Research workbench
Crystal structure of the unliganded drosophila epidermal growth factor receptor ectodomain
Analyse Crystal structure of the unliganded drosophila epidermal growth factor receptor… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3I2T
- Type
- protein
- Length
- 542 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Epidermal growth factor receptor, isoform a
- EC
- 2.7.10.-
- UniProt
- Q8MLW0
- Ligands
- NAG, NDG, BMA
- Pockets
- 7 · best druggability 0.72
Structure
x-ray diffraction · 1 distinct chain · 9% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Epidermal growth factor receptor, isoform a (EC 2.7.10.-) | protein | 542 | 9% helix, 26% strand | Q8MLW0 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 7 copies · chains A
- NDG · 2-acetamido-2-deoxy-alpha-D-glucopyranose · sugar · 3 copies · chains A
- BMA · beta-D-mannopyranose · sugar · 3 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 944 | 0.72 | 0.76 | 88 | empty |
| 2 | 94 | 0.51 | 0.83 | 22 | empty |
| 3 | 86 | 0.47 | 0.81 | 20 | empty |
| 4 | 56 | 0.37 | 0.80 | 19 | empty |
| 5 | 65 | 0.37 | 0.78 | 17 | empty |
Modifications
Observed in the structure: 21 disulfide, 5 glycan (disulfide, N-glycosylation).
Compared structures
- 3I2T · Crystal structure of the unliganded Drosophila Epidermal Growth Factor Receptor ectodomain · the same entry in another collection · chain A against A, 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
- Every structure of UniProt Q8MLW0
- Elsewhere: RCSB PDB 3I2T · PDBe 3I2T · UniProt Q8MLW0
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