Research workbench
Crystal structure of cyanobacterial aldehyde-deformylating oxygenase 122F mutant
Analyse Crystal structure of cyanobacterial aldehyde-deformylating oxygenase 122F mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4RC6
- Type
- protein
- Length
- 427 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Aldehyde decarbonylase
- EC
- 4.1.99.5
- UniProt
- Q54764
- Ligands
- FE2
- Pockets
- 3 · best druggability 0.84
Structure
x-ray diffraction · 2 distinct chains · 86% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Aldehyde decarbonylase (EC 4.1.99.5) | protein | 215 | 86% helix, 0% strand | Q54764 |
| B | Aldehyde decarbonylase (EC 4.1.99.5) | protein | 212 | 85% helix, 0% strand | Q54764 |
Ligands and binding sites
- FE2 · Fe (II) ion · metal · 4 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 197 | 0.84 | 0.97 | 31 | empty |
| 2 | 146 | 0.81 | 0.97 | 27 | empty |
| 3 | 144 | 0.51 | 0.79 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 837 Ų buried · 9 hydrogen bonds · protein-protein
Compared structures
- 4RC6 · Crystal structure of cyanobacterial aldehyde-deformylating oxygenase 122F mutant · the same entry in another collection · chain A against A, TM-score 1.00
- Q54764 · AlphaFold monomer V2.0 prediction for aldehyde decarbonylase (Q54764) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 Q54764
- Elsewhere: RCSB PDB 4RC6 · PDBe 4RC6 · UniProt Q54764
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