Crystal structure of human tyrosine-protein kinase C-src, in complex with AMP-pnp. Determined by X-ray diffraction at 1.5 Å resolution. Released 22 Jul 1999.
Explore 2SRC in 3D Show helices and sheets RCSB PDB PDBe
2SRC contains 26 α-helices and 26 β-strands across 1 chain. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 86-88 | 3 | 1 |
| β-strand | 92 | 1 | 2 |
| β-strand | 99 | 1 | 1 |
| β-strand | 102 | 1 | 2 |
| β-strand | 107-112 | 6 | 1 |
| β-strand | 118-123 | 6 | 1 |
| β-strand | 129-133 | 5 | 1 |
| α-helix | 134-136 | 3 | |
| β-strand | 137-139 | 3 | 1 |
| β-strand | 149 | 1 | 3 |
| α-helix | 155-162 | 8 | |
| α-helix | 167-168 | 2 | |
| β-strand | 171-176 | 6 | 3 |
| β-strand | 184-192 | 9 | 3 |
| β-strand | 196-204 | 9 | 3 |
| β-strand | 205-206 | 2 | 4 |
| β-strand | 212-213 | 2 | 4 |
| β-strand | 219-220 | 2 | 4 |
| α-helix | 223-229 | 7 | |
| β-strand | 243-244 | 2 | 3 |
| α-helix | 245-246 | 2 | |
| α-helix | 248-252 | 5 | |
| β-strand | 261 | 1 | 5 |
| α-helix | 264-266 | 3 | |
| β-strand | 267-275 | 9 | 5 |
| β-strand | 279-286 | 8 | 5 |
| β-strand | 290-297 | 8 | 5 |
| α-helix | 304-315 | 12 | |
| β-strand | 322 | 1 | 6 |
| α-helix | 323-324 | 2 | |
| β-strand | 325-329 | 5 | 5 |
| α-helix | 334 | 1 | |
| β-strand | 335-338 | 4 | 5 |
| β-strand | 345 | 1 | 6 |
| α-helix | 346-350 | 5 | |
| α-helix | 360-379 | 20 | |
| α-helix | 389-391 | 3 | |
| β-strand | 392-395 | 4 | 6 |
| α-helix | 396-398 | 3 | |
| β-strand | 399-402 | 4 | 6 |
| α-helix | 407-410 | 4 | |
| α-helix | 414-417 | 4 | |
| α-helix | 426-428 | 3 | |
| α-helix | 431-436 | 6 | |
| α-helix | 441-455 | 15 | |
| α-helix | 460-461 | 2 | |
| α-helix | 468-476 | 9 | |
| α-helix | 481-484 | 4 | |
| α-helix | 489-498 | 10 | |
| α-helix | 503-505 | 3 | |
| α-helix | 507-508 | 2 | |
| α-helix | 509-517 | 9 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Tyrosine-protein kinase src | A | protein | 452 | Homo sapiens | P12931 (AlphaFold model) |
>2SRC_1 TYROSINE-PROTEIN KINASE SRC (chains A) MVTTFVALYDYESRTETDLSFKKGERLQIVNNTEGDWWLAHSLSTGQTGYIPSNYVAPSD SIQAEEWYFGKITRRESERLLLNAENPRGTFLVRESETTKGAYCLSVSDFDNAKGLNVKH YKIRKLDSGGFYITSRTQFNSLQQLVAYYSKHADGLCHRLTTVCPTSKPQTQGLAKDAWE IPRESLRLEVKLGQGCFGEVWMGTWNGTTRVAIKTLKPGTMSPEAFLQEAQVMKKLRHEK LVQLYAVVSEEPIYIVTEYMSKGSLLDFLKGETGKYLRLPQLVDMAAQIASGMAYVERMN YVHRDLRAANILVGENLVCKVADFGLARLIEDNEYTARQGAKFPIKWTAPEAALYGRFTI KSDVWSFGILLTELTTKGRVPYPGMVNREVLDQVERGYRMPCPPECPESLHDLMCQCWRK EPEERPTFEYLQAFLEDYFTSTEPQYQPGENL
| ID | Name | Formula | Copies |
|---|---|---|---|
| ANP | Phosphoaminophosphonic acid-adenylate ester | C10 H17 N6 O12 P3 | 1 |
Crystal structures of c-Src reveal features of its autoinhibitory mechanism. Xu, W., Doshi, A., Lei, M. et al. Mol Cell (1999) 3:629-638. DOI 10.1016/S1097-2765(00)80356-1 · PubMed
Other PDB entries of the same protein (UniProt P12931 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 2SRC directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.