NMR Solution Structure, Stability, and Interaction of the Recombinant Bovine Fibrinogen alphaC-Domain Fragment. Determined by solution NMR. Released 7 Aug 2007.
Explore 2JOR in 3D Show helices and sheets RCSB PDB PDBe
2JOR contains 0 α-helices and 6 β-strands across 1 chain. 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 | 17 | 1 | 1 |
| β-strand | 21-29 | 9 | 2 |
| β-strand | 33-41 | 9 | 2 |
| β-strand | 42 | 1 | 1 |
| β-strand | 49 | 1 | 3 |
| β-strand | 52 | 1 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Fibrinogen alpha chain | A | protein | 79 | Bos taurus | P02672 (AlphaFold model) |
>2JOR_1 Fibrinogen alpha chain (chains A) MIDNEKVTSGHTTTTRRSCSKVITKTVTNADGRTETTKEVVKSEDGSDCGDADFDWHHTF PSRGNLDDFFHRDKDDFFT
NMR Solution Structure, Stability, and Interaction of the Recombinant Bovine Fibrinogen alphaC-Domain Fragment. Burton, R.A., Tsurupa, G., Hantgan, R.R. et al. Biochemistry (2007) 46:8550-8560. DOI 10.1021/bi700606v · PubMed
Other PDB entries of the same protein (UniProt P02672 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 2JOR 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.