Research workbench
Unactivated rubisco with magnesium and a water molecule bound
Analyse Unactivated rubisco with magnesium and a water molecule bound in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4F0M
- Type
- protein
- Length
- 586 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P23755, P23756
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 448 | — | P23755 |
| B | — | protein | 138 | — | P23756 |
Compared structures
- 4F0M · UNACTIVATED RUBISCO with MAGNESIUM AND A WATER MOLECULE BOUND · the same entry in another collection · chain A against A, TM-score 1.00
- P23756 · AlphaFold monomer V2.0 prediction for ribulose bisphosphate carboxylase small subunit… · a predicted model of the same protein · chain B against A, TM-score 0.99
- P23755 · AlphaFold monomer V2.0 prediction for ribulose bisphosphate carboxylase large chain… · a predicted model of the same protein · chain A 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 P23755
- Every structure of UniProt P23756
- Elsewhere: RCSB PDB 4F0M · PDBe 4F0M · UniProt P23755 · UniProt P23756
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