1XIP: N-terminal Domain of Nup159

Crystal Structure of the N-terminal Domain of Nup159. Determined by X-ray diffraction at 2.5 Å resolution. Released 14 Dec 2004.

Method: X-ray diffraction
Resolution: 2.5 Å
Organism: Saccharomyces cerevisiae
Chains: 1
Atoms: 2,981
Mol. weight: 43.18 kDa
Released: 14 Dec 2004

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

Secondary structure: helices and β-sheets

1XIP contains 8 α-helices and 35 β-strands across 1 chain. 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: 8 helices, 35 β-strands

Element	Residues	Length	Sheet
β-strand	3-4	2	1
β-strand	10-13	4	2
β-strand	17-25	9	3
β-strand	40	1	4
β-strand	42-45	4	5
β-strand	50-55	6	5
β-strand	58-63	6	5
α-helix	64-72	9
β-strand	82-85	4	5
β-strand	89-95	7	4
β-strand	98-103	6	4
β-strand	106-111	6	4
β-strand	118-123	6	4
β-strand	128-133	6	6
β-strand	137-142	6	6
β-strand	146-151	6	6
β-strand	157-162	6	6
β-strand	164-169	6	7
β-strand	173-178	6	7
β-strand	183-189	7	7
β-strand	192-199	8	7
α-helix	203-206	4
β-strand	214-220	7	1
β-strand	225-231	7	1
α-helix	232-235	4
β-strand	245-253	9	1
β-strand	256-262	7	1
β-strand	278-288	11	2
β-strand	291-298	8	2
β-strand	303	1	8
β-strand	305-307	3	2
β-strand	312-315	4	2
α-helix	318-320	3
β-strand	323	1	8
α-helix	324-325	2
β-strand	326	1	9
α-helix	327	1
α-helix	332	1
β-strand	333	1	9
α-helix	334	1
β-strand	336-342	7	3
β-strand	364-369	6	3
β-strand	373-380	8	3

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Nucleoporin NUP159	A	protein	388	Saccharomyces cerevisiae	P40477 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>1XIP_1 Nucleoporin NUP159 (chains A)
GASSLKDEVPTETSEDFGFKFLGQKQILPSFNEKLPFASLQNLDISNSKSLFVAASGSKA
VVGELQLLRDHITSDSTPLTFKWEKEIPDVIFVCFHGDQVLVSTRNALYSLDLEELSEFR
TVTSFEKPVFQLKNVNNTLVILNSVNDLSALDLRTKSTKQLAQNVTSFDVTNSQLAVLLK
DRSFQSFAWRNGEMEKQFEFSLPSELEELPVEEYSPLSVTILSPQDFLAVFGNVISETDD
EVSYDQKMYIIKHIDGSASFQETFDITPPFGQIVRFPYMYKVTLSGLIEPDANVNVLASS
CSSEVSIWDSKQVIEPSQDSERAVLPISEETDKDTNPIGVAVDVVTSGTILEPCSGVDTI
ERLPLVYILNNEGSLQIVGLFHVAAIKS

Primary citation

The N-Terminal Domain of Nup159 Forms a beta-Propeller that Functions in mRNA Export by Tethering the Helicase Dbp5 to the Nuclear Pore. Weirich, C.S., Erzberger, J.P., Berger, J.M. et al. Mol Cell (2004) 16:749-760. DOI 10.1016/j.molcel.2004.10.032 · PubMed

Other PDB entries of the same protein (UniProt P40477 (AlphaFold model), which also has an AlphaFold model), best resolution first:

4DS1 1.85 Å, The Structure of a Yeast Dyn2-Nup159 Complex and the Molecular Basis for the Dynein…
3PBP 2.6 Å, Structure of the yeast heterotrimeric Nup82-Nup159-Nup116 nucleoporin complex
3RRM 2.9 Å, S. cerevisiae dbp5 l327v bound to nup159, gle1 h337r, ip6 and adp
3TKN 3.4 Å, Structure of the Nup82-Nup159-Nup98 heterotrimer
7N9F 37.0 Å, Structure of the in situ yeast NPC
8ZZA Integrative structure and functional anatomy of a single spoke of a nuclear pore complex
8ZZB Integrative structure and functional anatomy of three spokes of a nuclear pore complex
8ZZC Integrative structure and functional anatomy of eight spokes of a nuclear pore complex
8ZZK Structure of the S. cerevisiae nuclear pore complex cytoplasmic mRNA export platform,…
9A0F Integrative model of the wild type yeast nuclear pore complex

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