Research workbench

Spatial structure of the ERBB4 dimeric tm domain

Analyse Spatial structure of the ERBB4 dimeric tm domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2LCX
Type: protein
Length: 88 residues
Chains: 2
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Receptor tyrosine-protein kinase erbb-4
EC: 2.7.10.1
UniProt: Q15303

Structure

solution nmr · 1 distinct chain · 59% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Receptor tyrosine-protein kinase erbb-4 (EC 2.7.10.1)	protein	44	59% helix, 0% strand	Q15303

Interfaces

1 interface between chains.

A–B · 427 Å² buried · 0 hydrogen bonds · protein-protein

Compared structures

2LCX · Spatial Structure of the ErbB4 dimeric TM domain · the same entry in another collection · chain A against A, TM-score 1.00
Q15303 · AlphaFold monomer V2.0 prediction for receptor tyrosine-protein kinase erbb-4 (Q15303) · a predicted model of the same protein · chain A against A, TM-score 0.63

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 Q15303
Elsewhere: RCSB PDB 2LCX · PDBe 2LCX · UniProt Q15303

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.