MolNFT v1 · #58787 · protein
Dual specific BH1 Fab in complex with the extracellular domain of HER2/ERBB-2
3BE1: “Dual specific BH1 Fab in complex with the extracellular domain of HER2/ERBB-2”. X-ray diffraction. MolNFT v1 #58787 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 3BE1
- Type
- protein
- Length
- 1,012 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P04626
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 583 | — | P04626 |
| H | — | protein | 213 | — | — |
| L | — | protein | 216 | — | — |
Compared structures
- 3BE1 · Dual specific bH1 Fab in complex with the extracellular domain of HER2/ErbB-2 · 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 0.94
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 3BE1 · PDBe 3BE1 · UniProt P04626
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