Crystal structure of K12V/C16S/C117V/P134V mutant of human acidic fibroblast growth factor. Determined by X-ray diffraction at 1.55 Å resolution. Released 11 Mar 2015.
Explore 4Q9G in 3D Show helices and sheets RCSB PDB PDBe
4Q9G contains 15 α-helices and 26 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 |
|---|---|---|---|
| α-helix | 4-6 | 3 | |
| β-strand | 12-16 | 5 | 1 |
| α-helix | 21 | 1 | |
| β-strand | 22-25 | 4 | 1 |
| β-strand | 31-34 | 4 | 1 |
| α-helix | 40-42 | 3 | |
| 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 |
| α-helix | 116 | 1 | |
| β-strand | 117 | 1 | 2 |
| α-helix | 118-119 | 2 | |
| α-helix | 120-122 | 3 | |
| α-helix | 128-130 | 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 | 117 | 1 | 4 |
| 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) |
>4Q9G_1 Fibroblast growth factor 1 (chains A, B) HHHHHHFNLPPGNYKKPVLLYSSNGGHFLRILPDGTVDGTRDRSDQHIQLQLSAESVGEV YIKSTETGQYLAMDTDGLLYGSQTPNEECLFLERLEENHYNTYISKKHAEKNWFVGLKKN GSVKRGPRTHYGQKAILFLVLPVSSD
| ID | Name | Formula | Copies |
|---|---|---|---|
| PO4 | Phosphate ion | O4 P | 1 |
Water and common crystallization additives (FMT) are not listed.
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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