6L4O: API5-FGF2 complex

Crystal structure of API5-FGF2 complex. Determined by X-ray diffraction at 2.6 Å resolution. Released 29 Apr 2020.

Method: X-ray diffraction
Resolution: 2.6 Å
Organism: Homo sapiens
Chains: 2
Atoms: 4,475
Mol. weight: 80.97 kDa
Released: 29 Apr 2020

Explore 6L4O in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

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.

Chain A: 37 helices, 0 β-strands

Element	Residues	Length
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

Chain B: 6 helices, 14 β-strands

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

Molecules and chains

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)

Sequence of entity 1 (A), FASTA

>6L4O_1 Apoptosis inhibitor 5 (chains A)
MGSSHHHHHHSSGLVPRGSHMPTVEELYRNYGILADATEQVGQHKDAYQVILDGVKGGTK
EKRLAAQFIPKFFKHFPELADSAINAQLDLCEDEDVSIRRQAIKELPQFATGENLPRVAD
ILTQLLQTDDSAEFNLVNNALLSIFKMDAKGTLGGLFSQILQGEDIVRERAIKFLSTKLK
TLPDEVLTKEVEELILTESKKVLEDVTGEEFVLFMKILSGLKSLQTVSGRQQLVELVAEQ
ADLEQTFNPSDPDCVDRLLQCTRQAVPLFSKNVHSTRFVTYFCEQVLPNLGTLTTPVEGL
DIQLEVLKLLAEMSSFCGDMEKLETNLRKLFDKLLEYMPLPPEEAENGENAGNEEPKLQF
SYVECLLYSFHQLGRKLPDFLTAKLNAEKLKDFKIRLQYFARGLQVYIRQLRLALQGKTG
EALKTEENKIKVVALKITNNINVLIKDLFHIPPSYKSTVTLSWKPVQKVEIGQKRASEDT
TSGSPPKKSSAGPKRDARQIYNPPSGKYSSNLGNFNYEQRGAFRGSRGGRGWGTRGNRSR
GRLY

Sequence of entity 2 (B), FASTA

>6L4O_2 Fibroblast growth factor 2 (chains B)
MHHHHHHGSLVPRSENLYFQGSAAGSITTLPALPEDGGSGAFPPGHFKDPKRLYCKNGGF
FLRIHPDGRVDGVREKSDPHIKLQLQAEERGVVSIKGVSANRYLAMKEDGRLLASKSVTD
ECFFFERLESNNYNTYRSRKYTSWYVALKRTGQYKLGSKTGPGQKAILFLPMSAKS

Primary citation

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:

3U0R 2.5 Å, Helical repeat structure of apoptosis inhibitor 5 reveals protein-protein interaction…
3V6A 2.6 Å, Helical repeat structure of apoptosis inhibitor 5 reveals protein-protein interaction…

Browse structure collections

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