Crystal structure of FGF2-M2 mutant - D28E/C78I/C96I/S137P. Determined by X-ray diffraction at 1.48 Å resolution. Released 26 Jun 2024.
Explore 8HUE in 3D Show helices and sheets RCSB PDB PDBe
8HUE contains 19 α-helices and 42 β-strands across 3 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 |
|---|---|---|---|
| α-helix | 23-26 | 4 | |
| β-strand | 30-34 | 5 | 1 |
| β-strand | 39-43 | 5 | 1 |
| β-strand | 49-52 | 4 | 1 |
| α-helix | 58-60 | 3 | |
| β-strand | 62-68 | 7 | 1 |
| β-strand | 71-76 | 6 | 1 |
| β-strand | 81-85 | 5 | 1 |
| β-strand | 91-94 | 4 | 1 |
| α-helix | 99-101 | 3 | |
| β-strand | 103-107 | 5 | 1 |
| β-strand | 113-117 | 5 | 1 |
| β-strand | 124 | 1 | 1 |
| β-strand | 127 | 1 | 2 |
| β-strand | 132 | 1 | 1 |
| β-strand | 133 | 1 | 2 |
| α-helix | 134-135 | 2 | |
| α-helix | 136-138 | 3 | |
| α-helix | 144-146 | 3 | |
| β-strand | 148-152 | 5 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 30-34 | 5 | 3 |
| α-helix | 39 | 1 | |
| β-strand | 40-43 | 4 | 3 |
| β-strand | 49-52 | 4 | 3 |
| α-helix | 58-60 | 3 | |
| β-strand | 62-68 | 7 | 3 |
| β-strand | 71-76 | 6 | 3 |
| β-strand | 81-85 | 5 | 3 |
| β-strand | 91-94 | 4 | 3 |
| α-helix | 99-101 | 3 | |
| β-strand | 103-107 | 5 | 3 |
| β-strand | 113-117 | 5 | 3 |
| β-strand | 124 | 1 | 3 |
| β-strand | 127 | 1 | 4 |
| β-strand | 132 | 1 | 3 |
| β-strand | 133 | 1 | 4 |
| α-helix | 134-135 | 2 | |
| α-helix | 136-138 | 3 | |
| α-helix | 144-146 | 3 | |
| β-strand | 148-152 | 5 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 30-34 | 5 | 5 |
| α-helix | 39 | 1 | |
| β-strand | 40-43 | 4 | 5 |
| β-strand | 48-52 | 5 | 5 |
| α-helix | 58-60 | 3 | |
| β-strand | 62-68 | 7 | 5 |
| β-strand | 71-76 | 6 | 5 |
| β-strand | 81-85 | 5 | 5 |
| β-strand | 91-94 | 4 | 5 |
| α-helix | 99-101 | 3 | |
| β-strand | 103-107 | 5 | 5 |
| α-helix | 109-111 | 3 | |
| β-strand | 113-117 | 5 | 5 |
| β-strand | 124 | 1 | 5 |
| β-strand | 127 | 1 | 6 |
| β-strand | 132 | 1 | 5 |
| β-strand | 133 | 1 | 6 |
| α-helix | 134-135 | 2 | |
| α-helix | 136-138 | 3 | |
| α-helix | 144-146 | 3 | |
| β-strand | 148-152 | 5 | 5 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Fibroblast growth factor 2 | A, B, C | protein | 147 | Homo sapiens | P09038 (AlphaFold model) |
>8HUE_1 Fibroblast growth factor 2 (chains A, B, C) MPALPEDGGSGAFPPGHFKEPKRLYCKNGGFFLRIHPDGRVDGVREKSDPHIKLQLQAEE RGVVSIKGVIANRYLAMKEDGRLLASKIVTDECFFFERLESNNYNTYRSRKYTSWYVALK RTGQYKLGPKTGPGQKAILFLPMSAKS
Structural and biochemical investigation into stable FGF2 mutants with novel mutation sites and hydrophobic replacements for surface-exposed cysteines. An, Y.J., Jung, Y.E., Lee, K.W. et al. PLoS One (2024) 19:e0307499-e0307499. DOI 10.1371/journal.pone.0307499 · PubMed
Other PDB entries of the same protein (UniProt P09038 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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