4JQ5: Human Nup49CCS2+3* coiled-coil segment

Crystal structure of the human Nup49CCS2+3* coiled-coil segment. Determined by X-ray diffraction at 2.19 Å resolution. Released 24 Sept 2014.

Method: X-ray diffraction
Resolution: 2.19 Å
Organism: Homo sapiens
Chains: 12
Atoms: 8,526
Mol. weight: 121.66 kDa
Released: 24 Sept 2014

Explore 4JQ5 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4JQ5 contains 26 α-helices and 0 β-strands across 12 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: 2 helices, 0 β-strands

Element	Residues	Length	Sheet
α-helix	328-357	30
α-helix	368-409	42

Chain B: 2 helices, 0 β-strands

Element	Residues	Length	Sheet
α-helix	329-362	34
α-helix	368-410	43

Chain C: 2 helices, 0 β-strands

Element	Residues	Length	Sheet
α-helix	328-360	33
α-helix	368-409	42

Chain D: 2 helices, 0 β-strands

Element	Residues	Length	Sheet
α-helix	328-362	35
α-helix	368-410	43

Chains E and F: 2 helices, 0 β-strands

Element	Residues	Length	Sheet
α-helix	327-363	37
α-helix	368-410	43

Chain G: 3 helices, 0 β-strands

Element	Residues	Length
α-helix	329-360	32
α-helix	365-367	3
α-helix	368-410	43

Chain H: 2 helices, 0 β-strands

Element	Residues	Length	Sheet
α-helix	328-360	33
α-helix	368-410	43

Chain I: 3 helices, 0 β-strands

Element	Residues	Length
α-helix	327-363	37
α-helix	365-367	3
α-helix	368-409	42

2 more chain groups are not listed. Open the entry in the viewer and use the sequence panel to see them.

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Nucleoporin p58/p45	A, B, C, D, E, F, G, H, I, J, K, L	protein	86	Homo sapiens	Q9BVL2 (AlphaFold model)

Sequence of entity 1 (A, B, C, D, E, F, G, H, I, J, K, L), FASTA

>4JQ5_1 Nucleoporin p58/p45 (chains A, B, C, D, E, F, G, H, I, J, K, L)
SAPADYFRILVQQFEVQLQQYRQQIEELENHLATQANNSHITPQDLSMAMQKIYQTFVAL
AAQLQSIHENVKVLKEQYLGYRKMFL

Primary citation

Architecture of the fungal nuclear pore inner ring complex. Stuwe, T., Bley, C.J., Thierbach, K. et al. Science (2015) 350:56-64. DOI 10.1126/science.aac9176 · PubMed

Other PDB entries of the same protein (UniProt Q9BVL2 (AlphaFold model), which also has an AlphaFold model), best resolution first:

4JO7 1.75 Å, Crystal structure of the human Nup49CCS2+3* Nup57CCS3* complex with 2:2 stoichiometry
4JO9 2.5 Å, Crystal structure of the human Nup49CCS2+3* Nup57CCS3* complex 1:2 stoichiometry
7R5K 12.0 Å, Human nuclear pore complex (constricted)
5IJN 21.4 Å, Composite structure of the inner ring of the human nuclear pore complex (32 copies of…
5IJO 21.4 Å, Alternative composite structure of the inner ring of the human nuclear pore complex (16…
7PER 35.0 Å, Model of the inner ring of the human nuclear pore complex
7R5J 50.0 Å, Human nuclear pore complex (dilated)
9A25 Molecular assembly pathway of the human Nuclear Pore Complex after cell division
9A8T Integrative spatiotemporal modeling of biomolecular processes: application to the…

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