5UNG: PDB entry 5UNG

XFEL structure of human angiotensin II type 2 receptor (Orthorhombic form) in complex with compound 1 (N-benzyl-N-(2-ethyl-4-oxo-3-{[2'-(2H-tetrazol-5-yl)[1,1'-biphenyl]-4-yl] methyl}-3,4-dihydroquinazolin-6-yl)thiophene-2-carboxamide). Determined by X-ray diffraction at 2.8 Å resolution. Released 5 Apr 2017.

Method: X-ray diffraction
Resolution: 2.8 Å
Organisms: Escherichia coli, Homo sapiens
Chains: 1
Atoms: 3,266
Mol. weight: 47.77 kDa
Ligands: OLA, OLC, 8ES
Released: 5 Apr 2017

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

Secondary structure: helices and β-sheets

5UNG contains 23 α-helices and 2 β-strands across 1 chain. 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 B: 23 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	1003-1019	17
α-helix	1023-1042	20
α-helix	1056-1080	25
α-helix	1084-1090	7
α-helix	1091-1093	3
α-helix	1094-1104	11
α-helix	46-68	23
α-helix	69-73	5
α-helix	78-94	17
α-helix	97-105	9
α-helix	114-147	34
α-helix	149-151	3
α-helix	160-174	15
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	222-239	18
α-helix	246-284	39
α-helix	290-315	26
α-helix	316-320	5
α-helix	321-323	3
α-helix	325-333	9

Molecules and chains

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

Sequence of entity 1 (B), FASTA

>5UNG_1 Chimera protein of Type-2 angiotensin II receptor and Soluble cytochrome b562 (chains B)
ADLEDNWETLNDNLKVIEKADNAAQVKDALTKMRAAALDAQKATPPKLEDKSPDSPEMKD
FRHGFDILVGQIDDALKLANEGKVKEAQAAAEQLKTTRNAYIQKYLGSGSCSQKPSDKHL
DAIPILYYIIFVIGFLVNIVVVTLFCCQKGPKKVSSIYIFNLAVADLLLLATLPLWATYY
SYRYDWLFGPVMCKVFGSFLTLNMFASIFFITCMSVDRYQSVIYPFLSQRRNPWQASYIV
PLVWCMACLSSLPTFYFRDVRTIEYLGVNACIMAFPPEKYAQWSAGIALMKNILGFIIPL
IFIATCYFGIRKHLLKTNSYGKNRITRDQVLKMAAAVVLAFIICWLPFHVLTFLDALAWM
GVINSCEVIAVIDLALPFAILLGFTNSCVNPFLYCFVGNRFQQKLRSVFRV

Ligands and cofactors

ID	Name	Formula	Copies
OLA	Oleic acid	C18 H34 O2	1
OLC	(2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate	C21 H40 O4	1
8ES	N-benzyl-N-(2-ethyl-4-oxo-3-{[2'-(2H-tetrazol-5-yl)[1,1'-biphenyl]-4-yl]methyl}…	C36 H29 N7 O2 S	1

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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