Structure of rFnBPA(189-505) in complex with fibrinogen gamma chain C- terminal peptide. Determined by X-ray diffraction at 1.83 Å resolution. Released 9 Oct 2013.
Explore 4B60 in 3D Show helices and sheets RCSB PDB PDBe
4B60 contains 15 α-helices and 56 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 | 196 | 1 | 1 |
| α-helix | 198-200 | 3 | |
| β-strand | 201-209 | 9 | 2 |
| α-helix | 211-213 | 3 | |
| β-strand | 216-217 | 2 | 1 |
| β-strand | 221 | 1 | 3 |
| β-strand | 225-233 | 9 | 2 |
| β-strand | 242-247 | 6 | 1 |
| β-strand | 251-252 | 2 | 4 |
| β-strand | 255 | 1 | 3 |
| β-strand | 257 | 1 | 5 |
| α-helix | 263-264 | 2 | |
| β-strand | 265-267 | 3 | 1 |
| β-strand | 270-277 | 8 | 1 |
| β-strand | 282-287 | 6 | 1 |
| α-helix | 289-291 | 3 | |
| β-strand | 298-305 | 8 | 2 |
| β-strand | 306-307 | 2 | 4 |
| β-strand | 316-324 | 9 | 1 |
| β-strand | 327-335 | 9 | 1 |
| β-strand | 341-342 | 2 | 5 |
| β-strand | 346-356 | 11 | 5 |
| β-strand | 361-370 | 10 | 5 |
| β-strand | 375-386 | 12 | 3 |
| α-helix | 393-395 | 3 | |
| β-strand | 396-402 | 7 | 5 |
| α-helix | 406-408 | 3 | |
| β-strand | 423-425 | 3 | 5 |
| α-helix | 427-429 | 3 | |
| β-strand | 434-436 | 3 | 3 |
| β-strand | 442-448 | 7 | 3 |
| β-strand | 453-460 | 8 | 5 |
| β-strand | 469-478 | 10 | 3 |
| β-strand | 490-501 | 12 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 196 | 1 | 6 |
| α-helix | 198-200 | 3 | |
| β-strand | 201-209 | 9 | 7 |
| α-helix | 211-213 | 3 | |
| β-strand | 216-217 | 2 | 6 |
| β-strand | 221 | 1 | 8 |
| β-strand | 225-233 | 9 | 7 |
| β-strand | 242-247 | 6 | 6 |
| β-strand | 251-252 | 2 | 9 |
| β-strand | 255 | 1 | 8 |
| β-strand | 257 | 1 | 10 |
| α-helix | 263-264 | 2 | |
| β-strand | 265-267 | 3 | 6 |
| β-strand | 270-277 | 8 | 6 |
| α-helix | 279-281 | 3 | |
| β-strand | 282-287 | 6 | 6 |
| α-helix | 289-291 | 3 | |
| β-strand | 298-305 | 8 | 7 |
| β-strand | 306-307 | 2 | 9 |
| β-strand | 316-324 | 9 | 6 |
| β-strand | 327-335 | 9 | 6 |
| β-strand | 341-342 | 2 | 10 |
| β-strand | 346-356 | 11 | 10 |
| β-strand | 361-370 | 10 | 10 |
| β-strand | 378-386 | 9 | 8 |
| α-helix | 393-395 | 3 | |
| β-strand | 396-402 | 7 | 10 |
| α-helix | 406-408 | 3 | |
| β-strand | 423-425 | 3 | 10 |
| α-helix | 427-429 | 3 | |
| β-strand | 434-436 | 3 | 8 |
| β-strand | 442-446 | 5 | 8 |
| β-strand | 453-460 | 8 | 10 |
| β-strand | 469-475 | 7 | 8 |
| β-strand | 491-500 | 10 | 8 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 6-16 | 11 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 7-15 | 9 | 8 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Fibronectin-binding protein A | A, B | protein | 321 | STAPHYLOCOCCUS AUREUS SUBSP. AUREUS NCTC 8325 | P14738 (AlphaFold model) |
| Fibrinogen gamma chain | C, D | protein | 17 | HOMO SAPIENS | P02679 (AlphaFold model) |
>4B60_1 FIBRONECTIN-BINDING PROTEIN A (chains A, B) GPAMAKVETGTDVTSKVTVEIGSIEGHNNTNKVEPHAGQRAVLKYKLKFENGLHQGDYFD FTLSNNVNTHGVSTARKVPEIKNGSVVMATGEVLEGGKIRYTFTNDIEDKVDVTAELEIN LFIDPKTVQTNGNQTITSTLNEEQTSKELDVKYKDGIGNYYANLNGSIETFNKANNRFSH VAFIKPNNGKTTSVTVTGTLMKGSNQNGNQPKVRIFEYLGNNEDIAKSVYANTTDTSKFK EVTSNMSGNLNLQNNGSYSLNIENLDKTYVVHYDGEYLNGTDEVDFRTQMVGHPEQLYKY YYDRGYTLTWDNGLVLYSNKA
>4B60_2 FIBRINOGEN GAMMA CHAIN (chains C, D) GEGQQHHLGGAKQAGDV
| ID | Name | Formula | Copies |
|---|---|---|---|
| CA | Calcium ion | Ca | 1 |
Evidence for Steric Regulation of Fibrinogen Binding to Staphylococcus Aureus Fibronectin-Binding Protein a (Fnbpa). Stemberk, V., Jones, R.P., Moroz, O. et al. J Biol Chem (2014) 289:12842. DOI 10.1074/JBC.M113.543546 · PubMed
Other PDB entries of the same protein (UniProt P14738 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 4B60 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.