10ZJ: Cbl-B

Structure of Cbl-B bound to compound 8. Determined by X-ray diffraction at 1.77 Å resolution. Released 1 Jul 2026.

Method: X-ray diffraction
Resolution: 1.77 Å
Organism: Homo sapiens
Chains: 1
Atoms: 3,570
Mol. weight: 48.64 kDa
Ligands: ZN, MG, A1DCC
Released: 1 Jul 2026

Explore 10ZJ in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

10ZJ contains 21 α-helices and 12 β-strands across 1 chain. 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: 21 helices, 12 β-strands

Element	Residues	Length	Sheet
α-helix	43-60	18
α-helix	63-65	3
α-helix	74-91	18
α-helix	95-102	8
α-helix	105-128	24
α-helix	129-133	5
α-helix	138-160	23
α-helix	162-164	3
α-helix	168-170	3
α-helix	176-186	11
β-strand	191-193	3	1
α-helix	194-204	11
α-helix	210-220	11
β-strand	227-229	3	1
α-helix	230-239	10
α-helix	243-245	3
α-helix	246-250	5
α-helix	251-255	5
β-strand	260-263	4	2
α-helix	266-274	9
β-strand	282-287	6	2
β-strand	296-300	5	2
β-strand	306-309	4	2
α-helix	316-325	10
β-strand	331-332	2	2
α-helix	342-345	4
α-helix	357-364	8
β-strand	372	1	3
β-strand	380	1	3
β-strand	383-386	4	4
β-strand	391-392	2	4
α-helix	394-402	9
β-strand	417-420	4	4

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
E3 ubiquitin-protein ligase CBL-B	A	protein	410	Homo sapiens	Q13191 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>10ZJ_1 E3 ubiquitin-protein ligase CBL-B (chains A)
MHHHHHHHHGENLYFQGSPKQAAADRRTVEKTWKLMDKVVRLCQNPKLQLKNSPPYILDI
LPDTYQHLRLILSKYDDNQKLAQLSENEYFKIYIDSLMKKSKRAIRLFKEGKERMYEEQS
QDRRNLTKLSLIFSHMLAEIKAIFPNGQFQGDNFRITKADAAEFWRKFFGDKTIVPWKVF
RQCLHEVHQISSGLEAMALKSTIDLTCNDYISVFEFDIFTRLFQPWGSILRNWNFLAVTH
PGYMAFLTYDEVKARLQKYSTKPGSYIFRLSCTRLGQWAIGYVTGDGNILQTIPHNKPLF
QALIDGSREGFYLYPDGRSYNPDLTGLCEPTPHDHIKVTQEQYELYCEMGSTFQLCKICA
ENDKDVKIEPCGHLMCTSCLTAWQESDGQGCPFCRCEIKGTEPIIVDPFD

Ligands and cofactors

ID	Name	Formula	Copies
ZN	Zinc ion	Zn	2
MG	Magnesium ion	Mg	1
A1DCC	6-{[(3,3-difluoropropyl)amino]methyl}-2-(3-{3-[(R)-fluoro(4-methyl-4H-1,2,4-tri…	C26 H25 F6 N5 O2	1

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

Primary citation

Optimization and In Vivo Characterization of a Series of Cbl‐b Inactive-State Inhibitors. Lambrecht, M.J., Liang, J., Ung, P.M. et al. ACS Med Chem Lett (2026) 17:1253-1257. DOI 10.1021/acsmedchemlett.6c00103 · PubMed

Other PDB entries of the same protein (UniProt Q13191 (AlphaFold model), which also has an AlphaFold model), best resolution first:

8QTG 1.42 Å, Crystal structure of CBL-b in complex with an allosteric inhibitor (compound 9)
8QTJ 1.52 Å, Crystal structure of Cbl-b in complex with an allosteric inhibitor (compound 30)
2OOA 1.56 Å, crystal structure of the UBA domain from Cbl-b ubiquitin ligase
9FQJ 1.56 Å, E3 ligase Cbl-b in complex with a carbamate scaffold inhibitor (compound 12)
9XZD 1.65 Å, E3 ubiquitin-protein ligase CBL-B in complex with compound 8
9I0B 1.66 Å, E3 ubiquitin ligase CBL-B in complex with inhibitor
2J6F 1.7 Å, N-terminal SH3 domain of cms (CD2AP human homolog) bound to cbl-B peptide
9XZB 1.75 Å, E3 ubiquitin-protein ligase CBL-B in complex with compound 2
8VW5 1.76 Å, Crystal structure of Cbl-b TKB bound to compound 2
9FQH 1.79 Å, E3 ligase Cbl-b in complex with a triazolone core inhibitor (compound 1)
9XZC 1.8 Å, E3 ubiquitin-protein ligase CBL-B in complex with compound 6
8GCY 1.81 Å, Co-crystal structure of CBL-B in complex with N-Aryl isoindolin-1-one inhibitor

Browse structure collections

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