5NM4: PDB entry 5NM4

A2A Adenosine receptor room-temperature structure determined by serial femtosecond crystallography. Determined by X-ray diffraction at 1.7 Å resolution. Released 27 Sept 2017.

Method: X-ray diffraction
Resolution: 1.7 Å
Organisms: Homo sapiens, Escherichia coli
Chains: 1
Atoms: 3,157
Mol. weight: 50.93 kDa
Ligands: CLR, ZMA, OLA
Released: 27 Sept 2017

Explore 5NM4 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5NM4 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	11-42	32
α-helix	44-46	3
α-helix	49-63	15
α-helix	64-68	5
α-helix	69-76	8
β-strand	80-82	3	1
α-helix	83-116	34
α-helix	118-124	7
α-helix	127-145	19
α-helix	147-150	4
α-helix	160-166	7
α-helix	168-169	2
β-strand	172-174	3	1
α-helix	177-180	4
α-helix	183-184	2
α-helix	185-196	12
α-helix	197-235	39
α-helix	240-259	20
α-helix	282-297	16
α-helix	301-314	14
α-helix	315-319	5
α-helix	320-363	44
α-helix	368-369	2
α-helix	372-396	25
α-helix	398-408	11

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

>5NM4_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
CLR	Cholesterol	C27 H46 O	3
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	5

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

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