2MPT: WW3 domain of Nedd4L

WW3 domain of Nedd4L in complex with its HECT domain PY motif. Determined by solution NMR. Released 22 Oct 2014.

Method
Solution NMR
Organism
Homo sapiens
Chains
2
Atoms
385
Mol. weight
7.27 kDa
Released
22 Oct 2014

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

Secondary structure: helices and β-sheets

2MPT contains 1 α-helix and 3 β-strands across 2 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: 0 helices, 3 β-strands

ElementResiduesLengthSheet
β-strand483-48751
β-strand493-49751
β-strand502-50431
Chain B: 1 helix, 0 β-strands
ElementResiduesLengthSheet
α-helix926-9316

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
E3 ubiquitin-protein ligase NEDD4-likeAprotein48Homo sapiensQ96PU5 (AlphaFold model)
E3 ubiquitin-protein ligase NEDD4-likeBprotein14Homo sapiensQ96PU5 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>2MPT_1 E3 ubiquitin-protein ligase NEDD4-like (chains A)
GAMEQSFLPPGWEMRIAPNGRPFFIDHNTKTTTWEDPRLKFPVHMRSK
Sequence of entity 2 (B), FASTA
>2MPT_2 E3 ubiquitin-protein ligase NEDD4-like (chains B)
RLDLPPYETFEDLX

Primary citation

Structural Basis of the Activation and Degradation Mechanisms of the E3 Ubiquitin Ligase Nedd4L. Escobedo, A., Gomes, T., Aragon, E. et al. Structure (2014) 22:1446-1457. DOI 10.1016/j.str.2014.08.016 · PubMed

Other PDB entries of the same protein (UniProt Q96PU5 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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