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Solution structure of the DNEDD4 WW3* domain- comm lpsy peptide complex

Analyse Solution structure of the DNEDD4 WW3* domain- comm lpsy peptide complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2EZ5
Type: protein
Length: 57 residues
Chains: 2
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: E3 ubiquitin-protein ligase NEDD4; Commissureless lpsy peptide
EC: 6.3.2.-
UniProt: Q9VVI3, Q24139

Structure

solution nmr · 2 distinct chains · 0% helix, 26% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
W	E3 ubiquitin-protein ligase NEDD4 (EC 6.3.2.-)	protein	46	0% helix, 33% strand	Q9VVI3
P	Commissureless lpsy peptide	protein	11	0% helix, 0% strand	Q24139

Interfaces

1 interface between chains.

W–P · 392 Å² buried · 2 hydrogen bonds · protein-protein

Compared structures

2EZ5 · Solution Structure of the dNedd4 WW3* Domain- Comm LPSY Peptide Complex · the same entry in another collection · chain W against W, TM-score 1.00
Q9VVI3 · AlphaFold monomer V2.0 prediction for E3 ubiquitin-protein ligase nedd-4 (Q9VVI3) · a predicted model of the same protein · chain W against A, TM-score 0.70
Q24139 · AlphaFold monomer V2.0 prediction for protein commissureless 1 (Q24139) · a predicted model of the same protein · chain P against A, TM-score 0.38

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt Q9VVI3
Every structure of UniProt Q24139
Elsewhere: RCSB PDB 2EZ5 · PDBe 2EZ5 · UniProt Q9VVI3 · UniProt Q24139

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