Research workbench
Structure of an effector induced inactivated state of ribulose bisphosphate CARBOXYLASE(SLASH)OXYGENASE: the binary complex between enzyme and xylulose bisphosphate
Analyse Structure of an effector induced inactivated state of ribulose bisphosphate… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1RSC
- Type
- protein
- Length
- 4,608 residues
- Chains
- 16
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ribulose 1,5 bisphosphate CARBOXYLASE/OXYGENASE (large chain); Ribulose 1,5 bisphosphate…
- EC
- 4.1.1.39
- UniProt
- P00880, P04716
- Ligands
- XBP
- Pockets
- 20 · best druggability 0.86
Structure
x-ray diffraction · 2 distinct chains · 40% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H | Ribulose 1,5 bisphosphate CARBOXYLASE/OXYGENASE (large chain) (EC 4.1.1.39) | protein | 467 | 44% helix, 17% strand | P00880 |
| M, I, N, J, O, K, P, L | Ribulose 1,5 bisphosphate CARBOXYLASE/OXYGENASE (small chain) (EC 4.1.1.39) | protein | 109 | 26% helix, 24% strand | P04716 |
Ligands and binding sites
- XBP · Xylulose-1,5-bisphosphate · ligand · 8 copies · chains A, B, C, D, E, F, G, H
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 | 955 | 0.86 | 0.88 | 147 | empty |
| 2 | 1000 | 0.85 | 0.86 | 111 | empty |
| 3 | 1113 | 0.83 | 0.84 | 114 | empty |
| 4 | 135 | 0.80 | 0.98 | 46 | XBP |
| 5 | 126 | 0.80 | 0.98 | 43 | XBP |
Interfaces
48 interfaces between chains.
- G–H · 5003 Ų buried · 106 hydrogen bonds · protein-protein
- E–F · 4969 Ų buried · 106 hydrogen bonds · protein-protein
- A–B · 4962 Ų buried · 100 hydrogen bonds · protein-protein
- C–D · 4933 Ų buried · 96 hydrogen bonds · protein-protein
- F–K · 1659 Ų buried · 23 hydrogen bonds · protein-protein
Compared structures
- 1RSC · Structure of an effector induced inactivated state of ribulose bisphosphate… · the same entry in another collection · chain L against L, 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 P04716
- Elsewhere: RCSB PDB 1RSC · PDBe 1RSC · UniProt P00880 · UniProt P04716
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.