Research workbench
Structure of cytochrome P450 eryk cocrystallized with inhibitor clotrimazole.
Analyse Structure of cytochrome P450 eryk cocrystallized with inhibitor clotrimazole. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2XFH
- Type
- protein
- Length
- 394 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Erythromycin B/D C-12 hydroxylase
- EC
- 1.14.-.-
- UniProt
- P48635
- Ligands
- CL6, HEM
- Pockets
- 2 · best druggability 0.78
Structure
x-ray diffraction · 1 distinct chain · 53% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Erythromycin B/D C-12 hydroxylase (EC 1.14.-.-) | protein | 394 | 53% helix, 10% strand | P48635 |
Ligands and binding sites
- CL6 · 1-[(2-chlorophenyl)(diphenyl)methyl]-1H-imidazole · ligand · 2 copies · chains A
- HEM · Protoporphyrin IX containing Fe · ligand · chains A
- DMS · Dimethyl sulfoxide · additive · 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 | 1171 | 0.78 | 0.79 | 82 | HEM, CL6 |
| 2 | 68 | 0.40 | 0.80 | 19 | empty |
Compared structures
- 2XFH · Structure of cytochrome P450 EryK cocrystallized with inhibitor clotrimazole. · the same entry in another collection · chain A against A, TM-score 1.00
- P48635 · AlphaFold monomer V2.0 prediction for erythromycin C-12 hydroxylase (P48635) · a predicted model of the same protein · chain A against A, TM-score 0.94
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 P48635
- Elsewhere: RCSB PDB 2XFH · PDBe 2XFH · UniProt P48635
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