- FASTA Sequence
- PDBx/mmCIF Format
- PDBx/mmCIF Format (gz)
- BinaryCIF Format (gz)
- PDB Format
- PDB Format (gz)
- PDBML/XML Format (gz)
- Structure Factors (CIF)
- Structure Factors (CIF - gz)
- Validation Full PDF
- Validation (XML - gz)
- Validation (CIF - gz)
- Validation 2fo-fc coefficients (CIF - gz)
- Validation fo-fc coefficients (CIF - gz)
- Biological Assembly 1 (CIF - gz)
- Biological Assembly 2 (CIF - gz)
- Biological Assembly 3 (CIF - gz)
- Biological Assembly 4 (CIF - gz)
- Biological Assembly 1 (PDB - gz)
- Biological Assembly 2 (PDB - gz)
- Biological Assembly 3 (PDB - gz)
- Biological Assembly 4 (PDB - gz)
8GK5
EGFR(T790M/V948R) kinase in complex with osimertinib and benzimidazole allosteric inhibitor
Domain Annotation: SCOP2 Classification SCOP2 Database Homepage
Chains | Type | Family Name | Domain Identifier | Family Identifier | Provenance Source (Version) |
---|---|---|---|---|---|
A | SCOP2B Superfamily | Protein kinase-like (PK-like) | 8043964 | 3000066 | SCOP2B (2022-06-29) |
B | SCOP2B Superfamily | Protein kinase-like (PK-like) | 8043964 | 3000066 | SCOP2B (2022-06-29) |
C | SCOP2B Superfamily | Protein kinase-like (PK-like) | 8043964 | 3000066 | SCOP2B (2022-06-29) |
D | SCOP2B Superfamily | Protein kinase-like (PK-like) | 8043964 | 3000066 | SCOP2B (2022-06-29) |
Protein Family Annotation Pfam Database Homepage
Chains | Accession | Name | Description | Comments | Source | |
---|---|---|---|---|---|---|
PF07714 | Protein tyrosine and serine/threonine kinase (PK_Tyr_Ser-Thr) | Protein tyrosine and serine/threonine kinase | Protein phosphorylation, which plays a key role in most cellular activities, is a reversible process mediated by protein kinases and phosphoprotein phosphatases. Protein kinases catalyse the transfer of the gamma phosphate from nucleotide triphosph ... | Protein phosphorylation, which plays a key role in most cellular activities, is a reversible process mediated by protein kinases and phosphoprotein phosphatases. Protein kinases catalyse the transfer of the gamma phosphate from nucleotide triphosphates (often ATP) to one or more amino acid residues in a protein substrate side chain, resulting in a conformational change affecting protein function. Phosphoprotein phosphatases catalyse the reverse process. Protein kinases fall into three broad classes, characterised with respect to substrate specificity [1]; Serine/threonine-protein kinases, tyrosine-protein kinases, and dual specificity protein kinases (e.g. MEK - phosphorylates both Thr and Tyr on target proteins). This entry represents the catalytic domain found in a number of serine/threonine- and tyrosine-protein kinases. It does not include the catalytic domain of dual specificity kinases. | Domain |
Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage
InterPro: Protein Family Classification InterPro Database Homepage
Chains | Accession | Name | Type |
---|---|---|---|
IPR016245 | Tyrosine protein kinase, EGF/ERB/XmrK receptor | Family | |
IPR020635 | Tyrosine-protein kinase, catalytic domain | Domain | |
IPR000719 | Protein kinase domain | Domain | |
IPR032778 | Growth factor receptor domain 4 | Domain | |
IPR006212 | Furin-like repeat | Repeat | |
IPR017441 | Protein kinase, ATP binding site | Binding Site | |
IPR001245 | Serine-threonine/tyrosine-protein kinase, catalytic domain | Domain | |
IPR009030 | Growth factor receptor cysteine-rich domain superfamily | Homologous Superfamily | |
IPR008266 | Tyrosine-protein kinase, active site | Active Site | |
IPR036941 | Receptor L-domain superfamily | Homologous Superfamily | |
IPR049328 | Epidermal growth factor receptor-like, transmembrane-juxtamembrane segment | Domain | |
IPR000494 | Receptor L-domain | Domain | |
IPR011009 | Protein kinase-like domain superfamily | Homologous Superfamily | |
IPR006211 | Furin-like cysteine-rich domain | Domain | |
IPR050122 | Receptor Tyrosine Kinase | Family |