Research workbench
Crystal structure of N-terminal three extracellular domains of ERBB4/HER4
Analyse Crystal structure of N-terminal three extracellular domains of ERBB4/HER4 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3U2P
- Type
- protein
- Length
- 479 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Receptor tyrosine-protein kinase erbb-4
- EC
- 2.7.10.1
- UniProt
- Q15303
- Ligands
- NAG
- Pockets
- 2 · best druggability 0.37
Structure
x-ray diffraction · 1 distinct chain · 13% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Receptor tyrosine-protein kinase erbb-4 (EC 2.7.10.1) | protein | 479 | 13% helix, 26% strand | Q15303 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 5 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 71 | 0.37 | 0.78 | 18 | empty |
| 2 | 59 | 0.28 | 0.74 | 17 | empty |
Modifications
Observed in the structure: 17 disulfide, 5 glycan (disulfide, N-glycosylation).
Compared structures
- 3U2P · Crystal structure of N-terminal three extracellular domains of ErbB4/Her4 · the same entry in another collection · chain A against A, TM-score 1.00
- Q15303 · AlphaFold monomer V2.0 prediction for receptor tyrosine-protein kinase erbb-4 (Q15303) · a predicted model of the same protein · chain A against A, TM-score 0.82
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 Q15303
- Elsewhere: RCSB PDB 3U2P · PDBe 3U2P · UniProt Q15303
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