Research workbench
Crystal structure of cabe, an aromatic hydroxylase from angucycline biosynthesis, determined to 2.7 a resolution
Analyse Crystal structure of cabe, an aromatic hydroxylase from angucycline… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2QA2
- Type
- protein
- Length
- 489 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Polyketide oxygenase cabe
- EC
- 1.14.13.-
- Ligands
- FAD
- Pockets
- 3 · best druggability 0.80
Structure
x-ray diffraction · 1 distinct chain · 32% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Polyketide oxygenase cabe (EC 1.14.13.-) | protein | 489 | 32% helix, 28% strand | — |
Ligands and binding sites
- FAD · Flavin-adenine dinucleotide · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1155 | 0.80 | 0.81 | 102 | FAD |
| 2 | 99 | 0.58 | 0.86 | 24 | empty |
| 3 | 145 | 0.39 | 0.73 | 26 | empty |
Compared structures
- 2QA2 · Crystal structure of CabE, an aromatic hydroxylase from angucycline biosynthesis… · the same entry in another collection · chain A against A, 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
- Elsewhere: RCSB PDB 2QA2 · PDBe 2QA2
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