3KEP: Nucleoporin NUP145

Crystal structure of the autoproteolytic domain from the nuclear pore complex component NUP145 from Saccharomyces cerevisiae. Determined by X-ray diffraction at 1.82 Å resolution. Released 22 Dec 2009.

Method
X-ray diffraction
Resolution
1.82 Å
Organism
Saccharomyces cerevisiae
Chains
2
Atoms
2,626
Mol. weight
41.87 kDa
Released
22 Dec 2009

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

Secondary structure: helices and β-sheets

3KEP contains 12 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

ElementResiduesLengthSheet
β-strand461-46441
α-helix467-4715
α-helix477-4793
β-strand48112
β-strand485-48841
β-strand492-49651
β-strand50012
α-helix503-5053
α-helix509-5135
β-strand51413
β-strand518-52143
β-strand525-52843
α-helix535-5373
β-strand546-55051
α-helix570-58213
β-strand587-59261
β-strand597-60261
Chain B: 6 helices, 13 β-strands
ElementResiduesLengthSheet
β-strand461-46444
α-helix467-4715
α-helix475-4784
β-strand48115
β-strand485-48844
β-strand492-49654
β-strand50015
α-helix503-5053
α-helix509-5135
β-strand51416
β-strand518-52146
β-strand525-52846
α-helix535-5373
β-strand546-55054
β-strand55617
β-strand56317
α-helix570-58112
β-strand587-59264
β-strand597-60264

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Nucleoporin NUP145A, Bprotein174Saccharomyces cerevisiaeP49687 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>3KEP_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:

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