Human Acidic Fibroblast Growth Factor. 141 Amino Acid Form with Amino Terminal His Tag AND LEU 44 REPLACED BY PHE AND LEU 73 REPLACED BY VAL AND VAL 109 REPLACED BY LEU (L44F/L73V/V109L). Determined by X-ray diffraction at 1.7 Å resolution. Released 19 Dec 2001.
Explore 1JT7 in 3D Show helices and sheets RCSB PDB PDBe
1JT7 contains 26 α-helices and 55 β-strands across 4 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 |
| β-strand | 21-25 | 5 | 1 |
| β-strand | 31-34 | 4 | 1 |
| β-strand | 43-50 | 8 | 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 | 2-5 | 4 | |
| 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 |
| 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 | 118-119 | 2 | |
| α-helix | 120-122 | 3 | |
| α-helix | 128-130 | 3 | |
| β-strand | 132-136 | 5 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 4-6 | 3 | |
| β-strand | 12-16 | 5 | 5 |
| β-strand | 21-25 | 5 | 5 |
| β-strand | 31-34 | 4 | 5 |
| β-strand | 44-50 | 7 | 5 |
| β-strand | 53-58 | 6 | 5 |
| α-helix | 63 | 1 | |
| β-strand | 64-67 | 4 | 5 |
| β-strand | 73-76 | 4 | 5 |
| α-helix | 81-83 | 3 | |
| β-strand | 85-90 | 6 | 5 |
| β-strand | 94-99 | 6 | 5 |
| α-helix | 103-105 | 3 | |
| β-strand | 108 | 1 | 5 |
| β-strand | 111 | 1 | 6 |
| β-strand | 116 | 1 | 5 |
| β-strand | 117 | 1 | 6 |
| α-helix | 118-119 | 2 | |
| α-helix | 120-122 | 3 | |
| β-strand | 132-136 | 5 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 2-5 | 4 | |
| β-strand | 12-16 | 5 | 7 |
| β-strand | 21-25 | 5 | 7 |
| β-strand | 31-34 | 4 | 7 |
| β-strand | 44-48 | 5 | 7 |
| β-strand | 53-58 | 6 | 7 |
| β-strand | 64-67 | 4 | 7 |
| β-strand | 73-76 | 4 | 7 |
| α-helix | 81-83 | 3 | |
| β-strand | 85-90 | 6 | 7 |
| β-strand | 94-99 | 6 | 7 |
| α-helix | 103-105 | 3 | |
| β-strand | 108 | 1 | 7 |
| β-strand | 111 | 1 | 8 |
| β-strand | 116 | 1 | 7 |
| β-strand | 117 | 1 | 8 |
| α-helix | 118-119 | 2 | |
| α-helix | 120-122 | 3 | |
| α-helix | 128-130 | 3 | |
| β-strand | 132-136 | 5 | 7 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| acidic fibroblast growth factor | A, B, C, D | protein | 146 | Homo sapiens | P05230 (AlphaFold model) |
>1JT7_1 acidic fibroblast growth factor (chains A, B, C, D) HHHHHHFNLPPGNYKKPKLLYCSNGGHFLRILPDGTVDGTRDRSDQHIQFQLSAESVGEV YIKSTETGQYLAMDTDGLVYGSQTPNEECLFLERLEENHYNTYISKKHAEKNWFLGLKKN 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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