Structural and Biochemical Characterization of Fibrinogen binding to ClfA from Staphylocccus aureus. Determined by X-ray diffraction at 1.95 Å resolution. Released 19 May 2009.
Explore 2VR3 in 3D Show helices and sheets RCSB PDB PDBe
2VR3 contains 15 α-helices and 62 β-strands across 4 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 | 231 | 1 | 1 |
| α-helix | 233-235 | 3 | |
| β-strand | 237-244 | 8 | 1 |
| β-strand | 248-249 | 2 | 1 |
| β-strand | 253 | 1 | 2 |
| β-strand | 257-265 | 9 | 1 |
| α-helix | 266 | 1 | |
| β-strand | 274-278 | 5 | 1 |
| β-strand | 283-284 | 2 | 3 |
| β-strand | 287 | 1 | 2 |
| β-strand | 289 | 1 | 4 |
| α-helix | 294-296 | 3 | |
| β-strand | 297-298 | 2 | 1 |
| β-strand | 305-309 | 5 | 1 |
| β-strand | 315-319 | 5 | 1 |
| α-helix | 322-325 | 4 | |
| β-strand | 326-337 | 12 | 1 |
| β-strand | 338-339 | 2 | 3 |
| β-strand | 348-356 | 9 | 1 |
| β-strand | 359-367 | 9 | 1 |
| β-strand | 373-375 | 3 | 5 |
| β-strand | 378-388 | 11 | 5 |
| β-strand | 393-400 | 8 | 5 |
| β-strand | 407-416 | 10 | 2 |
| α-helix | 417 | 1 | |
| β-strand | 424-425 | 2 | 5 |
| β-strand | 432-437 | 6 | 5 |
| α-helix | 441-443 | 3 | |
| β-strand | 457 | 1 | 5 |
| α-helix | 459-461 | 3 | |
| β-strand | 463-468 | 6 | 2 |
| β-strand | 471-475 | 5 | 2 |
| β-strand | 482-483 | 2 | 2 |
| β-strand | 487-495 | 9 | 5 |
| β-strand | 505-512 | 8 | 2 |
| β-strand | 518-530 | 13 | 2 |
| β-strand | 533-540 | 8 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 231 | 1 | 6 |
| α-helix | 233-235 | 3 | |
| β-strand | 237-244 | 8 | 6 |
| β-strand | 248-249 | 2 | 6 |
| β-strand | 253 | 1 | 7 |
| β-strand | 257-265 | 9 | 6 |
| α-helix | 266 | 1 | |
| β-strand | 274-278 | 5 | 6 |
| β-strand | 283-284 | 2 | 8 |
| β-strand | 287 | 1 | 7 |
| β-strand | 289 | 1 | 9 |
| α-helix | 293-296 | 4 | |
| β-strand | 297-299 | 3 | 6 |
| β-strand | 302-309 | 8 | 6 |
| β-strand | 315-319 | 5 | 6 |
| α-helix | 321-324 | 4 | |
| β-strand | 326-337 | 12 | 6 |
| β-strand | 338-339 | 2 | 8 |
| β-strand | 348-356 | 9 | 6 |
| β-strand | 359-367 | 9 | 6 |
| β-strand | 373-375 | 3 | 9 |
| β-strand | 378-388 | 11 | 9 |
| β-strand | 393-400 | 8 | 9 |
| β-strand | 407-416 | 10 | 7 |
| α-helix | 417 | 1 | |
| β-strand | 424-425 | 2 | 9 |
| β-strand | 432-437 | 6 | 9 |
| α-helix | 441-443 | 3 | |
| α-helix | 452-454 | 3 | |
| β-strand | 456-457 | 2 | 9 |
| α-helix | 459-461 | 3 | |
| β-strand | 463-468 | 6 | 7 |
| β-strand | 471-475 | 5 | 7 |
| β-strand | 482-483 | 2 | 7 |
| β-strand | 487-495 | 9 | 9 |
| β-strand | 504-512 | 9 | 7 |
| β-strand | 518-530 | 13 | 7 |
| β-strand | 533-540 | 8 | 6 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 401-410 | 10 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 400-410 | 11 | 7 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Clumping factor A | A, B | protein | 329 | STAPHYLOCOCCUS AUREUS | Q2G015 (AlphaFold model) |
| Fibrinogen gamma-chain | C, D | protein | 13 | HOMO SAPIENS | P02679 (AlphaFold model) |
>2VR3_1 CLUMPING FACTOR A (chains A, B) MRGSHHHHHHGSGTDITNQLTNVTVGIDSGTTVYPHQAGYVKLNYGFSVPNSAVKGDTFK ITVPKELNLNGVTSTAKVPPIMAGDQVLANGVIDSDGNVIYTFTDYVNTKCDVKATLTMP AYIDPENVKKTGNVTLATGIGSTTANKTVLVDYEKYGKFYNLSIKGTIDQIDKTNNTYRQ TIYVNPSGDNVIAPVLTGNLKPNTDSNALIDQQNTSIKVYKVDNAADLSESYFVNPENFE DVTNSVNITFPNPNQYKVEFNTPDDQITTPYIVVVNGHIDPNSKGDLALRSTLYGYNSNI IWRSMSWDNEVAFNNGSGSGDGIDCPVVP
>2VR3_2 FIBRINOGEN GAMMA-CHAIN (chains C, D) QHHLGGAKQAGAV
A Structural Model of the Staphylococcus Aureus Clfa-Fibrinogen Interaction Opens New Avenues for the Design of Anti-Staphylococcal Therapeutics. Ganesh, V.K., Rivera, J.J., Smeds, E. et al. PLoS Pathog (2008) 4:226. DOI 10.1371/JOURNAL.PPAT.1000226 · PubMed
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