Crystal structure of RbcX-IIa from Chlamydomonas reinhardtii. Determined by X-ray diffraction at 1.6 Å resolution. Released 5 Aug 2015.
Explore 5BS1 in 3D Show helices and sheets RCSB PDB PDBe
5BS1 contains 27 α-helices and 0 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 | 36-38 | 3 | |
| α-helix | 46-71 | 26 | |
| α-helix | 79-92 | 14 | |
| α-helix | 99-101 | 3 | |
| α-helix | 102-111 | 10 | |
| α-helix | 113-129 | 17 | |
| α-helix | 132-154 | 23 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 37-39 | 3 | |
| α-helix | 46-70 | 25 | |
| α-helix | 79-92 | 14 | |
| α-helix | 95-97 | 3 | |
| α-helix | 102-111 | 10 | |
| α-helix | 113-126 | 14 | |
| α-helix | 132-154 | 23 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 36-38 | 3 | |
| α-helix | 46-71 | 26 | |
| α-helix | 80-92 | 13 | |
| α-helix | 99-101 | 3 | |
| α-helix | 102-111 | 10 | |
| α-helix | 113-129 | 17 | |
| α-helix | 132-153 | 22 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 37-39 | 3 | |
| α-helix | 46-70 | 25 | |
| α-helix | 76-92 | 17 | |
| α-helix | 102-111 | 10 | |
| α-helix | 113-126 | 14 | |
| α-helix | 132-153 | 22 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| CrRbcX-IIa | A, B, C, D | protein | 123 | Chlamydomonas reinhardtii | A0A2K3E6P2 (AlphaFold model) |
>5BS1_1 CrRbcX-IIa (chains A, B, C, D) MHIPADSFSGASPERKAAVALRSLFTFVAARVVLEQLQGPGGPETTYNQQAYLDLMDFLG TPMKGDGGDEWMAAVMRKNHALALRLMEVREAYLDEFEWGKTMEMASRETREANTRLMRA AAM
| ID | Name | Formula | Copies |
|---|---|---|---|
| MG | Magnesium ion | Mg | 1 |
Structural Analysis of the Rubisco-Assembly Chaperone RbcX-II from Chlamydomonas reinhardtii. Bracher, A., Hauser, T., Liu, C. et al. PLoS One (2015) 10:e0135448-e0135448. DOI 10.1371/journal.pone.0135448 · PubMed
Other PDB entries of the same protein (UniProt A0A2K3E6P2 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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