MolNFT v1 · #16161 · protein
Structure of the extracellular domain of human epidermal growth factor (EGF) receptor in an inactive (low pH) complex with EGF.
1NQL · Epidermal growth factor receptor: “Structure of the extracellular domain of human epidermal growth factor (EGF) receptor in an inactive (low pH)…”. X-ray diffraction, 2 ligands (NAG, BMA), 5 pockets (best druggability 0.71). MolNFT…
- PDB
- 1NQL
- Type
- protein
- Length
- 660 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Epidermal growth factor receptor; Epidermal growth factor
- UniProt
- P01133
- Ligands
- NAG, BMA
- Pockets
- 5 · best druggability 0.71
Structure
x-ray diffraction · 2 distinct chains · 11% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Epidermal growth factor receptor | protein | 612 | 12% helix, 25% strand | — |
| B | Epidermal growth factor | protein | 48 | 0% helix, 40% strand | P01133 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 11 copies · chains A
- BMA · beta-D-mannopyranose · sugar · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 794 | 0.71 | 0.77 | 99 | empty |
| 2 | 74 | 0.32 | 0.75 | 17 | empty |
| 3 | 86 | 0.32 | 0.73 | 16 | empty |
| 4 | 76 | 0.31 | 0.73 | 21 | empty |
| 5 | 63 | 0.28 | 0.73 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 830 Ų buried · 8 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 28 disulfide, 7 glycan (disulfide, N-glycosylation, glycosylation).
Compared structures
- 1NQL · Structure of the extracellular domain of human epidermal growth factor (EGF) receptor in… · the same entry in another collection · chain A against A, TM-score 1.00
- P01133 · AlphaFold monomer V2.0 prediction for pro-epidermal growth factor (P01133) · a predicted model of the same protein · chain B against A, TM-score 0.66
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 P01133
- Elsewhere: RCSB PDB 1NQL · PDBe 1NQL · UniProt P01133
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