Solution structure of tgf-B1, NMR, models 1-17 of 33 structures. Determined by solution NMR. Released 17 Aug 1996.
Explore 1KLA in 3D Show helices and sheets RCSB PDB PDBe
1KLA contains 2 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 |
|---|---|---|---|
| β-strand | 3 | 1 | 1 |
| β-strand | 16-18 | 3 | 2 |
| β-strand | 22 | 1 | 3 |
| β-strand | 35 | 1 | 1 |
| β-strand | 39 | 1 | 3 |
| β-strand | 43-45 | 3 | 2 |
| α-helix | 57-68 | 12 | |
| β-strand | 80-92 | 13 | 1 |
| β-strand | 95-109 | 15 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Transforming growth factor-beta 1 | A, B | protein | 112 | Homo sapiens | P01137 (AlphaFold model) |
>1KLA_1 TRANSFORMING GROWTH FACTOR-BETA 1 (chains A, B) ALDTNYCFSSTEKNCCVRQLYIDFRKDLGWKWIHEPKGYHANFCLGPCPYIWSLDTQYSK VLALYNQHNPGASAAPCCVPQALEPLPIVYYVGRKPKVEQLSNMIVRSCKCS
Transforming growth factor beta 1: three-dimensional structure in solution and comparison with the X-ray structure of transforming growth factor beta 2. Hinck, A.P., Archer, S.J., Qian, S.W. et al. Biochemistry (1996) 35:8517-8534. DOI 10.1021/bi9604946 · PubMed
Other PDB entries of the same protein (UniProt P01137 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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