9LW4: UbCh8-ISG15 complex

UbCh8-ISG15 complex. Determined by X-ray diffraction at 2.7 Å resolution. Released 1 Jul 2026.

Method: X-ray diffraction
Resolution: 2.7 Å
Organism: Homo sapiens
Chains: 4
Atoms: 3,891
Mol. weight: 52.97 kDa
Ligands: 3CN
Released: 1 Jul 2026

Explore 9LW4 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9LW4 contains 21 α-helices and 28 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: 3 helices, 7 β-strands

Element	Residues	Length	Sheet
β-strand	82-87	6	3
β-strand	93-98	6	3
β-strand	103	1	4
α-helix	104-115	12
β-strand	122-126	5	3
β-strand	129-130	2	3
α-helix	131-132	2
β-strand	136	1	4
α-helix	137-140	4
β-strand	147-152	6	3

Chain B: 7 helices, 7 β-strands

Element	Residues	Length	Sheet
α-helix	3-16	14
β-strand	22-28	7	1
β-strand	31-39	9	1
α-helix	46-48	3
β-strand	50	1	2
β-strand	51-56	6	1
β-strand	67-70	4	1
β-strand	84	1	1
α-helix	101-113	13
α-helix	123-131	9
α-helix	133-147	15
α-helix	148	1
β-strand	149	1	2
α-helix	150	1

Chain C: 8 helices, 7 β-strands

Element	Residues	Length	Sheet
α-helix	3-16	14
β-strand	22-28	7	5
β-strand	31-39	9	5
α-helix	46-48	3
β-strand	50	1	6
β-strand	51-56	6	5
β-strand	67-70	4	5
β-strand	84	1	5
α-helix	88-90	3
α-helix	101-113	13
α-helix	123-131	9
α-helix	133-147	15
α-helix	148	1
β-strand	149	1	6
α-helix	150	1

Chain D: 3 helices, 7 β-strands

Element	Residues	Length	Sheet
β-strand	82-87	6	7
β-strand	93-98	6	7
β-strand	103	1	8
α-helix	104-115	12
β-strand	122-126	5	7
β-strand	129-130	2	7
α-helix	131-132	2
β-strand	136	1	8
α-helix	137-139	3
β-strand	147-152	6	7

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Ubiquitin/ISG15-conjugating enzyme E2 L6	B, C	protein	152	Homo sapiens	O14933 (AlphaFold model)
Ubiquitin-like protein ISG15	A, D	protein	76	Homo sapiens	P05161 (AlphaFold model)

Sequence of entity 1 (B, C), FASTA

>9LW4_1 Ubiquitin/ISG15-conjugating enzyme E2 L6 (chains B, C)
SMASMRVVKELEDLQKKPPPYLRNLSSDDANVLVWHALLLPDQPPYHLKAFNLRISFPPE
YPFKPPMIKFTTKIYHPNVDENGQICLPIISSENWKPSTKTSQVLEALNVLVNRPNIREP
LRMDLADLLTQNPELFRKNAEEFTLRFGVDRP

Sequence of entity 2 (A, D), FASTA

>9LW4_2 Ubiquitin-like protein ISG15 (chains A, D)
PLSILVRNNKGRSSTYEVRLTQTVAHLKQQVSGLEGVQDDLFWLTFEGKPLEDQLPLGEY
GLKPLSTVFMNLRLRG

Ligands and cofactors

ID	Name	Formula	Copies
3CN	3-aminopropane	C3 H9 N	2

Water and common crystallization additives (EDO, PEG, CL) are not listed.

Primary citation

ISGylation mechanism uncovers conformational specificity for HECT-family E3 ligase HERC5. Sahoo, P., Parmar, G.G., Lenka, D.R. et al. Cell Rep (2026) 45:117565-117565. DOI 10.1016/j.celrep.2026.117565 · PubMed

Other PDB entries of the same protein (UniProt O14933 (AlphaFold model), which also has an AlphaFold model), best resolution first:

1WZV 2.1 Å, Crystal Structure of UbcH8
1WZW 2.4 Å, Crystal Structure of UbcH8
8SE9 3.2 Å, Cryo-EM structure of a double loaded human UBA7-UBE2L6-ISG15 thioester mimetic complex…
8SEB 3.24 Å, Cryo-EM structure of a single loaded human UBA7-UBE2L6-ISG15 adenylate complex
8SV8 3.38 Å, Cryo-EM structure of a double loaded human UBA7-UBE2L6-ISG15 thioester mimetic complex…
8SEA 3.4 Å, Cryo-EM structure of a double loaded human UBA7-UBE2L6-ISG15 thioester mimetic complex…
8OIF 3.5 Å, Structure of the UBE1L activating enzyme bound to ISG15 and UBE2L6
2KJH NMR based structural model of the UBCH8-UBIQUITIN complex

Browse structure collections

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