6DRY: 5HT2B receptor, BRIL chimera

Structural Determinants of Activation and Biased Agonism at the 5-HT2B Receptor. Determined by X-ray diffraction at 2.92 Å resolution. Released 29 Aug 2018.

Method: X-ray diffraction
Resolution: 2.92 Å
Organisms: Homo sapiens, Escherichia coli
Chains: 1
Atoms: 3,040
Mol. weight: 47.81 kDa
Ligands: PO4, OLC, OLA, CLR
Released: 29 Aug 2018

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

Secondary structure: helices and β-sheets

6DRY contains 21 α-helices and 0 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 A: 21 helices, 0 β-strands

Element	Residues	Length
α-helix	54-60	7
α-helix	61-65	5
α-helix	66-81	16
α-helix	83-85	3
α-helix	88-102	15
α-helix	103-107	5
α-helix	108-116	9
α-helix	127-158	32
α-helix	169-187	19
α-helix	189-193	5
α-helix	211-222	12
α-helix	223-227	5
α-helix	228-1018	39
α-helix	1023-1041	19
α-helix	1064-1081	18
α-helix	1084-1097	14
α-helix	1098-1102	5
α-helix	1103-349	41
α-helix	355-374	20
α-helix	376-381	6
α-helix	385-395	11

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
5HT2B receptor, BRIL chimera	A	protein	411	Homo sapiens, Escherichia coli	P0ABE7 (AlphaFold model), P41595 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>6DRY_1 5HT2B receptor, BRIL chimera (chains A)
TESIPEEMKQIVEEQGNKLHWAALLILMVIIPTIGGNTLVILAVSLEKKLQYATNYFLMS
LAVADLLVGLFVMPIALLTIMFEAMWPLPLVLCPAWLFLDVLFSTASIWHLCAISVDRYI
AIKKPIQANQYNSRATAFIKITVVWLISIGIAIPVPIKGIETDVDNPNNITCVLTKERFG
DFMLFGSLAAFFTPLAIMIVTYFLTIHALQKKAADLEDNWETLNDNLKVIEKADNAAQVK
DALTKMRAAALDAQKATPPKLEDKSPDSPEMKDFRHGFDILVGQIDDALKLANEGKVKEA
QAAAEQLKTTRNAYIQKYLVQTISNEQRASKVLGIVFFLFLLMWCPFFITNITLVLCDSC
NQTTLQMLLEIFVWIGYVSSGVNPLVYTLFNKTFRDAFGRYITCNYRATKS

Ligands and cofactors

ID	Name	Formula	Copies
PO4	Phosphate ion	O4 P	2
OLC	(2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate	C21 H40 O4	1
OLA	Oleic acid	C18 H34 O2	1
CLR	Cholesterol	C27 H46 O	1
H8D	(8beta)-N-[(2S)-1-hydroxybutan-2-yl]-6-methyl-9,10-didehydroergoline-8-carboxam…	C20 H25 N3 O2	1

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

Primary citation

Structural determinants of 5-HT2Breceptor activation and biased agonism. McCorvy, J.D., Wacker, D., Wang, S. et al. Nat Struct Mol Biol (2018) 25:787-796. DOI 10.1038/s41594-018-0116-7 · 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

Browse structure collections

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