9ERZ: CBL-TKBD

Structure of CBL-TKBD bound to Ubiquitin-fused CBLock peptide. Determined by X-ray diffraction at 2.02 Å resolution. Released 14 May 2025.

Method
X-ray diffraction
Resolution
2.02 Å
Organism
Homo sapiens
Chains
4
Atoms
6,415
Mol. weight
96.27 kDa
Ligands
CA
Released
14 May 2025

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

Secondary structure: helices and β-sheets

9ERZ contains 48 α-helices and 29 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: 20 helices, 7 β-strands

ElementResiduesLengthSheet
α-helix49-513
α-helix53-7018
α-helix73-753
α-helix84-10219
α-helix106-1116
α-helix113-13624
α-helix137-1415
α-helix146-16823
α-helix176-1783
α-helix184-19411
β-strand199-20131
α-helix202-21211
α-helix218-22811
β-strand235-23731
α-helix238-24710
α-helix251-2533
α-helix254-2585
α-helix259-2635
β-strand268-27142
α-helix274-2818
α-helix282-2843
β-strand290-29562
β-strand303-30862
β-strand314-31742
α-helix324-33411
β-strand339-34022
α-helix350-3523
Chain B: 5 helices, 7 β-strands
ElementResiduesLengthSheet
β-strand2-653
β-strand12-1653
β-strand2214
α-helix23-3412
α-helix38-403
β-strand43-4533
β-strand48-4923
α-helix50-512
β-strand5514
β-strand66-6943
α-helix80-823
α-helix83-9210
Chain C: 18 helices, 7 β-strands
ElementResiduesLengthSheet
α-helix53-7018
α-helix73-753
α-helix84-10118
α-helix106-1116
α-helix113-13624
α-helix137-1415
α-helix146-16823
α-helix176-1783
α-helix184-19411
β-strand199-20135
α-helix202-2109
α-helix218-22811
β-strand235-23735
α-helix238-24710
α-helix251-2533
α-helix254-2585
α-helix259-2635
β-strand268-27146
α-helix274-2829
β-strand290-29566
β-strand303-30866
β-strand314-31746
α-helix324-33310
β-strand339-34026
α-helix350-3523
Chain D: 5 helices, 8 β-strands
ElementResiduesLengthSheet
β-strand2-547
β-strand13-1647
β-strand2218
α-helix23-3412
α-helix38-403
β-strand41-4449
β-strand4919
β-strand5518
α-helix57-593
β-strand66-6727
β-strand68-7149
α-helix80-823
α-helix83-9210

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
E3 ubiquitin-protein ligase CBLA, Cprotein311Homo sapiensP22681 (AlphaFold model)
Polyubiquitin-C,Ub-fused CBLock peptideB, Dprotein107Homo sapiensP0CG48 (AlphaFold model)
Sequence of entity 1 (A, C), FASTA
>9ERZ_1 E3 ubiquitin-protein ligase CBL (chains A, C)
GSPPGTVDKKMVEKCWKLMDKVVRLCQNPKLALKNSPPYILDLLPDTYQHLRTILSRYEG
KMETLGENEYFRVFMENLMKKTKQTISLFKEGKERMYEENSQPRRNLTKLSLIFSHMLAE
LKGIFPSGLFQGDTFRITKADAAEFWRKAFGEKTIVPWKSFRQALHEVHPISSGLEAMAL
KSTIDLTCNDYISVFEFDIFTRLFQPWSSLLRNWNSLAVTHPGYMAFLTYDEVKARLQKF
IHKPGSYIFRLSCTRLGQWAIGYVTADGNILQTIPHNKPLFQALIDGFREGFYLFPDGRN
QNPDLTGLCEP
Sequence of entity 2 (B, D), FASTA
>9ERZ_2 Polyubiquitin-C,Ub-fused CBLock peptide (chains B, D)
GSGGSMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRT
LSDYNIQKESTLHLVLRLRAAPGGSMTVEEMDSWIKSWDQMHHHHHH

Ligands and cofactors

IDNameFormulaCopies
CACalcium ionCa2

Primary citation

Locking CBL TKBD in its native conformation presents a novel therapeutic opportunity in mutant CBL-dependent leukemia. Ahmed, S.F., Anand, J., Zhang, W. et al. Mol Ther (2025) 33:3624-3643. DOI 10.1016/j.ymthe.2025.04.042 · PubMed

Other PDB entries of the same protein (UniProt P22681 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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