9JTC: Bovine UBA7-UBE2L6-ISG15

Cryo-EM structure of bovine UBA7-UBE2L6-ISG15. Determined by electron microscopy at 2.99 Å resolution. Released 5 Mar 2025.

Method: Electron microscopy
Resolution: 2.99 Å
Organism: Bos taurus
Chains: 3
Atoms: 9,158
Mol. weight: 146.39 kDa
Ligands: AMP
Released: 5 Mar 2025

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

Secondary structure: helices and β-sheets

9JTC contains 72 α-helices and 63 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: 62 helices, 47 β-strands

Element	Residues	Length	Sheet
α-helix	30-32	3
β-strand	34-38	5	1
α-helix	42-54	13
β-strand	58-62	5	1
β-strand	66	1	2
α-helix	67	1
α-helix	69-71	3
α-helix	80-82	3
β-strand	86	1	2
α-helix	87-98	12
β-strand	103-106	4	1
α-helix	113-116	4
β-strand	121-124	4	1
α-helix	129-141	13
β-strand	145-152	8	1
β-strand	155-161	7	1
β-strand	166-168	3	3
β-strand	170	1	4
α-helix	175-176	2
β-strand	179-180	2	5
β-strand	181-184	4	6
β-strand	187	1	7
α-helix	190	1
β-strand	191-194	4	6
β-strand	208-214	7	5
α-helix	218-220	3
β-strand	221	1	5
α-helix	223-225	3
β-strand	226-227	2	5
β-strand	229-230	2	6
β-strand	236-237	2	6
β-strand	241	1	7
β-strand	250-255	6	5
β-strand	260-262	3	3
α-helix	267-270	4
β-strand	276	1	1
α-helix	283-303	21
α-helix	306-308	3
α-helix	312-324	13
α-helix	342-351	10
α-helix	357-376	20
β-strand	378	1	4
α-helix	380-382	3
β-strand	385-389	5	1
α-helix	391-393	3
α-helix	395-396	2
α-helix	400-403	4
α-helix	415-421	7
α-helix	423-430	8
β-strand	433-437	5	8
α-helix	441-453	13
β-strand	462-466	5	8
β-strand	470	1	9
α-helix	473-475	3
α-helix	484-486	3
β-strand	490	1	9
α-helix	491-502	12
β-strand	508-511	4	8
α-helix	517-519	3
α-helix	525-530	6
β-strand	533-536	4	8
α-helix	541-554	14
β-strand	558-564	7	8
β-strand	565	1	10
β-strand	567-573	7	8
α-helix	579-581	3
α-helix	596-599	4
α-helix	606-618	13
α-helix	619-623	5
α-helix	624-630	7
α-helix	632-635	4
α-helix	638-644	7
α-helix	647-654	8
α-helix	660-661	2
α-helix	664-676	13
α-helix	677-681	5
α-helix	682-689	8
α-helix	712-715	4
α-helix	720-737	18
α-helix	739-741	3
α-helix	745-754	10
α-helix	761-765	5
α-helix	770-773	4
α-helix	776-786	11
α-helix	794-797	4
α-helix	809-824	16
α-helix	826-829	4
α-helix	831-839	9
β-strand	844	1	10
α-helix	846-864	19
β-strand	875-879	5	8
α-helix	880-882	3
β-strand	884-888	5	8
α-helix	889-894	6
β-strand	896-898	3	11
β-strand	901-903	3	11
β-strand	908-912	5	12
α-helix	918	1
β-strand	919	1	13
α-helix	920-931	12
β-strand	935-940	6	14
β-strand	943-947	5	14
α-helix	952-960	9
β-strand	962	1	13
β-strand	975-978	4	12
β-strand	979-982	4	14
α-helix	985-986	2
α-helix	991-992	2
β-strand	993-997	5	12

Chain B: 6 helices, 9 β-strands

Element	Residues	Length	Sheet
α-helix	4-15	12
β-strand	22-27	6	15
β-strand	34-39	6	15
α-helix	46-48	3
β-strand	50	1	16
β-strand	51-56	6	15
β-strand	67-70	4	15
β-strand	79	1	17
β-strand	84	1	15
β-strand	85	1	17
α-helix	101-113	13
α-helix	123-131	9
α-helix	133-146	14
β-strand	149	1	16
α-helix	150-151	2

Chain C: 4 helices, 7 β-strands

Element	Residues	Length	Sheet
β-strand	81-84	4	18
β-strand	90-93	4	18
β-strand	100	1	19
α-helix	101-112	12
α-helix	116-118	3
β-strand	119-123	5	18
β-strand	126-128	3	18
β-strand	133	1	19
α-helix	135-137	3
β-strand	144-149	6	18
α-helix	150-151	2

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
UBA7 protein	A	protein	998	Bos taurus	Q5GF34 (AlphaFold model)
Ubiquitin/ISG15-conjugating enzyme E2 L6	B	protein	159	Bos taurus	A5PJC4 (AlphaFold model)
Ubiquitin-like protein ISG15	C	protein	154	Bos taurus	O02741 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>9JTC_1 UBA7 protein (chains A)
MDTLETSKLLDKELYSRQLYVLGLPAMQRIQGAKVLLSGLQGLGAEVAKNLVLMGVGSLT
LHDPHPTCWSDLAAQFLLSEQDLGRSRAEASQKLLAELNGAVQVSVYTGDITKDLLLDFQ
VVVLTASRLEEQLRVGTLCHEHGVCFLVADTRGLVGQLFCDFGENFTVQDPTEAEPLTAN
IQHISQGSPGILTLREEAGTHHFHTGDWVTFSGIEGMVELNGCDPRPLHVREDGTLEIGD
TTAFSCYLRGGAVTEVKRAKTVSHEPLDTALLQPRVVAQSAQKVRARCLHQSFRALHKFQ
QLHGRPPKPWDPVDAEMVVDLAQAMGPLKGTEGEPLEEQLDEALVRTVALSSAGGLSPMA
AVLGAVAAQEVLKAISGKFMPLDQWLYFDALDCLPEDGDPFPNPEDCAPRRCRYDGQTAV
FGTNFQEKLSHQHYLLVGAGAVGCELLKSFALMGLGAGDGGGVTVADMDHVELSNLSRQF
LFRSQDIHRKKAEVAAEATRRLNADLQVTPLNLQLDPTTEDIFGDDFFSGVNGVAAALDT
FEARDYVAARCTHFLKPLLEAGTMGTRGSASVFIPHVTENYKAPSDAASEDAPDPVCTVR
YIPATTEHTVQWAKGEFDDLFCESAKTINSHPQALSSPEDLVKSQKQPLLQTMRGVLTER
PQTWQDCVLWAFGHWQLRFHYGITQLLRTYPPDKVQEDGTPFWSGPKQCPQPLKFDASQD
MHLLYVLAAANLYAQMHGLPGSQDQTALRGLLNLLPLPDPQNLDRIFASELELDSPSGCK
QLHEDLKTWSKGPPLKPLTFEKDNDSNFHVDFVVAAASLRAQNYGIPVASHAETKRIVGR
IIPAVVTTTAAVAGLVGLELYKVVGGPRPRHAFRHSYLHLAENYFSRWVPKAPDIQKFHH
LKWTCWDRLEVPAGQPERTLESLLAHIQELQGLRVTMLLHGSALLYSAGWSEEKQTQHLS
RRVTDLVKKVPGQRVLVLELGYEGEEDDTNFPRLHYKL

Sequence of entity 2 (B), FASTA

>9JTC_2 Ubiquitin/ISG15-conjugating enzyme E2 L6 (chains B)
MAASKRVAKELEDLQKELPKYLRNLSSEEDNVLVWHALLLPERPPYNLKAFRLSISFPRE
YPFQPPTVKFTTRIYHPNVDRDGRVCLPIISKKNWKASTRTSQVLEALNMLVNQPEPGQP
VRLELAEQLTQDPELFDQMAQEFTLQFGVDRPSHHHHHH

Sequence of entity 3 (C), FASTA

>9JTC_3 Ubiquitin-like protein ISG15 (chains C)
MGGDLTVKMLGGQEILVPLRDSMTVSELKQFIAQKINVPAFQQRLAHLDSREVLQEGVPL
VLQGLRAGSTVLLVVQNCISILVRNDKGRSSPYEVQLKQTVAELKQQVCQKERVQADQFW
LSFEGRPMDDEHPLEEYGLMKGCTVFMNLRLRGG

Ligands and cofactors

ID	Name	Formula	Copies
AMP	Adenosine monophosphate	C10 H14 N5 O7 P	1

Primary citation

Elucidating the Mechanism Underlying UBA7-UBE2L6 Disulfide Complex Formation. Chen, P.-T., Yeh, J.-Y., Weng, J.-H. et al. Elife (2025). DOI 10.7554/eLife.105638.1

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