4NC3: PDB entry 4NC3

Crystal structure of the 5-HT2B receptor solved using serial femtosecond crystallography in lipidic cubic phase. Determined by X-ray diffraction at 2.8 Å resolution. Released 18 Dec 2013.

Method: X-ray diffraction
Resolution: 2.8 Å
Organisms: Homo sapiens, Escherichia coli
Chains: 1
Atoms: 3,123
Mol. weight: 53.26 kDa
Ligands: PLM, OLA, DGA, OLC
Released: 18 Dec 2013

Explore 4NC3 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4NC3 contains 19 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 A: 19 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	54-60	7
α-helix	61-65	5
α-helix	66-81	16
α-helix	89-102	14
α-helix	103-107	5
α-helix	108-116	9
β-strand	120	1	1
α-helix	127-158	32
α-helix	165-187	23
α-helix	189-193	5
β-strand	206	1	1
α-helix	211-222	12
α-helix	223-227	5
α-helix	228-1018	39
α-helix	1023-1031	9
α-helix	1060-1081	22
α-helix	1084-335	45
α-helix	338-349	12
α-helix	355-374	20
α-helix	376-381	6
α-helix	385-395	11

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Chimera protein of human 5-hydroxytryptamine receptor 2B and E. Coli soluble cytochrome b562	A	protein	430	Homo sapiens, Escherichia coli	P0ABE7 (AlphaFold model), P41595 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>4NC3_1 Chimera protein of human 5-hydroxytryptamine receptor 2B and E. Coli soluble cytochrome b562 (chains A)
DYKDDDDGAPTESIPEEMKQIVEEQGNKLHWAALLILMVIIPTIGGNTLVILAVSLEKKL
QYATNYFLMSLAVADLLVGLFVMPIALLTIMFEAMWPLPLVLCPAWLFLDVLFSTASIWH
LCAISVDRYIAIKKPIQANQYNSRATAFIKITVVWLISIGIAIPVPIKGIETDVDNPNNI
TCVLTKERFGDFMLFGSLAAFFTPLAIMIVTYFLTIHALQKKAADLEDNWETLNDNLKVI
EKADNAAQVKDALTKMRAAALDAQKATPPKLEDKSPDSPEMKDFRHGFDILVGQIDDALK
LANEGKVKEAQAAAEQLKTTRNAYIQKYLQTISNEQRASKVLGIVFFLFLLMWCPFFITN
ITLVLCDSCNQTTLQMLLEIFVWIGYVSSGVNPLVYTLFNKTFRDAFGRYITCNYRATKS
VGRPLEVLFQ

Ligands and cofactors

ID	Name	Formula	Copies
PLM	Palmitic acid	C16 H32 O2	1
OLA	Oleic acid	C18 H34 O2	3
DGA	Diacyl glycerol	C39 H76 O5	2
OLC	(2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate	C21 H40 O4	4
CLR	Cholesterol	C27 H46 O	1
ERM	Ergotamine	C33 H35 N5 O5	1

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

Primary citation

Serial femtosecond crystallography of G protein-coupled receptors. Liu, W., Wacker, D., Gati, C. et al. Science (2013) 342:1521-1524. DOI 10.1126/science.1244142 · 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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