Structural and biochemical characterization of ClfB:ligand interactions. Determined by X-ray diffraction at 2.6 Å resolution. Released 4 May 2011.
Explore 3ASW in 3D Show helices and sheets RCSB PDB PDBe
3ASW contains 7 α-helices and 35 β-strands across 2 chains. 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 | 214 | 1 | 1 |
| α-helix | 216-218 | 3 | |
| β-strand | 219-226 | 8 | 1 |
| β-strand | 230-231 | 2 | 2 |
| β-strand | 235 | 1 | 3 |
| β-strand | 239-247 | 9 | 1 |
| β-strand | 256-260 | 5 | 1 |
| β-strand | 265-266 | 2 | 4 |
| β-strand | 269 | 1 | 5 |
| β-strand | 271 | 1 | 6 |
| α-helix | 274-276 | 3 | |
| β-strand | 279-287 | 9 | 1 |
| β-strand | 292-299 | 8 | 1 |
| β-strand | 304-309 | 6 | 1 |
| α-helix | 311-315 | 5 | |
| β-strand | 320-327 | 8 | 1 |
| β-strand | 328-329 | 2 | 4 |
| β-strand | 338-341 | 4 | 2 |
| β-strand | 344-346 | 3 | 1 |
| β-strand | 350-351 | 2 | 1 |
| β-strand | 354-357 | 4 | 2 |
| α-helix | 359-361 | 3 | |
| β-strand | 365 | 1 | 7 |
| β-strand | 373 | 1 | 7 |
| β-strand | 374-381 | 8 | 6 |
| β-strand | 389-396 | 8 | 6 |
| β-strand | 403-411 | 9 | 8 |
| α-helix | 417-419 | 3 | |
| β-strand | 422-423 | 2 | 6 |
| β-strand | 430-436 | 7 | 6 |
| α-helix | 439-441 | 3 | |
| β-strand | 455-457 | 3 | 6 |
| α-helix | 459-462 | 4 | |
| β-strand | 466-470 | 5 | 8 |
| β-strand | 473-481 | 9 | 8 |
| β-strand | 485-493 | 9 | 6 |
| β-strand | 501-509 | 9 | 8 |
| β-strand | 518-525 | 8 | 8 |
| β-strand | 526-528 | 3 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 479-481 | 3 | 8 |
| β-strand | 483 | 1 | 3 |
| β-strand | 484-486 | 3 | 5 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Clumping factor B | A | protein | 328 | Staphylococcus aureus | Q7A382 (AlphaFold model) |
| Tail region derived peptide | B | protein | 15 | Homo sapiens | P13645 (AlphaFold model) |
>3ASW_1 Clumping factor B (chains A) HHHHHHGSGTNVNDKVTASNFKLEKTTFDPNQSGNTFMAANFTVTDKVKSGDYFTAKLPD SLTGNGDVDYSNSNNTMPIADIKSTNGDVVAKATYDILTKTYTFVFTDYVNNKENINGQF SLPLFTDRAKAPKSGTYDANINIADEMFNNKITYNYSSPIAGIDKPNGANISSQIIGVDT ASGQNTYKQTVFVNPKQRVLGNTWVYIKGYQDKIEESSGKVSATDTKLRIFEVNDTSKLS ESYYADPNDSNLKEVTDQFKNRIYYEHPNVASIKFGDITKTYVVLVEGHYDNTGKNLKTQ VIQENVDPVTNRDYSIFGWNNENVVRYG
>3ASW_2 Tail region derived peptide (chains B) YGGGSSGGGSSGGGH
Structural and biochemical characterization of ClfB:ligand interactions. Ganesh, V.K., Barbu, E.M., Deivanayagam, C.C.S. et al. To be published.
Other PDB entries of the same protein (UniProt Q7A382 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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