Research workbench
Structure of oxye (CYP165D3), a cytochrome P450 involved in teicoplanin biosynthesis
Analyse Structure of oxye (CYP165D3), a cytochrome P450 involved in teicoplanin… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3O1A
- Type
- protein
- Length
- 383 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Oxy protein
- EC
- 1.14.14.1
- UniProt
- Q6ZZI7
- Ligands
- HEM
- Pockets
- 2 · best druggability 0.79
Structure
x-ray diffraction · 1 distinct chain · 54% helix, 9% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Oxy protein (EC 1.14.14.1) | protein | 383 | 54% helix, 9% strand | Q6ZZI7 |
Ligands and binding sites
- HEM · Protoporphyrin IX containing Fe · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 756 | 0.79 | 0.82 | 78 | HEM |
| 2 | 58 | 0.34 | 0.77 | 13 | empty |
Compared structures
- 3O1A · Structure of OxyE (CYP165D3), a Cytochrome P450 Involved in Teicoplanin 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
- Every structure of UniProt Q6ZZI7
- Elsewhere: RCSB PDB 3O1A · PDBe 3O1A · UniProt Q6ZZI7
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