Research workbench
Cryo-EM structure of the rbcl-rbcx complex
Analyse Cryo-EM structure of the rbcl-rbcx complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2WVW
- Type
- protein
- Length
- 5,416 residues
- Chains
- 24
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ribulose bisphosphate carboxylase large chain; Rbcx protein
- EC
- 4.1.1.39
- UniProt
- P00880, Q44212
- Pockets
- 20 · best druggability 0.82
Structure
electron microscopy · 2 distinct chains · 52% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H | Ribulose bisphosphate carboxylase large chain (EC 4.1.1.39) | protein | 467 | 44% helix, 17% strand | P00880 |
| I, J, K, L, M, N, O, P, Q, R, S, T, U, V, W, X | Rbcx protein | protein | 105 | 89% helix, 0% strand | Q44212 |
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1002 | 0.82 | 0.83 | 77 | empty |
| 2 | 971 | 0.81 | 0.83 | 72 | empty |
| 3 | 964 | 0.81 | 0.83 | 73 | empty |
| 4 | 977 | 0.81 | 0.83 | 76 | empty |
| 5 | 860 | 0.81 | 0.83 | 62 | empty |
Interfaces
56 interfaces between chains.
- A–H · 4483 Ų buried · 88 hydrogen bonds · protein-protein
- F–G · 4474 Ų buried · 89 hydrogen bonds · protein-protein
- B–C · 4472 Ų buried · 86 hydrogen bonds · protein-protein
- D–E · 4465 Ų buried · 86 hydrogen bonds · protein-protein
- U–V · 2350 Ų buried · 11 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- 2WVW · Cryo-EM structure of the RbcL-RbcX complex · the same entry in another collection · chain K against K, TM-score 1.00
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 2WVW · PDBe 2WVW · UniProt P00880 · UniProt Q44212
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