3KES: Nucleoporin NUP145

Crystal structure of the autoproteolytic domain from the nuclear pore complex component NUP145 from Saccharomyces cerevisiae in the Hexagonal, P61 space group. Determined by X-ray diffraction at 2.1 Å resolution. Released 22 Dec 2009.

Method: X-ray diffraction
Resolution: 2.1 Å
Organism: Saccharomyces cerevisiae
Chains: 2
Atoms: 2,574
Mol. weight: 42.18 kDa
Released: 22 Dec 2009

Explore 3KES in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3KES contains 14 α-helices and 24 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: 6 helices, 11 β-strands

Element	Residues	Length	Sheet
β-strand	461-464	4	1
α-helix	467-470	4
α-helix	475-478	4
β-strand	481	1	2
β-strand	485-488	4	1
β-strand	492-496	5	1
β-strand	500	1	2
α-helix	503-505	3
α-helix	509-513	5
β-strand	514	1	3
β-strand	518-521	4	3
β-strand	525-528	4	3
α-helix	532-534	3
β-strand	546-550	5	1
α-helix	570-582	13
β-strand	587-592	6	1
β-strand	597-602	6	1

Chain B: 8 helices, 13 β-strands

Element	Residues	Length	Sheet
α-helix	454-458	5
β-strand	461-464	4	4
α-helix	467-471	5
α-helix	475-478	4
β-strand	481	1	5
β-strand	485-488	4	4
β-strand	492-496	5	4
β-strand	500	1	5
α-helix	503-505	3
α-helix	509-513	5
β-strand	514	1	6
β-strand	518-521	4	6
β-strand	525-528	4	6
α-helix	532-534	3
α-helix	536-537	2
β-strand	546-550	5	4
β-strand	556	1	7
β-strand	563	1	7
α-helix	570-582	13
β-strand	587-592	6	4
β-strand	597-602	6	4

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Nucleoporin NUP145	A, B	protein	174	Saccharomyces cerevisiae	P49687 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>3KES_1 Nucleoporin NUP145 (chains A, B)
MSLNKQDGENTLQHEKSSSFGYWCSPSPEQLERLSLKQLAAVSNFVIGRRGYGCITFQHD
VDLTAFTKSFREELFGKIVIFRSSKTVEVYPDEATKPMIGHGLNVPAIITLENVYPVDKK
TKKPMKDTTKFAEFQVFDRKLRSMREMNYISYNPFGGTWTFKVNHFEGHHHHHH

Primary citation

Structures of the autoproteolytic domain from the Saccharomyces cerevisiae nuclear pore complex component, Nup145. Sampathkumar, P., Ozyurt, S.A., Do, J. et al. Proteins (2010) 78:1992-1998. DOI 10.1002/prot.22707 · PubMed

Other PDB entries of the same protein (UniProt P49687 (AlphaFold model), which also has an AlphaFold model), best resolution first:

3KEP 1.82 Å, Crystal structure of the autoproteolytic domain from the nuclear pore complex component…
3JRP 2.6 Å, SEC13 with NUP145C (AA109-179) insertion blade
3BG1 3.0 Å, Architecture of a Coat for the Nuclear Pore Membrane
3BG0 3.15 Å, Architecture of a Coat for the Nuclear Pore Membrane
3IKO 3.2 Å, Crystal structure of the heterotrimeric Sec13-Nup145C-Nup84 nucleoporin complex
3JRO 4.0 Å, NUP84-NUP145C-SEC13 edge element of the NPC lattice
4XMM 7.38 Å, Structure of the yeast coat nucleoporin complex, space group C2
4XMN 7.6 Å, Structure of the yeast coat nucleoporin complex, space group P212121
8TIE 8.1 Å, Double nuclear outer ring of Nup84-complexes from the yeast NPC
7N84 11.6 Å, Double nuclear outer ring from the isolated yeast NPC
7N9F 37.0 Å, Structure of the in situ yeast NPC
8ZZ1 Structure of the Nup84 sub-complex of the Nuclear Pore Complex

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