Human Acidic Fibroblast Growth Factor. 141 Amino Acid Form with Amino Terminal His Tag. Determined by X-ray diffraction at 1.65 Å resolution. Released 19 Dec 2001.
Explore 1JQZ in 3D Show helices and sheets RCSB PDB PDBe
1JQZ contains 13 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 | 2-4 | 3 | |
| 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 |
| 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 |
|---|---|---|---|
| α-helix | 2-4 | 3 | |
| 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 |
| α-helix | 116 | 1 | |
| 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 |
|---|---|---|---|---|---|
| acidic fibroblast growth factor | A, B | protein | 146 | Homo sapiens | P05230 (AlphaFold model) |
>1JQZ_1 acidic fibroblast growth factor (chains A, B) HHHHHHFNLPPGNYKKPKLLYCSNGGHFLRILPDGTVDGTRDRSDQHIQLQLSAESVGEV YIKSTETGQYLAMDTDGLLYGSQTPNEECLFLERLEENHYNTYISKKHAEKNWFVGLKKN GSCKRGPRTHYGQKAILFLPLPVSSD
Structure and stability effects of mutations designed to increase the primary sequence symmetry within the core region of a beta-trefoil. Brych, S.R., Blaber, S.I., Logan, T.M. et al. Protein Sci (2001) 10:2587-2599. DOI 10.1110/ps.ps.34701 · 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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