Research workbench
Crystal structure of the active EGFR kinase domain in complex with an ATP analog-peptide conjugate
Analyse Crystal structure of the active EGFR kinase domain in complex with an ATP… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2GS6
- Type
- protein
- Length
- 316 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Epidermal growth factor receptor; Peptide
- EC
- 2.7.10.1
- UniProt
- Q9H2C9
- Ligands
- 112, CL
- Pockets
- 2 · best druggability 0.66
Structure
x-ray diffraction · 2 distinct chains · 38% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Epidermal growth factor receptor (EC 2.7.10.1) | protein | 311 | 38% helix, 17% strand | Q9H2C9 |
| B | Peptide | protein | 5 | 0% helix, 0% strand | — |
Ligands and binding sites
- 112 · Thiophosphoric acid O-((adenosyl-phospho)phospho)-S-acetamidyl-diester · ligand · chains A, B
- CL · Chloride ion · ion · 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, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 521 | 0.66 | 0.77 | 53 | CL, 112 |
| 2 | 158 | 0.53 | 0.79 | 23 | empty |
Interfaces
1 interface between chains.
- A–B · 379 Ų buried · 3 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 covalent (covalent ligand).
Compared structures
- 2GS6 · Crystal Structure of the active EGFR kinase domain in complex with an ATP analog-peptide… · the same entry in another collection · chain B against B, 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 Q9H2C9
- Elsewhere: RCSB PDB 2GS6 · PDBe 2GS6 · UniProt Q9H2C9
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