MolNFT v2 · #154214 · protein
HuA21-scFv in complex with the extracellular domain(ECD) of HER2
6J71: “HuA21-scFv in complex with the extracellular domain(ECD) of HER2”. X-ray diffraction at 2.918, 2 ligands (BMA, NAG). MolNFT v2 #154214 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6J71
- Type
- protein
- Length
- 851 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.918
- Source
- Homo sapiens
- UniProt
- P04626
- Ligands
- BMA, NAG
Structure
x-ray diffraction · resolution 2.918 · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 618 | — | P04626 |
| B | — | protein | 233 | — | — |
Ligands and binding sites
- BMA · beta-D-mannopyranose · sugar · 2 copies · chains A, B
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6J71 · HUA21-scfv in complex with the extracellular DOMAIN(ECD) of HER2 · 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 0.99
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 6J71 · PDBe 6J71 · UniProt P04626
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