MolNFT v1 · #144018 · protein
Structure of trastuzumab Fab mutant in complex with HER2 extracellular domain
6BGT: “Structure of trastuzumab Fab mutant in complex with HER2 extracellular domain”. X-ray diffraction, 1 ligand (NAG). MolNFT v1 #144018 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6BGT
- Type
- protein
- Length
- 1,010 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P04626, Q7Z3Y4, P0DOX5
- Ligands
- NAG
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| C | — | protein | 589 | — | P04626 |
| A | — | protein | 211 | — | Q7Z3Y4 |
| B | — | protein | 210 | — | P0DOX5 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · chains C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6BGT · Structure of Trastuzumab Fab mutant in complex with Her2 extracellular domain · the same entry in another collection · chain C against C, 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 C against A, TM-score 0.95
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 Q7Z3Y4
- Every structure of UniProt P0DOX5
- Elsewhere: RCSB PDB 6BGT · PDBe 6BGT · UniProt P04626 · UniProt Q7Z3Y4 · UniProt P0DOX5
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