7WVW: Human formyl peptide receptor 2

Cryo-EM structure of the human formyl peptide receptor 2 in complex with fMYFINILTL and Gi2. Determined by electron microscopy at 3.1 Å resolution. Released 13 Apr 2022.

Method: Electron microscopy
Resolution: 3.1 Å
Organism: Homo sapiens
Chains: 5
Atoms: 7,169
Mol. weight: 144.97 kDa
Released: 13 Apr 2022

Explore 7WVW in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

7WVW contains 30 α-helices and 41 β-strands across 4 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: 11 helices, 9 β-strands

Element	Residues	Length	Sheet
α-helix	7-31	25
β-strand	34-39	6	2
α-helix	46-52	7
β-strand	186-187	2	2
β-strand	190-192	3	2
β-strand	195-201	7	2
α-helix	209-211	3
α-helix	213-216	4
β-strand	221-227	7	2
α-helix	228-231	4
β-strand	234	1	3
β-strand	242	1	3
α-helix	243-255	13
α-helix	258-260	3
β-strand	264-270	7	2
α-helix	272-281	10
α-helix	284-286	3
α-helix	297-311	15
β-strand	320-324	5	2
α-helix	331-351	21

Chain B: 3 helices, 30 β-strands

Element	Residues	Length	Sheet
α-helix	4-25	22
α-helix	32-34	3
α-helix	38-39	2
β-strand	47-52	6	4
β-strand	58-63	6	5
β-strand	69-74	6	5
β-strand	78-83	6	5
β-strand	88-94	7	5
β-strand	100	1	6
β-strand	104-105	2	7
β-strand	111-114	4	7
β-strand	116	1	6
β-strand	121-125	5	7
β-strand	135-139	5	7
β-strand	146-151	6	8
β-strand	156-161	6	8
β-strand	165-170	6	8
β-strand	176-181	6	8
β-strand	187-192	6	9
β-strand	198-203	6	9
β-strand	208-212	5	9
β-strand	218-222	5	9
β-strand	232-234	3	10
β-strand	240-243	4	10
β-strand	249-254	6	10
β-strand	259-265	7	10
β-strand	273-278	6	11
β-strand	284-289	6	11
β-strand	294-298	5	11
β-strand	304-308	5	11
β-strand	315-320	6	4
β-strand	327-331	5	4
β-strand	335-339	5	4

Chain C: 2 helices, 0 β-strands

Element	Residues	Length	Sheet
α-helix	7-22	16
α-helix	30-43	14

Chain R: 14 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	20-47	28
α-helix	48-53	6
α-helix	54	1
α-helix	59-86	28
α-helix	95-128	34
α-helix	130-135	6
α-helix	139-163	25
β-strand	164-168	5	1
β-strand	174-178	5	1
α-helix	187-204	18
α-helix	205-211	7
α-helix	212-230	19
α-helix	238-266	29
α-helix	268-273	6
α-helix	279-302	24
α-helix	307-316	10

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Fme-tyr-phe-ile-asn-ile-leu-the-leu	L	protein	9	Homo sapiens
Soluble cytochrome b562,N-formyl peptide receptor 2	R	protein	513	Homo sapiens	P0ABE7 (AlphaFold model), P25090 (AlphaFold model)
Guanine nucleotide-binding protein G(i) subunit alpha-2	A	protein	355	Homo sapiens	P04899 (AlphaFold model)
Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1	B	protein	351	Homo sapiens	P62873 (AlphaFold model)
Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2	C	protein	71	Homo sapiens	P59768

Sequence of entity 1 (L), FASTA

>7WVW_1 FME-TYR-PHE-ILE-ASN-ILE-LEU-THE-LEU (chains L)
MYFINILTL

Sequence of entity 2 (R), FASTA

>7WVW_2 Soluble cytochrome b562,N-formyl peptide receptor 2 (chains R)
GAPADLEDNWETLNDNLKVIEKADNAAQVKDALTKMRAAALDAQKATPPKLEDKSPDSPE
MKDFRHGFDILVGQIDDALKLANEGKVKEAQAAAEQLKTTRNAYIQKYLGSGSENLYFQS
ETNFSTPLNEYEEVSYESAGYTVLRILPLVVLGVTFVLGVLGNGLVIWVAGFRMTRTVTT
ICYLNLALADFSFTATLPFLIVSMAMGEKWPFGWFLCKLIHIVVDINLFGSVFLIGFIAL
DRCICVLHPVWAQNHRTVSLAMKVIVGPWILALVLTLPVFLFLTTVTIPNGDTYCTFNFA
SWGGTPEERLKVAITMLTARGIIRFVIGFLLPMSIVAICYGLIAAKIHKKGMIKSSRPLR
VLTAVVASFFICWFPFQLVALLGTVWLKEMLFYGKYKIIDILVNPTSSLAFFNSCLNPML
YVFVGQDFRERLIHSLPTSLERALSEDSAPTNDTAANSASPPAETEFLEVLFQGPGSWSH
PQFEKGSGAGASAGSWSHPQFEKGSDYKDDDDK

Sequence of entity 3 (A), FASTA

>7WVW_3 Guanine nucleotide-binding protein G(i) subunit alpha-2 (chains A)
MGCTVSAEDKAAAERSKMIDKNLREDGEKAAREVKLLLLGAGESGKNTIVKQMKIIHEDG
YSEEECRQYRAVVYSNTIQSIMAIVKAMGNLQIDFADPSRADDARQLFALSCTAEEQGVL
PDDLSGVIRRLWADHGVQACFGRSREYQLNDSAAYYLNDLERIAQSDYIPTQQDVLRTRV
KTTGIVETHFTFKDLHFKMFDVGAQRSERKKWIHCFEGVTAIIFCVALSAYDLVLAEDEE
MNRMHASMKLFDSICNNKWFTDTSIILFLNKKDLFEEKITHSPLTICFPEYTGANKYDEA
ASYIQSKFEDLNKRKDTKEIYTHFTCSTDTKNVQFVFDAVTDVIIKNNLKDCGLF

Sequence of entity 4 (B), FASTA

>7WVW_4 Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 (chains B)
MHHHHHHGSLLQSELDQLRQEAEQLKNQIRDARKACADATLSQITNNIDPVGRIQMRTRR
TLRGHLAKIYAMHWGTDSRLLVSASQDGKLIIWDSYTTNKVHAIPLRSSWVMTCAYAPSG
NYVACGGLDNICSIYNLKTREGNVRVSRELAGHTGYLSCCRFLDDNQIVTSSGDTTCALW
DIETGQQTTTFTGHTGDVMSLSLAPDTRLFVSGACDASAKLWDVREGMCRQTFTGHESDI
NAICFFPNGNAFATGSDDATCRLFDLRADQELMTYSHDNIICGITSVSFSKSGRLLLAGY
DDFNCNVWDALKADRAGVLAGHDNRVSCLGVTDDGMAVATGSWDSFLKIWN

Sequence of entity 5 (C), FASTA

>7WVW_5 Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2 (chains C)
MASNNTASIAQARKLVEQLKMEANIDRIKVSKAAADLMAYCEAHAKEDPLLTPVPASENP
FREKKFFCAIL

Primary citation

Structural basis of FPR2 in recognition of A beta 42 and neuroprotection by humanin. Zhu, Y., Lin, X., Zong, X. et al. Nat Commun (2022) 13:1775-1775. DOI 10.1038/s41467-022-29361-x · 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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