Crystal structure of API5-FGF2 complex. Determined by X-ray diffraction at 2.6 Å resolution. Released 29 Apr 2020.
Explore 6L4O in 3D Show helices and sheets RCSB PDB PDBe
6L4O contains 43 α-helices and 14 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 | 4-15 | 12 | |
| α-helix | 25-32 | 8 | |
| α-helix | 33-36 | 4 | |
| α-helix | 39-51 | 13 | |
| α-helix | 53-55 | 3 | |
| α-helix | 57-59 | 3 | |
| α-helix | 60-71 | 12 | |
| α-helix | 76-83 | 8 | |
| α-helix | 86-89 | 4 | |
| α-helix | 92-94 | 3 | |
| α-helix | 95-104 | 10 | |
| α-helix | 105-107 | 3 | |
| α-helix | 111-127 | 17 | |
| α-helix | 129-142 | 14 | |
| α-helix | 145-158 | 14 | |
| α-helix | 159-161 | 3 | |
| α-helix | 169-182 | 14 | |
| α-helix | 183-185 | 3 | |
| α-helix | 188-199 | 12 | |
| α-helix | 202-204 | 3 | |
| α-helix | 207-221 | 15 | |
| α-helix | 226-227 | 2 | |
| α-helix | 232-243 | 12 | |
| α-helix | 246-248 | 3 | |
| α-helix | 256-261 | 6 | |
| α-helix | 262-266 | 5 | |
| α-helix | 267-269 | 3 | |
| α-helix | 282-293 | 12 | |
| α-helix | 294-296 | 3 | |
| α-helix | 303-315 | 13 | |
| α-helix | 319-321 | 3 | |
| α-helix | 340-353 | 14 | |
| α-helix | 354-356 | 3 | |
| α-helix | 359-362 | 4 | |
| α-helix | 367-394 | 28 | |
| α-helix | 402-404 | 3 | |
| α-helix | 406-428 | 23 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 163-167 | 5 | 1 |
| α-helix | 172 | 1 | |
| β-strand | 173-176 | 4 | 1 |
| β-strand | 181-185 | 5 | 1 |
| α-helix | 191-193 | 3 | |
| β-strand | 195-199 | 5 | 1 |
| β-strand | 204-209 | 6 | 1 |
| β-strand | 214-218 | 5 | 1 |
| β-strand | 224-227 | 4 | 1 |
| α-helix | 232-234 | 3 | |
| β-strand | 236-240 | 5 | 1 |
| β-strand | 246-250 | 5 | 1 |
| β-strand | 257 | 1 | 1 |
| β-strand | 260 | 1 | 2 |
| β-strand | 265 | 1 | 1 |
| β-strand | 266 | 1 | 2 |
| α-helix | 267-268 | 2 | |
| α-helix | 269-271 | 3 | |
| α-helix | 277-279 | 3 | |
| β-strand | 281-284 | 4 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Apoptosis inhibitor 5 | A | protein | 544 | Homo sapiens | Q9BZZ5 (AlphaFold model) |
| Fibroblast growth factor 2 | B | protein | 176 | Homo sapiens | P09038 (AlphaFold model) |
>6L4O_1 Apoptosis inhibitor 5 (chains A) MGSSHHHHHHSSGLVPRGSHMPTVEELYRNYGILADATEQVGQHKDAYQVILDGVKGGTK EKRLAAQFIPKFFKHFPELADSAINAQLDLCEDEDVSIRRQAIKELPQFATGENLPRVAD ILTQLLQTDDSAEFNLVNNALLSIFKMDAKGTLGGLFSQILQGEDIVRERAIKFLSTKLK TLPDEVLTKEVEELILTESKKVLEDVTGEEFVLFMKILSGLKSLQTVSGRQQLVELVAEQ ADLEQTFNPSDPDCVDRLLQCTRQAVPLFSKNVHSTRFVTYFCEQVLPNLGTLTTPVEGL DIQLEVLKLLAEMSSFCGDMEKLETNLRKLFDKLLEYMPLPPEEAENGENAGNEEPKLQF SYVECLLYSFHQLGRKLPDFLTAKLNAEKLKDFKIRLQYFARGLQVYIRQLRLALQGKTG EALKTEENKIKVVALKITNNINVLIKDLFHIPPSYKSTVTLSWKPVQKVEIGQKRASEDT TSGSPPKKSSAGPKRDARQIYNPPSGKYSSNLGNFNYEQRGAFRGSRGGRGWGTRGNRSR GRLY
>6L4O_2 Fibroblast growth factor 2 (chains B) MHHHHHHGSLVPRSENLYFQGSAAGSITTLPALPEDGGSGAFPPGHFKDPKRLYCKNGGF FLRIHPDGRVDGVREKSDPHIKLQLQAEERGVVSIKGVSANRYLAMKEDGRLLASKSVTD ECFFFERLESNNYNTYRSRKYTSWYVALKRTGQYKLGSKTGPGQKAILFLPMSAKS
Regulation of mRNA export through API5 and nuclear FGF2 interaction. Bong, S.M., Bae, S.H., Song, B. et al. Nucleic Acids Res (2020) 48:6340-6352. DOI 10.1093/nar/gkaa335 · PubMed
Other PDB entries of the same protein (UniProt Q9BZZ5 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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