Crystal structures of Bbp from Staphylococcus aureus with peptide ligand. Determined by X-ray diffraction at 1.45 Å resolution. Released 23 Sept 2015.
Explore 5CFA in 3D Show helices and sheets RCSB PDB PDBe
5CFA contains 13 α-helices and 58 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 | 4 | 1 | 1 |
| α-helix | 6-8 | 3 | |
| β-strand | 9-18 | 10 | 1 |
| β-strand | 25-27 | 3 | 1 |
| α-helix | 28-30 | 3 | |
| β-strand | 34-42 | 9 | 1 |
| β-strand | 51-55 | 5 | 1 |
| β-strand | 60-61 | 2 | 2 |
| α-helix | 71-73 | 3 | |
| β-strand | 74-75 | 2 | 1 |
| β-strand | 81-88 | 8 | 1 |
| β-strand | 93-98 | 6 | 1 |
| α-helix | 101-104 | 4 | |
| β-strand | 105-116 | 12 | 1 |
| β-strand | 117-118 | 2 | 2 |
| β-strand | 127-135 | 9 | 1 |
| β-strand | 138-147 | 10 | 1 |
| β-strand | 152-154 | 3 | 3 |
| β-strand | 157-167 | 11 | 3 |
| β-strand | 172-179 | 8 | 3 |
| β-strand | 186-195 | 10 | 4 |
| β-strand | 197-198 | 2 | 5 |
| β-strand | 204-205 | 2 | 5 |
| β-strand | 212 | 1 | 3 |
| β-strand | 218-223 | 6 | 3 |
| β-strand | 243-244 | 2 | 3 |
| α-helix | 246-248 | 3 | |
| β-strand | 250-256 | 7 | 4 |
| β-strand | 259-267 | 9 | 4 |
| β-strand | 271-278 | 8 | 3 |
| α-helix | 283-286 | 4 | |
| β-strand | 291-298 | 8 | 4 |
| β-strand | 304-316 | 13 | 4 |
| β-strand | 319-326 | 8 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 4 | 1 | 6 |
| α-helix | 6-8 | 3 | |
| β-strand | 9-18 | 10 | 6 |
| β-strand | 25-27 | 3 | 6 |
| α-helix | 28-30 | 3 | |
| β-strand | 34-42 | 9 | 6 |
| β-strand | 51-55 | 5 | 6 |
| β-strand | 60-61 | 2 | 7 |
| α-helix | 71-73 | 3 | |
| β-strand | 74-75 | 2 | 6 |
| β-strand | 81-88 | 8 | 6 |
| β-strand | 93-98 | 6 | 6 |
| α-helix | 101-104 | 4 | |
| β-strand | 105-116 | 12 | 6 |
| β-strand | 117-118 | 2 | 7 |
| β-strand | 127-135 | 9 | 6 |
| β-strand | 138-147 | 10 | 6 |
| β-strand | 152-154 | 3 | 8 |
| β-strand | 157-167 | 11 | 8 |
| β-strand | 172-179 | 8 | 8 |
| β-strand | 186-195 | 10 | 9 |
| β-strand | 197-198 | 2 | 10 |
| β-strand | 204-205 | 2 | 10 |
| β-strand | 212 | 1 | 8 |
| β-strand | 218-223 | 6 | 8 |
| α-helix | 224-225 | 2 | |
| β-strand | 243-244 | 2 | 8 |
| α-helix | 246-248 | 3 | |
| β-strand | 250-256 | 7 | 9 |
| β-strand | 259-267 | 9 | 9 |
| β-strand | 271-278 | 8 | 8 |
| α-helix | 283-286 | 4 | |
| β-strand | 290-298 | 9 | 9 |
| β-strand | 304-316 | 13 | 9 |
| β-strand | 319-326 | 8 | 6 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 28-33 | 6 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Bone sialoprotein-binding protein | A, B | protein | 331 | Staphylococcus aureus | Q14U76 (AlphaFold model) |
| Peptide from Fibrinogen alpha chain | C, D | protein | 15 | Homo sapiens | P02671 (AlphaFold model) |
>5CFA_1 Bone sialoprotein-binding protein (chains A, B) GPLGSNNVNDLITVTKQMITEGIKDDGVIQAHDGEHIIYTSDFKIDNAVKAGDTMTVKYD KHTIPSDITDDFTPVDITDPSGEVIAKGTFDLNTKTITYKFTDYVDRYENVNAKLELNSY IDKKEVPNETNLNLTFATADKETSKNVKVEYQKPIVKDESNIQSIFSHLDTTKHEVEQTI YVNPLKLNAKNTNVTIKSGGVADNGDYYTGDGSTIIDSNTEIKVYKVASGQQLPQSNKIY DYSQYEDVTNSVTINKNYGTNMANINFGDIDSAYIVKVVSKYTPGAEDDLAVQQGVRMTT TNKYNYSSYAGYTNTILSTTDSGGGDGTVKP
>5CFA_2 Peptide from Fibrinogen alpha chain (chains C, D) SKQFTSSTSYNRGDS
| ID | Name | Formula | Copies |
|---|---|---|---|
| MG | Magnesium ion | Mg | 1 |
Crystal structures of Bbp from Staphylococcus aureus reveal the ligand binding mechanism with Fibrinogen alpha. Zhang, X.Y., Wu, M., Zhuo, W. et al. Protein Cell (2015) 6:757-766. DOI 10.1007/s13238-015-0205-x · PubMed
Other PDB entries of the same protein (UniProt Q14U76 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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