6A93: 5-HT2AR

Crystal structure of 5-HT2AR in complex with risperidone. Determined by X-ray diffraction at 3.0 Å resolution. Released 13 Feb 2019.

Method: X-ray diffraction
Resolution: 3.0 Å
Organisms: Homo sapiens, Escherichia coli
Chains: 2
Atoms: 5,889
Mol. weight: 86.49 kDa
Ligands: 8NU, CLR, ZN, PLM
Released: 13 Feb 2019

Explore 6A93 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6A93 contains 32 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: 16 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	70-101	32
α-helix	103-105	3
α-helix	108-122	15
α-helix	123-127	5
α-helix	128-136	9
α-helix	145-178	34
α-helix	189-207	19
α-helix	209-216	8
β-strand	223	1	1
β-strand	226	1	1
α-helix	232-239	8
α-helix	240-244	5
α-helix	245-1018	39
α-helix	1023-1040	18
α-helix	1068-1080	13
α-helix	1084-348	59
α-helix	355-382	28
α-helix	385-395	11

Chain B: 16 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	74-101	28
α-helix	108-122	15
α-helix	123-127	5
α-helix	128-136	9
α-helix	145-178	34
α-helix	189-207	19
α-helix	209-216	8
α-helix	218-220	3
β-strand	223	1	2
β-strand	226	1	2
α-helix	232-238	7
α-helix	239-244	6
α-helix	245-1018	39
α-helix	1023-1040	18
α-helix	1067-1080	14
α-helix	1084-348	59
α-helix	356-382	27
α-helix	385-395	11

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
5-hydroxytryptamine receptor 2A,Soluble cytochrome b562	A, B	protein	376	Homo sapiens, Escherichia coli	P0ABE7 (AlphaFold model), P28223 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>6A93_1 5-hydroxytryptamine receptor 2A,Soluble cytochrome b562 (chains A, B)
GGTHLQEKNWSALLTAVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFL
VMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTAKIWHLCAISLDRYVAIQNPIHHSRF
NSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVSFFIP
LTIMVITYFLTIKSLQKEAADLEDNWETLNDNLKVIEKADNAAQVKDALTKMRAAALDAG
SGSGDILVGQIDDALKLANEGKVKEAQAAAEQLKTTINAYIQKYGQSISNEQKACKVLGI
VFFLFVVMWCPFFITNIMAVICKESCNEDVIGALLNVFVWIGYLSSAVNPLVYTLFNKTY
RSAFSRYIQCQYKENK

Ligands and cofactors

ID	Name	Formula	Copies
8NU	3-[2-[4-(6-fluoranyl-1,2-benzoxazol-3-yl)piperidin-1-yl]ethyl]-2-methyl-6,7,8,9…	C23 H27 F N4 O2	2
CLR	Cholesterol	C27 H46 O	2
ZN	Zinc ion	Zn	1
PLM	Palmitic acid	C16 H32 O2	1

Water and common crystallization additives (1PE) are not listed.

Primary citation

Structures of the 5-HT2Areceptor in complex with the antipsychotics risperidone and zotepine. Kimura, K.T., Asada, H., Inoue, A. et al. Nat Struct Mol Biol (2019) 26:121-128. DOI 10.1038/s41594-018-0180-z · 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 more

6A93 is part of these collections:

GPCRs and cell signaling

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