4A4B: E3 ubiquitin-protein ligase cbl

Structure of modified phosphoTyr371-c-Cbl-UbcH5B-ZAP-70 complex. Determined by X-ray diffraction at 2.79 Å resolution. Released 25 Jan 2012.

Method
X-ray diffraction
Resolution
2.79 Å
Organism
HOMO SAPIENS
Chains
3
Atoms
4,284
Mol. weight
63.41 kDa
Ligands
ZN, CA
Released
25 Jan 2012

Explore 4A4B in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4A4B contains 30 α-helices and 22 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: 20 helices, 14 β-strands

ElementResiduesLengthSheet
α-helix53-7018
α-helix84-10118
α-helix106-1105
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-helix238-24811
α-helix251-2533
α-helix254-2585
α-helix259-2635
β-strand26812
α-helix274-2829
β-strand290-29562
β-strand303-30862
β-strand314-31742
α-helix324-33310
β-strand339-34022
α-helix350-3534
α-helix355-3584
β-strand36013
α-helix365-37410
β-strand38014
β-strand38814
β-strand391-39445
β-strand399-40025
α-helix402-4098
β-strand425-42845
β-strand43013
Chain B: 1 helix, 1 β-strand
ElementResiduesLengthSheet
β-strand812
α-helix9-113
Chain C: 9 helices, 7 β-strands
ElementResiduesLengthSheet
α-helix3-1513
α-helix17-182
β-strand21-2666
β-strand29-38106
α-helix39-402
β-strand49-5576
α-helix64-652
β-strand66-6946
β-strand7817
β-strand8316
β-strand8417
α-helix87-893
α-helix99-11113
α-helix121-1299
α-helix131-14111
α-helix142-1465

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
E3 ubiquitin-protein ligase cblAprotein391HOMO SAPIENSP22681 (AlphaFold model)
Tyrosine-protein kinase zap-70Bprotein12HOMO SAPIENSP43403 (AlphaFold model)
Ubiquitin-conjugating enzyme E2 D2Cprotein147HOMO SAPIENSP62837 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>4A4B_1 E3 UBIQUITIN-PROTEIN LIGASE CBL (chains A)
GSPPGTVDKKMVEKCWKLMDKVVRLCQNPKLALKNSPPYILDLLPDTYQHLRTILSRYEG
KMETLGENEYFRVFMENLMKKTKQTISLFKEGKERMYEENSQPRRNLTKLSLIFSHMLAE
LKGIFPSGLFQGDTFRITKADAAEFWRKAFGEKTIVPWKSFRQALHEVHPISSGLEAMAL
KSTIDLTCNDYISVFEFDIFTRLFQPWSSLLRNWNSLAVTHPGYMAFLTYDEVKARLQKF
IHKPGSYIFRLSCTRLGQWAIGYVTADGNILQTIPHNKPLFQALIDGFREGFYLFPDGRN
QNPDLTGLCEPTPQDHIKVTQEQFELYCEMGSTFQLCKICAENDKDVKIEPCGHLMCTSC
LTSWQESEGQGCPFCRCEIKGTEPIVVDPFD
Sequence of entity 2 (B), FASTA
>4A4B_2 TYROSINE-PROTEIN KINASE ZAP-70 (chains B)
TLNSDGYTPEPA
Sequence of entity 3 (C), FASTA
>4A4B_3 UBIQUITIN-CONJUGATING ENZYME E2 D2 (chains C)
MALKRIHKELNDLARDPPAQCSAGPVGDDMFHWQATIMGPNDSPYQGGVFFLTIHFPTDY
PFKPPKVAFTTRIYHPNINSNGSICLDILRSQWSPALTISKVLLSICSLLCDPNPDDPLV
PEIARIYKTDREKYNRIAREWTQKYAM

Ligands and cofactors

IDNameFormulaCopies
ZNZinc ionZn2
CACalcium ionCa1

Primary citation

Structural Basis for Autoinhibition and Phosphorylation-Dependent Activation of C-Cbl. Dou, H., Buetow, L., Hock, A. et al. Nat Struct Mol Biol (2012) 19:184. DOI 10.1038/NSMB.2231 · PubMed

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

Browse structure collections

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