Research workbench
Crystal structure of a chaperone-bound assembly intermediate of form I rubisco
Analyse Crystal structure of a chaperone-bound assembly intermediate of form I rubisco in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3RG6
- Type
- protein
- Length
- 1,322 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P00880, Q44212
Structure
x-ray diffraction · 6 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 442 | — | P00880 |
| C | — | protein | 115 | — | Q44212 |
| D | — | protein | 107 | — | Q44212 |
| B | — | protein | 438 | — | P00880 |
| E | — | protein | 114 | — | Q44212 |
| F | — | protein | 106 | — | Q44212 |
Compared structures
- 3RG6 · Crystal structure of a chaperone-bound assembly intermediate of form I Rubisco · the same entry in another collection · chain F against F, TM-score 1.00
- Q44212 · AlphaFold monomer V2.0 prediction for rubisco chaperone rbcx (Q44212) · a predicted model of the same protein · chain D against A, TM-score 0.98
- P00880 · AlphaFold monomer V2.0 prediction for ribulose bisphosphate carboxylase large chain… · a predicted model of the same protein · chain B against A, TM-score 0.97
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P00880
- Every structure of UniProt Q44212
- Elsewhere: RCSB PDB 3RG6 · PDBe 3RG6 · UniProt P00880 · UniProt Q44212
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