Crystal structure of K112N mutant of Human acidic fibroblast growth factor. Determined by X-ray diffraction at 1.65 Å resolution. Released 15 Apr 2008.
Explore 3BAH in 3D Show helices and sheets RCSB PDB PDBe
3BAH contains 11 α-helices and 27 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 | 12-16 | 5 | 1 |
| β-strand | 21-25 | 5 | 1 |
| β-strand | 31-34 | 4 | 1 |
| β-strand | 44-50 | 7 | 1 |
| β-strand | 53-58 | 6 | 1 |
| α-helix | 63 | 1 | |
| β-strand | 64-67 | 4 | 1 |
| β-strand | 73-76 | 4 | 1 |
| α-helix | 81-83 | 3 | |
| β-strand | 85-90 | 6 | 1 |
| β-strand | 94-99 | 6 | 1 |
| α-helix | 103-105 | 3 | |
| β-strand | 108 | 1 | 1 |
| β-strand | 111 | 1 | 2 |
| α-helix | 116 | 1 | |
| β-strand | 117 | 1 | 2 |
| α-helix | 118-119 | 2 | |
| α-helix | 120-122 | 3 | |
| β-strand | 132-136 | 5 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 12-16 | 5 | 3 |
| α-helix | 21 | 1 | |
| β-strand | 22-25 | 4 | 3 |
| β-strand | 31-34 | 4 | 3 |
| β-strand | 44-48 | 5 | 3 |
| β-strand | 53-58 | 6 | 3 |
| α-helix | 63 | 1 | |
| β-strand | 64-67 | 4 | 3 |
| β-strand | 73-76 | 4 | 3 |
| α-helix | 81-83 | 3 | |
| β-strand | 85-90 | 6 | 3 |
| β-strand | 94-99 | 6 | 3 |
| α-helix | 103-105 | 3 | |
| β-strand | 108 | 1 | 3 |
| β-strand | 111 | 1 | 4 |
| β-strand | 116 | 1 | 3 |
| β-strand | 117 | 1 | 4 |
| α-helix | 120-122 | 3 | |
| β-strand | 132-136 | 5 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Heparin-binding growth factor 1 | A, B | protein | 146 | Homo sapiens | P05230 (AlphaFold model) |
>3BAH_1 Heparin-binding growth factor 1 (chains A, B) HHHHHHFNLPPGNYKKPKLLYCSNGGHFLRILPDGTVDGTRDRSDQHIQLQLSAESVGEV YIKSTETGQYLAMDTDGLLYGSQTPNEECLFLERLEENHYNTYISKKHAEKNWFVGLNKN GSCKRGPRTHYGQKAILFLPLPVSSD
A logical OR redundancy within the Asx-Pro-Asx-Gly type I beta-turn motif. Lee, J., Dubey, V.K., Longo, L.M. et al. J Mol Biol (2008) 377:1251-1264. DOI 10.1016/j.jmb.2008.01.055 · PubMed
Other PDB entries of the same protein (UniProt P05230 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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