Structure of the Brx1 and Ebp2 complex. Determined by X-ray diffraction at 2.29 Å resolution. Released 11 Apr 2018.
Explore 5Z1G in 3D Show helices and sheets RCSB PDB PDBe
5Z1G contains 23 α-helices and 32 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 |
|---|---|---|---|
| α-helix | 198-208 | 11 | |
| α-helix | 212-214 | 3 | |
| α-helix | 217-219 | 3 | |
| β-strand | 222-224 | 3 | 1 |
| α-helix | 239-263 | 25 | |
| α-helix | 270-271 | 2 | |
| β-strand | 278 | 1 | 2 |
| α-helix | 282-288 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 33-37 | 5 | 3 |
| α-helix | 43-55 | 13 | |
| β-strand | 59-61 | 3 | 3 |
| α-helix | 73-80 | 8 | |
| β-strand | 85-92 | 8 | 3 |
| β-strand | 96-102 | 7 | 3 |
| β-strand | 109-118 | 10 | 3 |
| β-strand | 130 | 1 | 4 |
| β-strand | 133 | 1 | 5 |
| α-helix | 134-135 | 2 | |
| β-strand | 136-139 | 4 | 3 |
| α-helix | 141-144 | 4 | |
| α-helix | 147-160 | 14 | |
| β-strand | 170 | 1 | 5 |
| β-strand | 175-182 | 8 | 3 |
| β-strand | 185-194 | 10 | 3 |
| β-strand | 211-214 | 4 | 3 |
| β-strand | 218-227 | 10 | 3 |
| β-strand | 235-238 | 4 | 3 |
| α-helix | 245-253 | 9 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 33-37 | 5 | 1 |
| α-helix | 43-55 | 13 | |
| β-strand | 59-61 | 3 | 1 |
| α-helix | 73-80 | 8 | |
| β-strand | 85-92 | 8 | 1 |
| β-strand | 96-102 | 7 | 1 |
| β-strand | 109-118 | 10 | 1 |
| β-strand | 130 | 1 | 2 |
| β-strand | 133 | 1 | 6 |
| β-strand | 136-139 | 4 | 1 |
| α-helix | 141-144 | 4 | |
| α-helix | 147-160 | 14 | |
| β-strand | 170 | 1 | 6 |
| β-strand | 175-182 | 8 | 1 |
| β-strand | 185-194 | 10 | 1 |
| β-strand | 211-214 | 4 | 1 |
| β-strand | 218-227 | 10 | 1 |
| β-strand | 235-238 | 4 | 1 |
| α-helix | 245-253 | 9 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| rRNA-processing protein EBP2 | A, C | protein | 110 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) | P36049 (AlphaFold model) |
| Ribosome biogenesis protein BRX1 | B, D | protein | 234 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) | Q08235 (AlphaFold model) |
>5Z1G_1 rRNA-processing protein EBP2 (chains A, C) DVVPHHKLTVNNTKAMKHALERVQLPWKKHSFQEHQSVTSETNTDEHIKDIYDDTERELA FYKQSLDAVLVARDELKRLKVPFKRPLDYFAEMVKSDEHMDKIKGKLIEE
>5Z1G_2 Ribosome biogenesis protein BRX1 (chains B, D) QFMNKQRTLLISSRGVNYRHRHLIQDLSGLLPHSRKEPKLDTKKDLQQLNEIAELYNCNN VLFFEARKHQDLYLWLSKPPNGPTIKFYIQNLHTMDELNFTGNCLKGSRPVLSFDQRFES SPHYQLIKELLVHNFGVPPNARKSKPFIDHVMSFSIVDDKIWVRTYEISHSTKNKEEYED GEEDISLVEIGPRFVMTVILILEGSFGGPKIYENKQYVSPNVVRAQIKQQAAEE
Cryo-EM structure of an early precursor of large ribosomal subunit reveals a half-assembled intermediate. Zhou, D., Zhu, X., Zheng, S. et al. Protein Cell (2019) 10:120-130. DOI 10.1007/s13238-018-0526-7 · PubMed
Other PDB entries of the same protein (UniProt P36049 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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