2KRB: EIF3B-RRM

Solution structure of EIF3B-RRM bound to EIF3J peptide. Determined by solution NMR. Released 5 Jan 2010.

Method
Solution NMR
Organism
Homo sapiens
Chains
2
Atoms
745
Mol. weight
10.56 kDa
Released
5 Jan 2010

Explore 2KRB in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2KRB contains 2 α-helices and 5 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: 2 helices, 5 β-strands

ElementResiduesLengthSheet
β-strand17-2151
α-helix31-4313
β-strand48-5251
β-strand5612
β-strand5912
β-strand63-6861
α-helix71-788

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Eukaryotic translation initiation factor 3 subunit BAprotein81Homo sapiensP55884 (AlphaFold model)
Eukaryotic translation initiation factor 3 subunit JBprotein11Homo sapiensO75822 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>2KRB_1 Eukaryotic translation initiation factor 3 subunit B (chains A)
DSVIVVDNVPQVGPDRLEKLKNVIHKIFSKFGKITNDFYPEEDGKTKGYIFLEYASPAHA
VDAVKNADGYKLDKQHTFRVN
Sequence of entity 2 (B), FASTA
>2KRB_2 Eukaryotic translation initiation factor 3 subunit J (chains B)
DEDVKDNWDDD

Primary citation

The indispensable N-terminal half of eIF3j/HCR1 co-operates with its structurally conserved binding partner eIF3b/PRT1-RRM and eIF1A in stringent AUG selection. Elantak, L., Wagner, S., Herrmannova, A. et al. To be published.

Other PDB entries of the same protein (UniProt P55884 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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