ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit
OrganismNot specified
State in the Current Structure
| Assembly | Oligomeric State | Construct | Mutations and Modifications | Ligands, Ions and Associated Components | Method and Experimental Conditions | Structure Quality |
|---|---|---|---|---|---|---|
| 1 | Protein heterocomplex Heteromer Protein × 16 PDB declaration: hexadecameric(16) Consistent with protein copy count | Chain A; UniProt 1–493 Chain C; UniProt 1–493 Chain E; UniProt 1–493 Chain G; UniProt 1–493 Chain I; UniProt 1–493 Chain K; UniProt 1–493 Chain M; UniProt 1–493 Chain O; UniProt 1–493 | Not recorded | ribulose-1,5-bisphosphate carboxylase/oxygenase small subunit × 8 (O98950) SO4 SULFATE ION × 8 | X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;VAPOR DIFFUSION, HANGING DROP | Resolution 2.60 Å R-free 0.235 |
Other States of the Same Protein in the Database
Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.
1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states
View Construct and Data Evidence
| UniProt name | O98949_9RHOD |
| Isoform | — |
| PDB entities | 1 |
| Chains and sequence ranges | Author chain A; PDBConstruct 1–493; UniProt 1–493 Author chain C; PDBConstruct 1–493; UniProt 1–493 Author chain E; PDBConstruct 1–493; UniProt 1–493 Author chain G; PDBConstruct 1–493; UniProt 1–493 Author chain I; PDBConstruct 1–493; UniProt 1–493 Author chain K; PDBConstruct 1–493; UniProt 1–493 Author chain M; PDBConstruct 1–493; UniProt 1–493 Author chain O; PDBConstruct 1–493; UniProt 1–493 |