Research workbench
NMR spatial structure of HER2 tm domain dimer in dpc micelles.
Analyse NMR spatial structure of HER2 tm domain dimer in dpc micelles. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5OB4
- 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
- EC
- 2.7.10.1
- UniProt
- P04626
Structure
solution nmr · 1 distinct chain · 64% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Receptor tyrosine-protein kinase erbb-2 (EC 2.7.10.1) | protein | 44 | 64% helix, 0% strand | P04626 |
Interfaces
1 interface between chains.
- A–B · 348 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 5OB4 · NMR spatial structure of HER2 TM domain dimer in DPC micelles. · 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 B against A, TM-score 0.57
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
- Elsewhere: RCSB PDB 5OB4 · PDBe 5OB4 · UniProt P04626
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