11MU: Hemagglutinin

Influenza A virus Hemagglutinin (A/Darwin/6/2021 H3N2) (C1 symmetry) determined using the SPT Labtech chameleon in the presence of 1x SurfACT. Determined by electron microscopy at 2.67 Å resolution. Released 8 Apr 2026.

Method: Electron microscopy
Resolution: 2.67 Å
Organism: Influenza A virus
Chains: 3
Atoms: 12,307
Mol. weight: 189.92 kDa
Released: 8 Apr 2026

Explore 11MU in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

11MU contains 40 α-helices and 133 β-strands across 3 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: 12 helices, 44 β-strands

Element	Residues	Length	Sheet
β-strand	27-33	7	1
β-strand	34	1	2
β-strand	40-42	3	3
β-strand	50-52	3	3
β-strand	55-57	3	4
β-strand	59-60	2	5
β-strand	67-68	2	6
β-strand	74-76	3	7
α-helix	82-87	6
α-helix	90-95	6
β-strand	99	1	8
β-strand	102-105	4	7
β-strand	117	1	9
α-helix	121-131	11
β-strand	133	1	8
β-strand	136-138	3	9
β-strand	146-147	2	10
β-strand	152-156	5	11
β-strand	161-162	2	11
β-strand	167-169	3	9
β-strand	171-172	2	10
β-strand	173	1	12
β-strand	176	1	12
β-strand	180-185	6	13
β-strand	192-200	9	9
α-helix	204-211	8
β-strand	218-221	4	13
β-strand	226-229	4	13
β-strand	245-253	9	9
β-strand	258-263	6	13
β-strand	267-270	4	9
β-strand	272-275	4	9
α-helix	276	1
β-strand	282-285	4	7
α-helix	288-289	2
β-strand	290-291	2	6
β-strand	297-299	3	14
β-strand	302-304	3	14
β-strand	310-311	2	5
β-strand	318	1	14
β-strand	319-320	2	15
α-helix	322	1
β-strand	323-324	2	5
β-strand	331-333	3	4
β-strand	337	1	3
β-strand	359	1	2
β-strand	367-372	6	1
β-strand	377-382	6	1
α-helix	383-400	18
β-strand	406-407	2	15
α-helix	421-471	51
α-helix	472-474	3
β-strand	475-477	3	1
β-strand	482-485	4	1
α-helix	491-498	8
α-helix	508-515	8

Chain B: 14 helices, 45 β-strands

Element	Residues	Length	Sheet
β-strand	27-33	7	16
β-strand	34	1	17
β-strand	40-42	3	18
β-strand	50-52	3	18
β-strand	55-57	3	19
β-strand	59-60	2	20
β-strand	67-68	2	21
β-strand	74-76	3	22
α-helix	82-87	6
α-helix	90-95	6
β-strand	99	1	23
β-strand	102-105	4	22
β-strand	116-117	2	24
α-helix	121-131	11
β-strand	133	1	23
β-strand	136-138	3	24
β-strand	146-147	2	25
β-strand	152-156	5	26
β-strand	161-162	2	26
β-strand	167-169	3	24
β-strand	171-172	2	25
β-strand	173	1	27
β-strand	176	1	27
α-helix	178-179	2
β-strand	180-185	6	28
β-strand	192-200	9	24
α-helix	204-211	8
β-strand	218-221	4	28
β-strand	226-229	4	28
β-strand	239	1	29
β-strand	242	1	29
β-strand	245-253	9	24
β-strand	258-263	6	28
β-strand	267-270	4	24
β-strand	272-275	4	24
β-strand	282-285	4	22
α-helix	288-289	2
β-strand	290-291	2	21
β-strand	297-299	3	30
β-strand	302-304	3	30
β-strand	310-311	2	20
β-strand	318-320	3	30
α-helix	322	1
β-strand	323-324	2	20
β-strand	331-333	3	19
α-helix	336	1
β-strand	337	1	18
α-helix	338	1
β-strand	359	1	17
β-strand	367-372	6	16
β-strand	377-382	6	16
α-helix	383-400	18
β-strand	406-407	2	30
α-helix	423-471	49
α-helix	472-474	3
β-strand	475-477	3	16
β-strand	482-485	4	16
α-helix	491-498	8
α-helix	504-515	12

Chain C: 14 helices, 44 β-strands

Element	Residues	Length	Sheet
β-strand	27-33	7	31
β-strand	34	1	32
β-strand	40-42	3	33
β-strand	50-52	3	33
β-strand	55-57	3	34
β-strand	59-60	2	35
β-strand	67-68	2	36
β-strand	74-76	3	37
α-helix	82-87	6
α-helix	90-95	6
β-strand	99	1	38
β-strand	102-105	4	37
α-helix	106	1
β-strand	116-117	2	39
α-helix	121-131	11
β-strand	133	1	38
β-strand	137-138	2	40
β-strand	146-147	2	41
β-strand	152	1	42
β-strand	162	1	42
β-strand	167-169	3	39
β-strand	171-172	2	41
β-strand	173	1	43
β-strand	176	1	43
β-strand	180-185	6	44
β-strand	192-200	9	39
α-helix	204-211	8
β-strand	218-221	4	44
β-strand	226-229	4	44
β-strand	245-253	9	39
β-strand	258-263	6	44
β-strand	267-270	4	39
β-strand	272-273	2	40
β-strand	274-275	2	39
β-strand	282-285	4	37
α-helix	288-289	2
β-strand	290-291	2	36
β-strand	297-299	3	45
β-strand	302-304	3	45
β-strand	310-311	2	35
β-strand	318-321	4	45
α-helix	322	1
β-strand	323-324	2	35
β-strand	331-333	3	34
α-helix	336	1
β-strand	337	1	33
α-helix	338	1
β-strand	359	1	32
β-strand	367-372	6	31
β-strand	377-382	6	31
α-helix	383-400	18
β-strand	405-407	3	45
α-helix	422-471	50
α-helix	472-474	3
β-strand	475-477	3	31
β-strand	482-485	4	31
α-helix	491-498	8
α-helix	504-515	12

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Hemagglutinin	A, B, C	protein	565	Influenza A virus	A0A8F5JT24

Sequence of entity 1 (A, B, C), FASTA

>11MU_1 Hemagglutinin (chains A, B, C)
MKTIIALSNILCLVFAQKIPGNDNSTATLCLGHHAVPNGTIVKTITNDRIEVTNATELVQ
NSSIGEICGSPHQILDGGNCTLIDALLGDPQCDGFQNKEWDLFVERSRANSNCYPYDVPD
YASLRSLVASSGTLEFKNESFNWTGVKQNGTSSACIRGSSSSFFSRLNWLTSLNNIYPAQ
NVTMPNKEQFDKLYIWGVHHPDTDKNQISLFAQSSGRITVSTKRSQQAVIPNIGSRPRIR
DIPSRISIYWTIVKPGDILLINSTGNLIAPRGYFKIRSGKSSIMRSDAPIGKCKSECITP
NGSIPNDKPFQNVNRITYGACPRYVKQSTLKLATGMRNVPEKQTRGIFGAIAGFIENGWE
GMVDGWYGFRHQNSEGRGQAADLKSTQAAIDQINGKLNRLIGKTNEKFHQIEKEFSEVEG
RVQDLEKYVEDTKIDLWSYNAELLVALENQHTIDLTDSEMNKLFEKTKKQLRENAEDMGN
GCFKIYHKCDNACIGSIRNETYDHNVYRDEALNNRFQIKGVGYIPEAPRDGQAYVRKDGE
WVLLSTFLGSENLYFQGGSHHHHHH

Primary citation

A Surfactant Cocktail Overcomes Air-Water Interface Artifacts in Single-Particle CryoEM. Enos, S.E., Cook, B.D., Rahmani, H. et al. bioRxiv (2026). DOI 10.64898/2026.03.17.712260 · PubMed

Other PDB entries of the same protein (UniProt A0A8F5JT24), best resolution first:

11MT 2.16 Å, Influenza A virus Hemagglutinin (A/Darwin/6/2021 H3N2) (C3 symmetry) determined using…
11MS 2.39 Å, Influenza A virus Hemagglutinin (A/Darwin/6/2021 H3N2) (C1 symmetry) determined using…
11MV 2.47 Å, Influenza A virus Hemagglutinin (A/Darwin/6/2021 H3N2) (C3 symmetry) determined using…
9BDF 3.01 Å, Influenza A virus Hemagglutinin H3/Darwin/6/2021 in complex with Fab ADI-85666
9BDG 3.01 Å, Influenza A virus Hemagglutinin H3/Darwin/6/2021 in complex with Fab ADI-85647

Browse structure collections

About this viewer

MolViewer shows 11MU directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.