Fold of the cbfa. Determined by solution NMR. Released 7 Jun 2000.
Explore 1CO1 in 3D Show helices and sheets RCSB PDB PDBe
1CO1 contains 1 α-helix and 12 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 | 23-24 | 2 | 1 |
| β-strand | 30-33 | 4 | 1 |
| β-strand | 39 | 1 | 2 |
| β-strand | 49-53 | 5 | 1 |
| β-strand | 61-68 | 8 | 3 |
| β-strand | 75 | 1 | 3 |
| β-strand | 81-84 | 4 | 3 |
| β-strand | 88-91 | 4 | 1 |
| β-strand | 105-111 | 7 | 3 |
| β-strand | 119-121 | 3 | 3 |
| β-strand | 127 | 1 | 3 |
| α-helix | 128 | 1 | |
| β-strand | 129 | 1 | 2 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Core binding factor alpha | A | protein | 115 | Homo sapiens | Q01196 (AlphaFold model) |
>1CO1_1 CORE BINDING FACTOR ALPHA (chains A) ELVRTDSPNFLCSVLPTHWRCNKTLPIAFKVVALGDVPDGTLVTVMAGNDENYSAELRNA TAAMKNQVARFNDLRFVGRSGRGKSFTLTITVFTNPPQVATYHRAIKITVDGPRE
The Ig fold of the core binding factor alpha Runt domain is a member of a family of structurally and functionally related Ig-fold DNA-binding domains. Berardi, M.J., Sun, C., Zehr, M. et al. Structure (1999) 7:1247-1256. DOI 10.1016/S0969-2126(00)80058-1 · PubMed
Other PDB entries of the same protein (UniProt Q01196 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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