Structure of eukaryotic translation initiation factor eIF3i complex with eIF3b C-terminus (655-700). Determined by X-ray diffraction at 2.2 Å resolution. Released 5 Oct 2011.
Explore 3ZWL in 3D Show helices and sheets RCSB PDB PDBe
3ZWL contains 12 α-helices and 62 β-strands across 4 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 1-7 | 7 | 1 |
| β-strand | 13-18 | 6 | 2 |
| β-strand | 24-29 | 6 | 2 |
| β-strand | 34-38 | 5 | 2 |
| β-strand | 44-48 | 5 | 2 |
| β-strand | 55-60 | 6 | 3 |
| β-strand | 66-71 | 6 | 3 |
| β-strand | 75-80 | 6 | 3 |
| β-strand | 86-91 | 6 | 3 |
| β-strand | 96-101 | 6 | 4 |
| β-strand | 107-112 | 6 | 4 |
| α-helix | 113-114 | 2 | |
| β-strand | 115 | 1 | 5 |
| β-strand | 118 | 1 | 5 |
| β-strand | 121-126 | 6 | 4 |
| β-strand | 127-129 | 3 | 6 |
| β-strand | 136-139 | 4 | 6 |
| β-strand | 145-148 | 4 | 4 |
| β-strand | 156-161 | 6 | 7 |
| α-helix | 163-165 | 3 | |
| β-strand | 167-172 | 6 | 7 |
| β-strand | 176-181 | 6 | 7 |
| β-strand | 187-193 | 7 | 7 |
| β-strand | 199-204 | 6 | 8 |
| β-strand | 210-215 | 6 | 8 |
| β-strand | 219-224 | 6 | 8 |
| β-strand | 230-235 | 6 | 8 |
| β-strand | 240-245 | 6 | 9 |
| α-helix | 246 | 1 | |
| β-strand | 251-256 | 6 | 9 |
| β-strand | 274-279 | 6 | 9 |
| β-strand | 285-290 | 6 | 9 |
| β-strand | 296-301 | 6 | 1 |
| β-strand | 307-312 | 6 | 1 |
| β-strand | 316-322 | 7 | 1 |
| α-helix | 324-327 | 4 | |
| α-helix | 332-339 | 8 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 1-6 | 6 | 10 |
| β-strand | 13-18 | 6 | 11 |
| β-strand | 24-29 | 6 | 11 |
| β-strand | 34-38 | 5 | 11 |
| β-strand | 44-48 | 5 | 11 |
| β-strand | 55-60 | 6 | 12 |
| β-strand | 66-71 | 6 | 12 |
| β-strand | 75-80 | 6 | 12 |
| β-strand | 85-91 | 7 | 12 |
| β-strand | 96-101 | 6 | 13 |
| β-strand | 107-112 | 6 | 13 |
| α-helix | 113 | 1 | |
| β-strand | 121-126 | 6 | 13 |
| β-strand | 127-129 | 3 | 14 |
| β-strand | 136-139 | 4 | 14 |
| β-strand | 145-148 | 4 | 13 |
| β-strand | 156-161 | 6 | 15 |
| α-helix | 163-165 | 3 | |
| β-strand | 167-172 | 6 | 15 |
| β-strand | 176-181 | 6 | 15 |
| β-strand | 187-193 | 7 | 15 |
| β-strand | 199-204 | 6 | 16 |
| β-strand | 210-215 | 6 | 16 |
| β-strand | 219-224 | 6 | 16 |
| β-strand | 230-235 | 6 | 16 |
| β-strand | 240-245 | 6 | 17 |
| α-helix | 246 | 1 | |
| β-strand | 251-256 | 6 | 17 |
| β-strand | 273-279 | 7 | 17 |
| β-strand | 285-292 | 8 | 17 |
| β-strand | 296-301 | 6 | 10 |
| β-strand | 307-312 | 6 | 10 |
| β-strand | 317-322 | 6 | 10 |
| α-helix | 324-327 | 4 | |
| α-helix | 332-339 | 8 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 663-689 | 27 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Eukaryotic translation initiation factor 3 subunit I | B, D | protein | 369 | SACCHAROMYCES CEREVISIAE | P40217 (AlphaFold model) |
| Eukaryotic translation initiation factor 3 subunit B | E, F | protein | 50 | SACCHAROMYCES CEREVISIAE | P06103 (AlphaFold model) |
>3ZWL_1 EUKARYOTIC TRANSLATION INITIATION FACTOR 3 SUBUNIT I (chains B, D) MGSSHHHHHHSSGENLYFQGSHMKAIKLTGHERPLTQVKYNKEGDLLFSCSKDSSASVWY SLNGERLGTLDGHTGTIWSIDVDCFTKYCVTGSADYSIKLWDVSNGQCVATWKSPVPVKR VEFSPCGNYFLAILDNVMKNPGSINIYEIERDSATHELTKVSEEPIHKIITHEGLDAATV AGWSTKGKYIIAGHKDGKISKYDVSNNYEYVDSIDLHEKSISDMQFSPDLTYFITSSRDT NSFLVDVSTLQVLKKYETDCPLNTAVITPLKEFIILGGGQEAKDVTTTSANEGKFEARFY HKIFEEEIGRVQGHFGPLNTVAISPQGTSYASGGEDGFIRLHHFEKSYFDFKYDVEKAAE AKEHMQEAN
>3ZWL_2 EUKARYOTIC TRANSLATION INITIATION FACTOR 3 SUBUNIT B (chains E, F) GSHMEADTAMRDLILHQRELLKQWTEYREKIGQEMEKSMNFKIFDVQPED
Structural Analysis of an Eif3 Subcomplex Reveals Conserved Interactions Required for a Stable and Proper Translation Pre-Initiation Complex Assembly. Herrmannova, A., Daujotyte, D., Yang, J.C. et al. Nucleic Acids Res (2012) 40:2294. DOI 10.1093/NAR/GKR765 · PubMed
Other PDB entries of the same protein (UniProt P40217 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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