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Crystal structure of octameric ribulose-1,5-bisphosphate CARBOXYLASE/OXYGENASE (rubisco) from pyrococcus horikoshii OT3 (form- 1 crystal)
Analyse Crystal structure of octameric ribulose-1,5-bisphosphate CARBOXYLASE/OXYGENASE… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2CWX
- Type
- protein
- Length
- 822 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ribulose bisphosphate carboxylase
- EC
- 4.1.1.39
- UniProt
- O58677
- Pockets
- 8 · best druggability 0.79
Structure
x-ray diffraction · 2 distinct chains · 45% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ribulose bisphosphate carboxylase (EC 4.1.1.39) | protein | 414 | 46% helix, 18% strand | O58677 |
| E | Ribulose bisphosphate carboxylase (EC 4.1.1.39) | protein | 408 | 45% helix, 18% strand | O58677 |
Pockets
8 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 796 | 0.79 | 0.83 | 64 | empty |
| 2 | 714 | 0.78 | 0.83 | 54 | empty |
| 3 | 82 | 0.77 | 0.98 | 21 | empty |
| 4 | 70 | 0.36 | 0.77 | 16 | empty |
| 5 | 71 | 0.33 | 0.75 | 14 | empty |
Interfaces
1 interface between chains.
- A–E · 3462 Ų buried · 50 hydrogen bonds · protein-protein
Compared structures
- 2CWX · Crystal structure of octameric ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco)… · the same entry in another collection · chain A against A, TM-score 1.00
- O58677 · AlphaFold monomer V2.0 prediction for ribulose bisphosphate carboxylase (O58677) · a predicted model of the same protein · chain E against A, TM-score 0.98
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 O58677
- Elsewhere: RCSB PDB 2CWX · PDBe 2CWX · UniProt O58677
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