Research workbench

NEDD4L WW2 domain in complex with a SMAD7 derived peptide

Analyse NEDD4L WW2 domain in complex with a SMAD7 derived peptide in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2LTY
Type: protein
Length: 49 residues
Chains: 2
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: E3 ubiquitin-protein ligase NEDD4-like; SMAD7 derived peptide
UniProt: Q96PU5, O15105

Structure

solution nmr · 2 distinct chains · 0% helix, 31% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	E3 ubiquitin-protein ligase NEDD4-like	protein	34	0% helix, 44% strand	Q96PU5
B	SMAD7 derived peptide	protein	15	0% helix, 0% strand	O15105

Interfaces

1 interface between chains.

A–B · 609 Å² buried · 11 hydrogen bonds · protein-protein

Compared structures

2LTY · NEDD4L WW2 domain in complex with a Smad7 derived peptide · the same entry in another collection · chain A against A, TM-score 1.00
Q96PU5 · AlphaFold monomer V2.0 prediction for E3 ubiquitin-protein ligase NEDD4-like (Q96PU5) · a predicted model of the same protein · chain A against A, TM-score 0.65
O15105 · AlphaFold monomer V2.0 prediction for mothers against decapentaplegic homolog 7 (O15105) · a predicted model of the same protein · chain B against A, TM-score 0.21

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 Q96PU5
Every structure of UniProt O15105
Elsewhere: RCSB PDB 2LTY · PDBe 2LTY · UniProt Q96PU5 · UniProt O15105

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