Bovine Fibrinogen alpha-C Domain. Determined by solution NMR. Released 28 Feb 2006.
Explore 2BAF in 3D Show helices and sheets RCSB PDB PDBe
2BAF contains 0 α-helices and 5 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 | 48-49 | 2 | 1 |
| β-strand | 53-55 | 3 | 1 |
| β-strand | 58-59 | 2 | 2 |
| β-strand | 67-68 | 2 | 2 |
| β-strand | 71-73 | 3 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Fibrinogen alpha chain | A | protein | 166 | Bos taurus | P02672 (AlphaFold model) |
>2BAF_1 Fibrinogen alpha chain (chains A) MGTFREEGSVSSGTKQEFHTGKLVTTKGDKELLIDNEKVTSGHTTTTRRSCSKVITKTVT NADGRTETTKEVVKSEDGSDCGDADFDWHHTFPSRGNLDDFFHRDKDDFFTRSSHEFDGR TGLAPEFAALGESGSSSSKTSTHSKQFVSSSTTVNRGGSAIESKHF
Identification of an Ordered Compact Structure within the Recombinant Bovine Fibrinogen alphaC-Domain Fragment by NMR. Burton, R.A., Tsurupa, G., Medved, L. et al. Biochemistry (2006) 45:2257-2266. DOI 10.1021/bi052380c · PubMed
Other PDB entries of the same protein (UniProt P02672 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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