2Y1N: C-Cbl-ZAP-70 peptide complex

Structure of c-Cbl-ZAP-70 peptide complex. Determined by X-ray diffraction at 2.0 Å resolution. Released 18 Jan 2012.

Method
X-ray diffraction
Resolution
2.0 Å
Organism
HOMO SAPIENS
Chains
4
Atoms
6,623
Mol. weight
92.89 kDa
Ligands
CA, ZN
Released
18 Jan 2012

Explore 2Y1N in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2Y1N contains 47 α-helices and 32 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: 22 helices, 16 β-strands

ElementResiduesLengthSheet
α-helix54-7017
α-helix84-10118
α-helix106-1116
α-helix113-13624
α-helix137-1415
α-helix146-16823
α-helix170-1723
α-helix176-1783
α-helix184-19411
β-strand199-20131
α-helix202-2109
α-helix218-22811
β-strand235-23731
α-helix238-24710
α-helix251-2533
α-helix254-2585
α-helix259-2635
β-strand26812
α-helix274-2818
α-helix282-2843
β-strand290-29562
β-strand30013
β-strand30213
β-strand303-30862
β-strand314-31742
α-helix324-33310
β-strand339-34022
α-helix345-3473
α-helix365-3717
α-helix372-3765
β-strand38014
β-strand38814
β-strand391-39445
β-strand399-40025
α-helix402-41110
β-strand41516
β-strand42216
β-strand425-42845
Chains B and D: 2 helices, 1 β-strand
ElementResiduesLengthSheet
α-helix71
β-strand812
α-helix9-113
Chain C: 21 helices, 14 β-strands
ElementResiduesLengthSheet
α-helix53-7119
α-helix801
α-helix84-10118
α-helix106-1116
α-helix113-13624
α-helix137-1415
α-helix146-16823
α-helix170-1723
α-helix184-19411
β-strand199-20137
α-helix202-2109
α-helix218-22811
β-strand235-23737
α-helix238-24710
α-helix251-2533
α-helix254-2585
α-helix259-2635
β-strand26818
α-helix274-2807
β-strand290-29568
β-strand303-30868
β-strand314-31748
α-helix324-33310
β-strand339-34028
α-helix345-3484
α-helix365-3717
α-helix372-3765
β-strand38019
β-strand38819
β-strand391-394410
β-strand399-400210
α-helix402-41110
β-strand415111
β-strand422111
β-strand425-428410

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
E3 ubiquitin-protein ligaseA, Cprotein389HOMO SAPIENSP22681 (AlphaFold model)
Tyrosine-protein kinase zap-70 zap-70,70 kda zeta-associated protein, syk-related tyrosine kinaseB, Dprotein12HOMO SAPIENSP43403 (AlphaFold model)
Sequence of entity 1 (A, C), FASTA
>2Y1N_1 E3 UBIQUITIN-PROTEIN LIGASE (chains A, C)
PPGTVDKKMVEKCWKLMDKVVRLCQNPKLALKNSPPYILDLLPDTYQHLRTILSRYEGKM
ETLGENEYFRVFMENLMKKTKQTISLFKEGKERMYEENSQPRRNLTKLSLIFSHMLAELK
GIFPSGLFQGDTFRITKADAAEFWRKAFGEKTIVPWKSFRQALHEVHPISSGLEAMALKS
TIDLTCNDYISVFEFDIFTRLFQPWSSLLRNWNSLAVTHPGYMAFLTYDEVKARLQKFIH
KPGSYIFRLSCTRLGQWAIGYVTADGNILQTIPHNKPLFQALIDGFREGFYLFPDGRNQN
PDLTGLCEPTPQDHIKVTQEQYELYCEMGSTFQLCKICAENDKDVKIEPCGHLMCTSCLT
SWQESEGQGCPFCRCEIKGTEPIVVDPFD
Sequence of entity 2 (B, D), FASTA
>2Y1N_2 TYROSINE-PROTEIN KINASE ZAP-70 ZAP-70,70 KDA ZETA-ASSOCIATED PROTEIN, SYK-RELATED TYROSINE KINASE (chains B, D)
TLNSDGYTPEPA

Ligands and cofactors

IDNameFormulaCopies
CACalcium ionCa2
ZNZinc ionZn4

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:

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