Structure of core-swapped mutant of fibronectin. Determined by X-ray diffraction at 2.0 Å resolution. Released 10 Apr 2007.
Explore 2CK2 in 3D Show helices and sheets RCSB PDB PDBe
2CK2 contains 6 α-helices and 16 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 |
|---|---|---|---|
| α-helix | 5 | 1 | |
| β-strand | 6-13 | 8 | 1 |
| β-strand | 18-23 | 6 | 1 |
| β-strand | 31-38 | 8 | 2 |
| β-strand | 46-51 | 6 | 2 |
| β-strand | 56-59 | 4 | 1 |
| α-helix | 62-63 | 2 | |
| β-strand | 67-76 | 10 | 2 |
| β-strand | 83-84 | 2 | 2 |
| α-helix | 85-87 | 3 | |
| β-strand | 88-93 | 6 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 6-13 | 8 | 2 |
| β-strand | 17-23 | 7 | 2 |
| β-strand | 31-38 | 8 | 1 |
| α-helix | 44-45 | 2 | |
| β-strand | 46-51 | 6 | 1 |
| β-strand | 56-60 | 5 | 2 |
| α-helix | 62-63 | 2 | |
| β-strand | 67-75 | 9 | 1 |
| β-strand | 84 | 1 | 1 |
| α-helix | 85-87 | 3 | |
| β-strand | 88-93 | 6 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Human fibronectin | A, B | protein | 96 | HOMO SAPIENS | P02751 (AlphaFold model) |
>2CK2_1 HUMAN FIBRONECTIN (chains A, B) VSDVPRDIEVVAVTPTSALISWDAPAVTIRYIRLTYGETGGNSPVQEITLPGSKSTYTIS GLKPGTDYTVTLYSVTGRGDSPASSKPASINFRTEI
| ID | Name | Formula | Copies |
|---|---|---|---|
| ACE | Acetyl group | C2 H4 O | 2 |
Designing an Extracellular Matrix Protein with Enhanced Mechanical Stability. Ng, S.P., Billings, K.S., Ohashi, T. et al. Proc Natl Acad Sci U S A (2007) 104:9633. DOI 10.1073/PNAS.0609901104 · PubMed
Other PDB entries of the same protein (UniProt P02751 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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