Research workbench
Crystal structure of fe-CAO1
Analyse Crystal structure of fe-CAO1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5U8X
- Type
- protein
- Length
- 1,991 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Carotenoid oxygenase 1
- UniProt
- Q7S860
- Ligands
- FE2, CL
- Pockets
- 20 · best druggability 0.88
Structure
x-ray diffraction · 2 distinct chains · 8% helix, 38% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, D | Carotenoid oxygenase 1 | protein | 497 | 8% helix, 38% strand | Q7S860 |
| C | Carotenoid oxygenase 1 | protein | 500 | 8% helix, 38% strand | Q7S860 |
Ligands and binding sites
- FE2 · Fe (II) ion · metal · 4 copies · chains A, B, C, D
- CL · Chloride ion · ion · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 | 1018 | 0.88 | 0.89 | 144 | empty |
| 2 | 1016 | 0.88 | 0.89 | 139 | empty |
| 3 | 437 | 0.83 | 0.91 | 64 | empty |
| 4 | 473 | 0.83 | 0.90 | 69 | empty |
| 5 | 369 | 0.82 | 0.91 | 68 | empty |
Interfaces
4 interfaces between chains.
- B–C · 1514 Ų buried · 35 hydrogen bonds · protein-protein
- A–D · 1507 Ų buried · 33 hydrogen bonds · protein-protein
- A–B · 378 Ų buried · 1 hydrogen bond · protein-protein
- C–D · 368 Ų buried · 2 hydrogen bonds · protein-protein
Compared structures
- 5U8X · Crystal structure of Fe-CAO1 · the same entry in another collection · chain D against D, 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 Q7S860
- Elsewhere: RCSB PDB 5U8X · PDBe 5U8X · UniProt Q7S860
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