Research workbench
Crystal structure of the extracellular region of rat HER2
Analyse Crystal structure of the extracellular region of rat HER2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1N8Y
- Type
- protein
- Length
- 592 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protooncoprotein
- Ligands
- NAG
- Pockets
- 4 · best druggability 0.67
Structure
x-ray diffraction · 1 distinct chain · 10% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| C | Protooncoprotein | protein | 592 | 10% helix, 26% strand | — |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 5 copies · chains C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 556 | 0.67 | 0.77 | 64 | empty |
| 2 | 139 | 0.51 | 0.79 | 23 | empty |
| 3 | 169 | 0.48 | 0.77 | 27 | NAG |
| 4 | 65 | 0.30 | 0.75 | 16 | empty |
Modifications
Observed in the structure: 22 disulfide, 3 glycan (disulfide, N-glycosylation).
Compared structures
- 1N8Y · Crystal structure of the extracellular region of rat HER2 · the same entry in another collection · chain C against C, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Elsewhere: RCSB PDB 1N8Y · PDBe 1N8Y
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