9ZZ6: ER membrane protein complex subunit 1

The ER membrane protein complex acts as a chaperone to promote voltage-gated calcium channel assembly. Determined by electron microscopy at 4.16 Å resolution. Released 18 Feb 2026.

Method: Electron microscopy
Resolution: 4.16 Å
Organisms: Homo sapiens, Lama glama
Chains: 11
Atoms: 20,560
Mol. weight: 333.28 kDa
Ligands: NAG
Released: 18 Feb 2026

Explore 9ZZ6 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9ZZ6 contains 104 α-helices and 150 β-strands across 11 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: 25 helices, 78 β-strands

Element	Residues	Length	Sheet
α-helix	24-26	3
β-strand	34-35	2	1
β-strand	40-44	5	2
β-strand	55-58	4	2
β-strand	62-66	5	2
β-strand	73-78	6	2
α-helix	83-85	3
β-strand	87-93	7	3
β-strand	96-101	6	3
α-helix	102-104	3
β-strand	106-111	6	3
β-strand	117-122	6	3
β-strand	133-134	2	4
β-strand	142-143	2	4
β-strand	145-146	2	5
β-strand	150-154	5	5
β-strand	155	1	4
β-strand	161-166	6	5
α-helix	167	1
β-strand	174-180	7	6
β-strand	185-192	8	6
β-strand	196-203	8	6
β-strand	212-215	4	6
β-strand	229	1	7
β-strand	234-239	6	7
β-strand	244-249	6	7
β-strand	257-260	4	7
α-helix	261-264	4
β-strand	275-277	3	8
α-helix	286-288	3
β-strand	290-296	7	8
β-strand	299-305	7	8
β-strand	310-311	2	8
β-strand	315-317	3	8
β-strand	319-327	9	9
β-strand	330-338	9	9
β-strand	372-379	8	9
β-strand	385	1	9
β-strand	391-394	4	9
β-strand	402-411	10	10
β-strand	417-425	9	10
β-strand	429	1	11
β-strand	430-434	5	10
α-helix	440-442	3
β-strand	446	1	11
α-helix	449-451	3
β-strand	452	1	12
β-strand	457-458	2	13
α-helix	459-463	5
α-helix	464-467	4
α-helix	470-473	4
α-helix	480-508	29
α-helix	513-515	3
β-strand	535-539	5	13
β-strand	540	1	12
β-strand	544-549	6	13
β-strand	555-560	6	13
β-strand	569-574	6	14
β-strand	587-592	6	14
β-strand	599-605	7	14
β-strand	610-611	2	14
α-helix	615-616	2
β-strand	626-632	7	15
β-strand	638-643	6	15
β-strand	649-651	3	15
α-helix	656-665	10
α-helix	666-668	3
β-strand	669-674	6	16
β-strand	680-686	7	16
β-strand	692-693	2	16
β-strand	697-699	3	16
β-strand	705-712	8	17
β-strand	723-725	3	18
β-strand	731-733	3	18
β-strand	740-747	8	17
α-helix	752-754	3
β-strand	756-763	8	17
β-strand	769-776	8	17
β-strand	778-779	2	19
β-strand	785-787	3	20
β-strand	790-792	3	20
β-strand	796-797	2	19
β-strand	802	1	19
β-strand	804-811	8	20
β-strand	813	1	18
β-strand	822	1	21
α-helix	824-826	3
α-helix	830-831	2
β-strand	832-839	8	20
β-strand	846-849	4	22
α-helix	858-859	2
β-strand	860-864	5	22
β-strand	870-874	5	22
α-helix	875-878	4
α-helix	888-892	5
α-helix	896-898	3
α-helix	906-908	3
β-strand	909	1	22
β-strand	922-926	5	23
β-strand	933-937	5	23
β-strand	941-942	2	1
β-strand	945-947	3	23
α-helix	962-991	30

Chain B: 20 helices, 0 β-strands

Element	Residues	Length
α-helix	15-25	11
α-helix	30-43	14
α-helix	45-48	4
α-helix	49-51	3
α-helix	52-66	15
α-helix	69-82	14
α-helix	87-99	13
α-helix	103-116	14
α-helix	122-134	13
α-helix	137-150	14
α-helix	155-167	13
α-helix	171-178	8
α-helix	181-184	4
α-helix	189-202	14
α-helix	205-221	17
α-helix	226-241	16
α-helix	247-274	28
α-helix	276-278	3
α-helix	279-292	14
α-helix	294-295	2

Chain C: 20 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	10-12	3
α-helix	13-17	5
α-helix	18-38	21
α-helix	46-63	18
α-helix	70-81	12
α-helix	85-92	8
α-helix	97-100	4
α-helix	105-118	14
α-helix	119-124	6
α-helix	125-129	5
β-strand	136-139	4	24
α-helix	146-148	3
β-strand	165-167	3	24
α-helix	168-178	11
α-helix	183-186	4
α-helix	196-199	4
α-helix	201-203	3
α-helix	209-210	2
α-helix	216-227	12
α-helix	237-243	7
α-helix	245-246	2
α-helix	248-250	3

Chain D: 8 helices, 3 β-strands

Element	Residues	Length	Sheet
α-helix	24-27	4
α-helix	43-44	2
α-helix	60-72	13
α-helix	75-92	18
α-helix	96-114	19
α-helix	116-125	10
α-helix	129-153	25
α-helix	161-164	4
β-strand	173	1	21
β-strand	176-177	2	16
β-strand	180-181	2	16

Chain E: 6 helices, 1 β-strand

Element	Residues	Length	Sheet
α-helix	2-33	32
α-helix	43-64	22
α-helix	67-69	3
β-strand	71	1	25
α-helix	74-76	3
α-helix	88-90	3
α-helix	96-100	5

Chain F: 6 helices, 1 β-strand

Element	Residues	Length	Sheet
β-strand	14	1	25
α-helix	16-44	29
α-helix	49-69	21
α-helix	74-77	4
α-helix	82-85	4
α-helix	89-104	16
α-helix	105-109	5

Chain G: 4 helices, 12 β-strands

Element	Residues	Length	Sheet
β-strand	45-50	6	26
β-strand	52	1	27
α-helix	58-60	3
β-strand	67-68	2	28
β-strand	75	1	28
β-strand	77-78	2	26
β-strand	83-89	7	26
β-strand	92-96	5	29
β-strand	97-98	2	28
β-strand	108-112	5	29
β-strand	120-122	3	29
β-strand	134	1	29
β-strand	141	1	27
α-helix	157-161	5
α-helix	164-168	5
α-helix	171-177	7

Chain H: 6 helices, 11 β-strands

Element	Residues	Length	Sheet
β-strand	5-6	2	30
α-helix	8-20	13
β-strand	26-33	8	31
β-strand	53-54	2	30
β-strand	56-62	7	31
α-helix	68-83	16
β-strand	87-95	9	31
α-helix	106-118	13
β-strand	123-126	4	31
β-strand	127	1	32
β-strand	141	1	32
β-strand	144-146	3	31
β-strand	151-153	3	31
β-strand	161	1	30
α-helix	164-176	13
α-helix	186-191	6
α-helix	200-209	10

3 more chain groups are not listed. Open the entry in the viewer and use the sequence panel to see them.

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
ER membrane protein complex subunit 1	A	protein	993	Homo sapiens	Q8N766 (AlphaFold model)
ER membrane protein complex subunit 2	B	protein	297	Homo sapiens	Q15006 (AlphaFold model)
ER membrane protein complex subunit 3	C	protein	261	Homo sapiens	Q9P0I2 (AlphaFold model)
ER membrane protein complex subunit 4	D	protein	183	Homo sapiens	Q5J8M3 (AlphaFold model)
Membrane magnesium transporter 1	E	protein	131	Homo sapiens	Q8N4V1
ER membrane protein complex subunit 6	F	protein	110	Homo sapiens	Q9BV81
ER membrane protein complex subunit 7	G	protein	242	Homo sapiens	Q9NPA0
ER membrane protein complex subunit 8	H	protein	210	Homo sapiens	O43402
ER membrane protein complex subunit 10	I	protein	262	Homo sapiens	Q5UCC4
Nanobody G9	K	protein	161	Lama glama
Nanobody E2	L	protein	132	Lama glama

Sequence of entity 1 (A), FASTA

>9ZZ6_1 ER membrane protein complex subunit 1 (chains A)
MAAEWASRFWLWATLLIPAAAVYEDQVGKFDWRQQYVGKVKFASLEFSPGSKKLVVATEK
NVIAALNSRTGEILWRHVDKGTAEGAVDAMLLHGQDVITVSNGGRIMRSWETNIGGLNWE
ITLDSGSFQALGLVGLQESVRYIAVLKKTTLALHHLSSGHLKWVEHLPESDSIHYQMVYS
YGSGVVWALGVVPFSHVNIVKFNVEDGEIVQQVRVSTPWLQHLSGACGVVDEAVLVCPDP
SSRSLQTLALETEWELRQIPLQSLDLEFGSGFQPRVLPTQPNPVDASRAQFFLHLSPSHY
ALLQYHYGTLSLLKNFPQTALVSFATTGEKTVAAVMACRNEVQKSSSSEDGSMGSFSEKS
SSKDSLACFNQTYTINLYLVETGRRLLDTTITFSLEQSGTRPERLYIQVFLKKDDSVGYR
ALVQTEDHLLLFLQQLAGKVVLWSREESLAEVVCLEMVDLPLTGAQAELEGEFGKKADGL
LGMFLKRLSSQLILLQAWTSHLWKMFYDARKPRSQIKNEINIDTLARDEFNLQKMMVMVT
ASGKLFGIESSSGTILWKQYLPNVKPDSSFKLMVQRTTAHFPHPPQCTLLVKDKESGMSS
LYVFNPIFGKWSQVAPPVLKRPILQSLLLPVMDQDYAKVLLLIDDEYKVTAFPATRNVLR
QLHELAPSIFFYLVDAEQGRLCGYRLRKDLTTELSWELTIPPEVQRIVKVKGKRSSEHVH
SQGRVMGDRSVLYKSLNPNLLAVVTESTDAHHERTFIGIFLIDGVTGRIIHSSVQKKAKG
PVHIVHSENWVVYQYWNTKARRNEFTVLELYEGTEQYNATAFSSLDRPQLPQVLQQSYIF
PSSISAMEATITERGITSRHLLIGLPSGAILSLPKALLDPRRPEIPTEQSREENLIPYSP
DVQIHAERFINYNQTVSRMRGIYTAPSGLESTCLVVAYGLDIYQTRVYPSKQFDVLKDDY
DYVLISSVLFGLVFATMITKRLAQVKLLNRAWR

Sequence of entity 2 (B), FASTA

>9ZZ6_2 ER membrane protein complex subunit 2 (chains B)
MAKVSELYDVTWEEMRDKMRKWREENSRNSEQIVEVGEELINEYASKLGDDIWIIYEQVM
IAALDYGRDDLALFCLQELRRQFPGSHRVKRLTGMRFEAMERYDDAIQLYDRILQEDPTN
TAARKRKIAIRKAQGKNVEAIRELNEYLEQFVGDQEAWHELAELYINEHDYAKAAFCLEE
LMMTNPHNHLYCQQYAEVKYTQGGLENLELSRKYFAQALKLNNRNMRALFGLYMSASHIA
SNPKASAKTKKDNMKYASWAASQINRAYQFAGRSKKETKYSLKAVEDMLETLQITQS

Sequence of entity 3 (C), FASTA

>9ZZ6_3 ER membrane protein complex subunit 3 (chains C)
MAGPELLLDSNIRLWVVLPIVIITFFVGMIRHYVSILLQSDKKLTQEQVSDSQVLIRSRV
LRENGKYIPKQSFLTRKYYFNNPEDGFFKKTKRKVVPPSPMTDPTMLTDMMKGNVTNVLP
MILIGGWINMTFSGFVTTKVPFPLTLRFKPMLQQGIELLTLDASWVSSASWYFLNVFGLR
SIYSLILGQDNAADQSRMMQEQMTGAAMAMPADTNKAFKTEWEALELTDHQWALDDVEEE
LMAKDLHFEGMFKKELQTSIF

Sequence of entity 4 (D), FASTA

>9ZZ6_4 ER membrane protein complex subunit 4 (chains D)
MTAQGGLVANRGRRFKWAIELSGPGGGSRGRSDRGSGQGDSLYPVGYLDKQVPDTSVQET
DRILVEKRCWDIALGPLKQIPMNLFIMYMAGNTISIFPTMMVCMMAWRPIQALMAISATF
KMLESSSQKFLQGLVYLIGNLMGLALAVYKCQSMGLLPTHASDWLAFIEPPERMEFSGGG
LLL

Sequence of entity 5 (E), FASTA

>9ZZ6_5 Membrane magnesium transporter 1 (chains E)
MAPSLWKGLVGIGLFALAHAAFSAAQHRSYMRLTEKEDESLPIDIVLQTLLAFAVTCYGI
VHIAGEFKDMDATSELKNKTFDTLRNHPSFYVFNHRGRVLFRPSDTANSSNQDALSSNTS
LKLRKLESLRR

Sequence of entity 6 (F), FASTA

>9ZZ6_6 ER membrane protein complex subunit 6 (chains F)
MAAVVAKREGPPFISEAAVRGNAAVLDYCRTSVSALSGATAGILGLTGLYGFIFYLLASV
LLSLLLILKAGRRWNKYFKSRRPLFTGGLIGGLFTYVLFWTFLYGMVHVY

Sequence of entity 7 (G), FASTA

>9ZZ6_7 ER membrane protein complex subunit 7 (chains G)
MAAALWGFFPVLLLLLLSGDVQSSEVPGAAAEGSGGSGVGIGDRFKIEGRAVVPGVKPQD
WISAARVLVDGEEHVGFLKTDGSFVVHDIPSGSYVVEVVSPAYRFDPVRVDITSKGKMRA
RYVNYIKTSEVVRLPYPLQMKSSGPPSYFIKRESWGWTDFLMNPMVMMMVLPLLIFVLLP
KVVNTSDPDMRREMEQSMNMLNSNHELPDVSEFMTRLFSSKSSGKSSSGSSKTGKSGAGK
RR

Sequence of entity 8 (H), FASTA

>9ZZ6_8 ER membrane protein complex subunit 8 (chains H)
MPGVKLTTQAYCKMVLHGAKYPHCAVNGLLVAEKQKPRKEHLPLGGPGAHHTLFVDCIPL
FHGTLALAPMLEVALTLIDSWCKDHSYVIAGYYQANERVKDASPNQVAEKVASRIAEGFS
DTALIMVDNTKFTMDCVAPTIHVYEHHENRWRCRDPHHDYCEDWPEAQRISASLLDSRSY
ETLVDFDNHLDDIRNDWTNPEINKAVLHLC

Sequence of entity 9 (I), FASTA

>9ZZ6_9 ER membrane protein complex subunit 10 (chains I)
MAAASAGATRLLLLLLMAVAAPSRARGSGCRAGTGARGAGAEGREGEACGTVGLLLEHSF
EIDDSANFRKRGSLLWNQQDGTLSLSQRQLSEEERGRLRDVAALNGLYRVRIPRRPGALD
GLEAGGYVSSFVPACSLVESHLSDQLTLHVDVAGNVVGVSVVTHPGGCRGHEVEDVDLEL
FNTSVQLQPPTTAPGPETAAFIERLEMEQAQKAKNPQEQKSFFAKYWMYIIPVVLFLMMS
GAPDTGGQGGGGGGGGGGGSGR

Sequence of entity 10 (K), FASTA

>9ZZ6_10 Nanobody G9 (chains K)
GSGSGGSGGTSGSSSGSCSSQVQLVESGGGLVQPGGSLRLSCAASGNIFGIYPMGWHRQA
PGKQREFVASTTTYNYTSYADSAKGRFTIARDNAKNTVYLQMNSLKPEDTAIYYCYILIR
AKVYRGQGTLVTVSSTSSSGSGSGGSGETGSHHHHHHHHHH

Sequence of entity 11 (L), FASTA

>9ZZ6_11 Nanobody E2 (chains L)
GSGSGGSGGSGGSGGSTSQVQLVESGGGLVQVGGSLRLSCAASGFEFSLFPMSWHRQAPG
KEREFVAAISNTGGNTNYADSVKGRFTISRDNAKNTAYLQMNSLKPEDTAVYYCNARSRE
YWGQGTQVTVSS

Ligands and cofactors

ID	Name	Formula	Copies
NAG	2-acetamido-2-deoxy-beta-D-glucopyranose	C8 H15 N O6	1

Primary citation

The ER membrane protein complex acts as a chaperone to promote the biogenesis of multi-bundle membrane proteins. Stanton, M., Singal, B., Biswal, M. et al. bioRxiv (2026). DOI 10.64898/2026.01.14.699575 · PubMed

Other PDB entries of the same protein (UniProt Q8N766 (AlphaFold model), which also has an AlphaFold model), best resolution first:

8J0O 3.32 Å, cryo-EM structure of human EMC and VDAC
7ADO 3.39 Å, Cryo-EM structure of human ER membrane protein complex in lipid nanodiscs
6WW7 3.4 Å, Structure of the human ER membrane protein complex in a lipid nanodisc
8EOI 3.4 Å, Structure of a human EMC:human Cav1.2 channel complex in GDN detergent
8J0N 3.47 Å, cryo-EM structure of human EMC
7ADP 3.6 Å, Cryo-EM structure of human ER membrane protein complex in GDN detergent
8S9S 3.6 Å, Structure of the human ER membrane protein complex (EMC) in GDN
6Z3W 6.4 Å, Human ER membrane protein complex
9C7V 6.6 Å, Structure of the human BOS:human EMC complex in GDN

Browse structure collections

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