› 3j8b

Electron Microscopy
9.3Å resolution

Model of the human eIF3 PCI-MPN octamer docked into the 43S-HCV IRES EM map

Released:
DOI: 10.2210/pdb3j8b/pdb
PDB entry 3j8b coloured by chain, front view.
PDB entry 3j8b coloured by chain, side view.
PDB entry 3j8b coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Molecular architecture of the 40S⋅eIF1⋅eIF3 translation initiation complex.
Erzberger JP, Stengel F, Pellarin R, Zhang S, Schaefer T, Aylett CHS, Cimermančič P, Boehringer D, Sali A, Aebersold R, Ban N
Cell 158 1123-1135 (2014)
PMID: 25171412
Related structures: EMD-2451

Function and Biology Details

Reaction catalysed: 
Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
hetero octamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-126239 (preferred)
Entry contents:
8 distinct polypeptide molecules
Macromolecules (8 distinct):
Eukaryotic translation initiation factor 3 subunit A Chain: A
Molecule details ›
Chain: A
Length: 529 amino acids
Theoretical weight: 61.04 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: Q14152 (Residues: 1-494; Coverage: 36%)
Gene names: EIF3A, EIF3S10, KIAA0139
Sequence domains: PCI domain
Eukaryotic translation initiation factor 3 subunit C Chain: C
Molecule details ›
Chain: C
Length: 547 amino acids
Theoretical weight: 62.81 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: Q99613 (Residues: 326-846; Coverage: 57%)
Gene names: EIF3C, EIF3S8
Sequence domains:
Eukaryotic translation initiation factor 3 subunit E Chain: E
Molecule details ›
Chain: E
Length: 422 amino acids
Theoretical weight: 48.85 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: P60228 (Residues: 1-395; Coverage: 89%)
Gene names: EIF3E, EIF3S6, INT6
Sequence domains:
Eukaryotic translation initiation factor 3 subunit F Chain: F
Molecule details ›
Chain: F
Length: 327 amino acids
Theoretical weight: 32.76 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: O00303 (Residues: 1-257; Coverage: 72%)
Gene names: EIF3F, EIF3S5
Sequence domains: JAB1/Mov34/MPN/PAD-1 ubiquitin protease
Eukaryotic translation initiation factor 3 subunit H Chain: H
Molecule details ›
Chain: H
Length: 343 amino acids
Theoretical weight: 35.13 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: O15372 (Residues: 1-221; Coverage: 63%)
Gene names: EIF3H, EIF3S3
Sequence domains:
Eukaryotic translation initiation factor 3 subunit K Chain: K
Molecule details ›
Chain: K
Length: 208 amino acids
Theoretical weight: 23.53 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: Q9UBQ5 (Residues: 1-190; Coverage: 87%)
Gene names: ARG134, EIF3K, EIF3S12, HSPC029, MSTP001, PTD001
Sequence domains: CSN8/PSMD8/EIF3K family
Eukaryotic translation initiation factor 3 subunit L Chain: L
Molecule details ›
Chain: L
Length: 540 amino acids
Theoretical weight: 63.01 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: Q9Y262 (Residues: 1-515; Coverage: 91%)
Gene names: EIF3EIP, EIF3L, EIF3S6IP, HSPC021, HSPC025, MSTP005
Sequence domains: RNA polymerase I-associated factor PAF67
Eukaryotic translation initiation factor 3 subunit M Chain: M
Molecule details ›
Chain: M
Length: 364 amino acids
Theoretical weight: 40.4 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: Q7L2H7 (Residues: 1-335; Coverage: 90%)
Gene names: EIF3M, GA17, HFLB5, PCID1, PNAS-125
Sequence domains: PCI domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 9.3Å
Relevant EMDB volumes: EMD-2451

Quick links

Citations

40 review citations

The nuclear pore complex: understanding its function through structural insight.
Beck et al. (2017)
39 more

1 mention without citation

Identifying direct contacts between protein complex subunits from their conditional dependence in proteomics datasets.
Drew et al. (2017)