25IF: MC5aR2

Structure of mC5aR2 in complex with mC5a-desArg (Monomer). Determined by electron microscopy at 3.42 Å resolution. Released 1 Jul 2026.

Method: Electron microscopy
Resolution: 3.42 Å
Organism: Mus musculus
Chains: 2
Atoms: 2,816
Mol. weight: 52.9 kDa
Released: 1 Jul 2026

Explore 25IF in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

25IF contains 17 α-helices and 5 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: 13 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	40-67	28
α-helix	76-101	26
α-helix	109-143	35
α-helix	145-147	3
α-helix	152-177	26
β-strand	179	1	1
β-strand	182-184	3	2
β-strand	189-191	3	2
β-strand	194	1	1
α-helix	202-211	10
α-helix	212-216	5
α-helix	217-232	16
α-helix	238-262	25
α-helix	270-276	7
α-helix	279-287	9
α-helix	289-299	11
α-helix	302-312	11

Chain B: 4 helices, 1 β-strand

Element	Residues	Length	Sheet
α-helix	4-14	11
α-helix	19-28	10
α-helix	37-42	6
α-helix	48-66	19
β-strand	71	1	1

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
C5a anaphylatoxin chemotactic receptor 2	A	protein	400	Mus musculus	E9QQ21 (AlphaFold model)
Complement C5	B	protein	76	Mus musculus	P06684 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>25IF_1 C5a anaphylatoxin chemotactic receptor 2 (chains A)
MGKTIIALSYIFCLVFADYKDDDDAANFTPVNGSSGNQSVRLVTSSSLEVLFQGPGSMNH
TTSEYYDYEYDHEHYSDLPDVPVDCPAGTCFTSDVYLIVLLVLYAAVFLVGVPGNTLVAW
VTWKESRHRLGASWFLHLTMADLLCCVSLPFLAVPIAQKGHWPYGAAGCWLLSSITILSM
YASVLLLTGLSGDLFLLAFRPSWKGADHRTFGVRVVQASSWMLGLLLTVPSAVYRRLLQE
HYPPRLVCGIDYGGSVSAEVAITTVRFLFGFLGPLVFMAGCHGILQRQMARRHWPLGTAV
VVGFFICWTPYHVLRVIIAAAPPHSLLLARVLEAEPLFNGLALAHSALNPIMFLYFGRKQ
LCKSLQAACHWALRDPQDEESAVTKVSISTSHEMVSEMPV

Sequence of entity 2 (B), FASTA

>25IF_2 Complement C5 (chains B)
NLHLLRQKIEEQAAKYKHSVPKKCCYDGARVNFYETCEERVARVTIGPLCIRAFNECCTI
ANKIRKESPHKPVQLG

Primary citation

Molecular mechanisms of naturally encoded signaling bias at the complement anaphylatoxin receptors. Tiwari, D., Sawada, K., Dalal, A. et al. Mol Cell (2026) 86:2586. DOI 10.1016/j.molcel.2026.06.002 · PubMed

Other PDB entries of the same protein (UniProt E9QQ21 (AlphaFold model), which also has an AlphaFold model), best resolution first:

9WDI 3.33 Å, Structure of mC5aR2 in complex with mC5a-desArg

Browse structure collections

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