- FASTA Sequence
- PDBx/mmCIF Format
- PDBx/mmCIF Format (gz)
- BinaryCIF Format (gz)
- Legacy PDB Format
- Legacy 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 1 (PDB - gz)
Crystal structure of c-Src in complex with covalent inhibitor DC-Srci-6668
Domain Annotation: SCOP2 Classification SCOP2 Database Homepage
Chains | Type | Family Name | Domain Identifier | Family Identifier | Provenance Source (Version) |
---|---|---|---|---|---|
A | SCOP2B Superfamily | SH3-domain | 8033421 | 3000153 | SCOP2B (2022-06-29) |
A | SCOP2B Superfamily | SH2 domain | 8037200 | 3000197 | SCOP2B (2022-06-29) |
A | SCOP2B Superfamily | Protein kinase-like (PK-like) | 8033424 | 3000066 | SCOP2B (2022-06-29) |
Protein Family Annotation Pfam Database Homepage
Chains | Accession | Name | Description | Comments | Source | |
---|---|---|---|---|---|---|
PF00017 | SH2 domain (SH2) | SH2 domain | Domain | |||
PF00018 | SH3 domain (SH3_1) | SH3 domain | SH3 (Src homology 3) domains are often indicative of a protein involved in signal transduction related to cytoskeletal organisation. First described in the Src cytoplasmic tyrosine kinase Swiss:P12931. The structure is a partly opened beta barrel. | Domain | ||
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 triphospha ... | 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 |
---|---|---|---|
IPR020635 | Tyrosine-protein kinase, catalytic domain | Domain | |
IPR000719 | Protein kinase domain | Domain | |
IPR017441 | Protein kinase, ATP binding site | Binding Site | |
IPR036860 | SH2 domain superfamily | Homologous Superfamily | |
IPR001245 | Serine-threonine/tyrosine-protein kinase, catalytic domain | Domain | |
IPR008266 | Tyrosine-protein kinase, active site | Active Site | |
IPR036028 | SH3-like domain superfamily | Homologous Superfamily | |
IPR001452 | SH3 domain | Domain | |
IPR000980 | SH2 domain | Domain | |
IPR011009 | Protein kinase-like domain superfamily | Homologous Superfamily | |
IPR050198 | Non-receptor tyrosine kinases involved in cell signaling | Family |