Research workbench
Rubisco / CSOS2 N-peptide complex responsible for alpha-carboxysome cargo loading
Analyse Rubisco / CSOS2 N-peptide complex responsible for alpha-carboxysome cargo… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6UEW
- Type
- protein
- Length
- 2,228 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ribulose bisphosphate carboxylase large chain, CSOS2 N- peptide fusion; Ribulose…
- EC
- 4.1.1.39
- UniProt
- O85040, P45686
- Pockets
- 20 · best druggability 0.86
Structure
x-ray diffraction · 8 distinct chains · 42% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ribulose bisphosphate carboxylase large chain, CSOS2 N- peptide fusion (EC 4.1.1.39) | protein | 453 | 46% helix, 19% strand | O85040 |
| B | Ribulose bisphosphate carboxylase small chain (EC 4.1.1.39) | protein | 104 | 29% helix, 27% strand | P45686 |
| C | Ribulose bisphosphate carboxylase large chain, CSOS2 N- peptide fusion (EC 4.1.1.39) | protein | 455 | 45% helix, 19% strand | O85040 |
| D | Ribulose bisphosphate carboxylase small chain (EC 4.1.1.39) | protein | 106 | 28% helix, 25% strand | P45686 |
| E | Ribulose bisphosphate carboxylase large chain, CSOS2 N- peptide fusion (EC 4.1.1.39) | protein | 450 | 46% helix, 18% strand | O85040 |
| F | Ribulose bisphosphate carboxylase small chain (EC 4.1.1.39) | protein | 105 | 28% helix, 26% strand | P45686 |
| G | Ribulose bisphosphate carboxylase large chain, CSOS2 N- peptide fusion (EC 4.1.1.39) | protein | 454 | 46% helix, 19% strand | O85040 |
| H | Ribulose bisphosphate carboxylase small chain (EC 4.1.1.39) | protein | 101 | 30% helix, 25% strand | P45686 |
Pockets
20 pockets found on a 1 Å grid, 12 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1168 | 0.86 | 0.87 | 147 | empty |
| 2 | 892 | 0.84 | 0.86 | 101 | empty |
| 3 | 786 | 0.81 | 0.84 | 97 | empty |
| 4 | 88 | 0.75 | 0.98 | 32 | empty |
| 5 | 329 | 0.68 | 0.82 | 50 | empty |
Interfaces
17 interfaces between chains.
- A–E · 3364 Ų buried · 48 hydrogen bonds · protein-protein
- C–D · 1783 Ų buried · 21 hydrogen bonds · protein-protein
- E–F · 1772 Ų buried · 25 hydrogen bonds · protein-protein
- A–B · 1694 Ų buried · 22 hydrogen bonds · protein-protein
- G–H · 1691 Ų buried · 25 hydrogen bonds · protein-protein
Compared structures
- 6UEW · Rubisco / CsoS2 N-peptide complex responsible for alpha-carboxysome cargo loading · the same entry in another collection · chain H against H, TM-score 1.00
- P45686 · AlphaFold monomer V2.0 prediction for ribulose bisphosphate carboxylase small subunit… · a predicted model of the same protein · chain B 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 O85040
- Every structure of UniProt P45686
- Elsewhere: RCSB PDB 6UEW · PDBe 6UEW · UniProt O85040 · UniProt P45686
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