Crystal structure of C117A mutant of human acidic fibroblast growth factor. Determined by X-ray diffraction at 1.5 Å resolution. Released 11 Mar 2015.
Explore 4QAL in 3D Show helices and sheets RCSB PDB PDBe
4QAL contains 9 α-helices and 28 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 | 44-48 | 5 | 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 |
| β-strand | 116 | 1 | 1 |
| β-strand | 117 | 1 | 2 |
| α-helix | 118-119 | 2 | |
| α-helix | 120-122 | 3 | |
| β-strand | 132-135 | 4 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 12-16 | 5 | 3 |
| β-strand | 21-25 | 5 | 3 |
| β-strand | 31-34 | 4 | 3 |
| β-strand | 44-48 | 5 | 3 |
| β-strand | 53-58 | 6 | 3 |
| 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 | 118-119 | 2 | |
| α-helix | 120-122 | 3 | |
| β-strand | 132-136 | 5 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Fibroblast growth factor 1 | A, B | protein | 146 | Homo sapiens | P05230 (AlphaFold model) |
>4QAL_1 Fibroblast growth factor 1 (chains A, B) HHHHHHFNLPPGNYKKPKLLYCSNGGHFLRILPDGTVDGTRDRSDQHIQLQLSAESVGEV YIKSTETGQYLAMDTDGLLYGSQTPNEECLFLERLEENHYNTYISKKHAEKNWFVGLKKN GSAKRGPRTHYGQKAILFLPLPVSSD
| ID | Name | Formula | Copies |
|---|---|---|---|
| FLC | Citrate anion | C6 H5 O7 | 2 |
Mutation choice to eliminate buried free cysteines in protein therapeutics. Xia, X., Longo, L.M., Blaber, M. J Pharm Sci (2015) 104:566-576. DOI 10.1002/jps.24188 · 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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