
α-helix	163-174	12
α-helix	176-181	6
β-strand	182-187	6	1
β-strand	192-197	6	1
α-helix	201-203	3
α-helix	204-216	13
α-helix	217-221	5
α-helix	222-238	17
α-helix	247-284	38
α-helix	290-314	25
α-helix	315-319	5
α-helix	322-332	11

Chain B: 17 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	1003-1019	17
α-helix	1023-1040	18
α-helix	1057-1080	24
α-helix	1084-1100	17
α-helix	46-69	24
α-helix	78-94	17
α-helix	97-105	9
α-helix	114-147	34
α-helix	163-174	12
α-helix	176-181	6
β-strand	182-187	6	2
β-strand	192-197	6	2
α-helix	205-216	12
α-helix	217-221	5
α-helix	222-239	18
α-helix	246-284	39
α-helix	290-314	25
α-helix	315-319	5
α-helix	322-329	8

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Soluble cytochrome b562,Type-2 angiotensin II receptor	A, B	protein	411	Escherichia coli, Homo sapiens	P0ABE7 (AlphaFold model), P50052 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>5UNH_1 Soluble cytochrome b562,Type-2 angiotensin II receptor (chains A, B)
ADLEDNWETLNDNLKVIEKADNAAQVKDALTKMRAAALDAQKATPPKLEDKSPDSPEMKD
FRHGFDILVGQIDDALKLANEGKVKEAQAAAEQLKTTRNAYIQKYLGSGSCSQKPSDKHL
DAIPILYYIIFVIGFLVNIVVVTLFCCQKGPKKVSSIYIFNLAVADLLLLATLPLWATYY
SYRYDWLFGPVMCKVFGSFLTLNMFASIFFITCMSVDRYQSVIYPFLSQRRNPWQASYIV
PLVWCMACLSSLPTFYFRDVRTIEYLGVNACIMAFPPEKYAQWSAGIALMKNILGFIIPL
IFIATCYFGIRKHLLKTNSYGKNRITRDQVLKMAAAVVLAFIICWLPFHVLTFLDALAWM
GVINSCEVIAVIDLALPFAILLGFTNSCVNPFLYCFVGNRFQQKLRSVFRV

Ligands and cofactors

ID	Name	Formula	Copies
8EM	N-[(furan-2-yl)methyl]-N-(4-oxo-2-propyl-3-{[2'-(2H-tetrazol-5-yl)[1,1'-bipheny…	C37 H31 N7 O3	2

Primary citation

Structural basis for selectivity and diversity in angiotensin II receptors. Zhang, H., Han, G.W., Batyuk, A. et al. Nature (2017) 544:327-332. DOI 10.1038/nature22035 · 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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