Research workbench
Heterodimeric association of transmembrane domains of ERBB1 and ERBB2 receptors enabling kinase activation
Analyse Heterodimeric association of transmembrane domains of ERBB1 and ERBB2 receptors… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2KS1
- Type
- protein
- Length
- 88 residues
- Chains
- 2
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Receptor tyrosine-protein kinase erbb-2; Epidermal growth factor receptor
- EC
- 2.7.10.1
- UniProt
- P04626, P00533
Structure
solution nmr · 2 distinct chains · 58% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Receptor tyrosine-protein kinase erbb-2 (EC 2.7.10.1) | protein | 44 | 66% helix, 0% strand | P04626 |
| B | Epidermal growth factor receptor (EC 2.7.10.1) | protein | 44 | 50% helix, 0% strand | P00533 |
Interfaces
1 interface between chains.
- A–B · 412 Ų buried · 1 hydrogen bond · protein-protein
Compared structures
- 2KS1 · Heterodimeric association of Transmembrane domains of ErbB1 and ErbB2 receptors Enabling… · the same entry in another collection · chain A against A, TM-score 1.00
- P04626 · AlphaFold monomer V2.0 prediction for receptor tyrosine-protein kinase erbb-2 (P04626) · a predicted model of the same protein · chain A against A, TM-score 0.61
- P00533 · AlphaFold monomer V2.0 prediction for epidermal growth factor receptor (P00533) · a predicted model of the same protein · chain B against A, TM-score 0.58
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 P04626
- Every structure of UniProt P00533
- Elsewhere: RCSB PDB 2KS1 · PDBe 2KS1 · UniProt P04626 · UniProt P00533
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