Crystal structure of "L44F/M67I/L73V/A103G/deletion 104-106/F108Y/V109L/L111I/C117V/R119G/deletion 120-122" mutant form of Human acidic fibroblast growth factor. Determined by X-ray diffraction at 1.6 Å resolution. Released 23 Feb 2011.
Explore 3O3Q in 3D Show helices and sheets RCSB PDB PDBe
3O3Q contains 16 α-helices and 52 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 |
|---|---|---|---|
| β-strand | 12-16 | 5 | 1 |
| β-strand | 21-25 | 5 | 1 |
| β-strand | 30-34 | 5 | 1 |
| β-strand | 44-45 | 2 | 1 |
| β-strand | 48-50 | 3 | 1 |
| β-strand | 53-54 | 2 | 1 |
| β-strand | 57-58 | 2 | 1 |
| β-strand | 64-67 | 4 | 1 |
| β-strand | 72-76 | 5 | 1 |
| β-strand | 85-89 | 5 | 1 |
| β-strand | 95-99 | 5 | 1 |
| α-helix | 107 | 1 | |
| β-strand | 108-111 | 4 | 1 |
| β-strand | 116-123 | 5 | 1 |
| α-helix | 128-130 | 3 | |
| β-strand | 132-136 | 5 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 12-16 | 5 | 2 |
| β-strand | 21-25 | 5 | 2 |
| β-strand | 30-34 | 5 | 2 |
| β-strand | 43-45 | 3 | 2 |
| β-strand | 48-50 | 3 | 2 |
| β-strand | 53-54 | 2 | 2 |
| β-strand | 57-58 | 2 | 2 |
| β-strand | 64-67 | 4 | 2 |
| β-strand | 72-76 | 5 | 2 |
| β-strand | 85-89 | 5 | 2 |
| β-strand | 95-99 | 5 | 2 |
| α-helix | 107 | 1 | |
| β-strand | 108-111 | 4 | 2 |
| β-strand | 117-123 | 4 | 2 |
| α-helix | 128-130 | 3 | |
| β-strand | 132-136 | 5 | 2 |
| 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 | 43-48 | 6 | 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 | 85-89 | 5 | 3 |
| α-helix | 91-93 | 3 | |
| β-strand | 95-99 | 5 | 3 |
| α-helix | 107 | 1 | |
| β-strand | 108-111 | 4 | 3 |
| β-strand | 116-123 | 5 | 3 |
| α-helix | 128-130 | 3 | |
| β-strand | 132-136 | 5 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 12-16 | 5 | 4 |
| α-helix | 21 | 1 | |
| β-strand | 22-25 | 4 | 4 |
| β-strand | 31-34 | 4 | 4 |
| β-strand | 43-48 | 6 | 4 |
| β-strand | 53-58 | 6 | 4 |
| α-helix | 63 | 1 | |
| β-strand | 64-67 | 4 | 4 |
| β-strand | 73-76 | 4 | 4 |
| α-helix | 81-83 | 3 | |
| β-strand | 84-89 | 6 | 4 |
| α-helix | 91-93 | 3 | |
| β-strand | 95-99 | 5 | 4 |
| α-helix | 107 | 1 | |
| β-strand | 108-111 | 4 | 4 |
| β-strand | 116-123 | 5 | 4 |
| α-helix | 128-130 | 3 | |
| β-strand | 132-136 | 5 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Heparin-binding growth factor 1 | A, B, C, D | protein | 140 | Homo sapiens | P05230 (AlphaFold model) |
>3O3Q_1 Heparin-binding growth factor 1 (chains A, B, C, D) HHHHHHFNLPPGNYKKPKLLYCSNGGHFLRILPDGTVDGTRDRSDQHIQFQLSAESVGEV YIKSTETGQYLAIDTDGLVYGSQTPNEECLFLERLEENHYNTYISKKHGWYLGIKKNGSV KGTHYGQKAILFLPLPVSSD
A polypeptide "building block"top-down symmetric deconstruction". Lee, J., Blaber, S.I., Dubey, V.K. et al. J Mol Biol (2011) 407:744-763. DOI 10.1016/j.jmb.2011.02.002 · 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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