5NM2: A2A Adenosine receptor cryo structure

A2A Adenosine receptor cryo structure. Determined by X-ray diffraction at 1.95 Å resolution. Released 27 Sept 2017.

Method: X-ray diffraction
Resolution: 1.95 Å
Organisms: Homo sapiens, Escherichia coli
Chains: 1
Atoms: 3,698
Mol. weight: 55.18 kDa
Ligands: ZMA, OLA, OLB, OLC
Released: 27 Sept 2017

Explore 5NM2 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5NM2 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 A: 23 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	2-33	32
α-helix	35-37	3
α-helix	40-54	15
α-helix	55-59	5
α-helix	60-67	8
β-strand	71-73	3	1
α-helix	74-107	34
α-helix	109-115	7
α-helix	118-136	19
α-helix	138-141	4
α-helix	151-156	6
β-strand	163-165	3	1
α-helix	168-171	4
α-helix	174-175	2
α-helix	176-187	12
α-helix	188-1018	39
α-helix	1023-1041	19
α-helix	1059-1080	22
α-helix	1084-1092	9
α-helix	1094-1097	4
α-helix	1098-1102	5
α-helix	1103-258	44
α-helix	263-264	2
α-helix	267-291	25
α-helix	293-304	12

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Adenosine receptor A2a,Soluble cytochrome b562,Adenosine receptor A2a	A	protein	433	Homo sapiens, Escherichia coli	P0ABE7 (AlphaFold model), P29274 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>5NM2_1 Adenosine receptor A2a,Soluble cytochrome b562,Adenosine receptor A2a (chains A)
DYKDDDDGAPPIMGSSVYITVELAIAVLAILGNVLVCWAVWLNSNLQNVTNYFVVSLAAA
DILVGVLAIPFAITISTGFCAACHGCLFIACFVLVLAQSSIFSLLAIAIDRYIAIAIPLR
YNGLVTGTRAAGIIAICWVLSFAIGLTPMLGWNNCGQPKEGKAHSQGCGEGQVACLFEDV
VPMNYMVYFNFFACVLVPLLLMLGVYLRIFAAARRQLADLEDNWETLNDNLKVIEKADNA
AQVKDALTKMRAAALDAQKATPPKLEDKSPDSPEMKDFRHGFDILVGQIDDALKLANEGK
VKEAQAAAEQLKTTRNAYIQKYLERARSTLQKEVHAAKSAAIIAGLFALCWLPLHIINCF
TFFCPDCSHAPLWLMYLAIVLAHTNSVVNPFIYAYRIREFRQTFRKIIRSHVLRQQEPFK
AAAHHHHHHHHHH

Ligands and cofactors

ID	Name	Formula	Copies
ZMA	4-{2-[(7-amino-2-furan-2-yl[1,2,4]triazolo[1,5-a][1,3,5]triazin-5-yl)amino]ethy…	C16 H15 N7 O2	1
OLA	Oleic acid	C18 H34 O2	15
OLB	(2S)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate	C21 H40 O4	2
OLC	(2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate	C21 H40 O4	2
CLR	Cholesterol	C27 H46 O	3

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

Primary citation

Serial millisecond crystallography for routine room-temperature structure determination at synchrotrons. Weinert, T., Olieric, N., Cheng, R. et al. Nat Commun (2017) 8:542-542. DOI 10.1038/s41467-017-00630-4 · 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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