1F59: Importin-beta-fxfg nucleoporin complex

Importin-beta-fxfg nucleoporin complex. Determined by X-ray diffraction at 2.8 Å resolution. Released 16 Aug 2000.

Method: X-ray diffraction
Resolution: 2.8 Å
Organisms: Homo sapiens, Saccharomyces cerevisiae
Chains: 4
Atoms: 7,158
Mol. weight: 104.14 kDa
Released: 16 Aug 2000

Explore 1F59 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1F59 contains 57 α-helices and 0 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: 29 helices, 0 β-strands

Element	Residues	Length
α-helix	3-8	6
α-helix	15-29	15
α-helix	33-45	13
α-helix	51-62	12
α-helix	70-81	12
α-helix	85-98	14
α-helix	108-120	13
α-helix	121-123	3
α-helix	129-138	10
α-helix	144-160	17
α-helix	163-169	7
α-helix	170-179	10
α-helix	188-201	14
α-helix	206-210	5
α-helix	212-225	14
α-helix	231-247	17
α-helix	249-252	4
α-helix	253-255	3
α-helix	256-260	5
α-helix	261-269	9
α-helix	273-300	28
α-helix	301-303	3
α-helix	314-329	16
α-helix	344-358	15
α-helix	363-374	12
α-helix	380-393	14
α-helix	399-407	9
α-helix	410-416	7
α-helix	422-437	16

Chain B: 28 helices, 0 β-strands

Element	Residues	Length
α-helix	3-8	6
α-helix	15-29	15
α-helix	33-43	11
α-helix	51-62	12
α-helix	70-81	12
α-helix	85-98	14
α-helix	108-120	13
α-helix	121-123	3
α-helix	129-138	10
α-helix	144-160	17
α-helix	163-169	7
α-helix	170-179	10
α-helix	188-201	14
α-helix	206-210	5
α-helix	212-225	14
α-helix	231-247	17
α-helix	249-254	6
α-helix	256-260	5
α-helix	261-269	9
α-helix	273-300	28
α-helix	301-303	3
α-helix	314-329	16
α-helix	344-358	15
α-helix	363-374	12
α-helix	380-393	14
α-helix	399-407	9
α-helix	410-416	7
α-helix	423-438	16

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Importin beta-1	A, B	protein	442	Homo sapiens	Q14974 (AlphaFold model)
Fxfg nucleoporin repeats	C, D	protein	28	Saccharomyces cerevisiae

Sequence of entity 1 (A, B), FASTA

>1F59_1 IMPORTIN BETA-1 (chains A, B)
MELITILEKTVSPDRLELEAAQKFLERAAVENLPTFLVELSRVLANPGNSQVARVAAGLQ
IKNSLTSKDPDIKAQYQQRWLAIDANARREVKNYVLHTLGTETYRPSSASQCVAGIACAE
IPVNQWPELIPQLVANVTNPNSTEHMKESTLEAIGYICQDIDPEQLQDKSNEILTAIIQG
MRKEEPSNNVKLAATNALLNSLEFTKANFDKESERHFIMQVVCEATQCPDTRVRVAALQN
LVKIMSLYYQYMETYMGPALFAITIEAMKSDIDEVALQGIEFWSNVCDEEMDLAIEASEA
AEQGRPPEHTSKFYAKGALQYLVPILTQTLTKQDENDDDDDWNPCKAAGVCLMLLATCCE
DDIVPHVLPFIKEHIKNPDWRYRDAAVMAFGCILEGPEPSQLKPLVIQAMPTLIELMKDP
SVVVRDTAAWTVGRICELLPEA

Sequence of entity 2 (C, D), FASTA

>1F59_2 FXFG NUCLEOPORIN REPEATS (chains C, D)
XDDSKPAFSFGXXXXXXXXXXXAFSFGX

Primary citation

Structural basis for the interaction between FxFG nucleoporin repeats and importin-beta in nuclear trafficking. Bayliss, R., Littlewood, T., Stewart, M. Cell (2000) 102:99-108. DOI 10.1016/S0092-8674(00)00014-3 · PubMed

Other PDB entries of the same protein (UniProt Q14974 (AlphaFold model), which also has an AlphaFold model), best resolution first:

1IBR 2.3 Å, Complex of ran with importin beta
1QGR 2.3 Å, Structure of importin beta bound to the ibb domain of importin alpha (II crystal form,…
2P8Q 2.35 Å, Crystal Structure of human Importin beta bound to the Snurportin1 IBB-domain
1QGK 2.5 Å, Structure of importin beta bound to the ibb domain of importin alpha
3W5K 2.6 Å, Crystal structure of Snail1 and importin beta complex
9N85 2.6 Å, Cryo-EM structure of human importin beta:Ran-GTP:RanBP1 trimeric complex
1O6O 2.8 Å, Importin Beta aa1-442 bound to five FxFG repeats from yeast Nsp1p. Second crystal form
1O6P 2.8 Å, Importin Beta bound to a GLFG Nucleoporin peptide
2QNA 2.84 Å, Crystal structure of human Importin-beta (127-876) in complex with the IBB-domain of…
1M5N 2.9 Å, Crystal structure of HEAT repeats (1-11) of importin b bound to the non-classical…
3LWW 3.15 Å, Structure of an open and closed conformation of Human Importin Beta bound to the…
2Q5D 3.2 Å, Crystal Structure of Human Importin Beta bound to the Snurportin1 IBB-domain second…

Browse structure collections

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