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Crystal structure of the substrate (obtusifoliol)-bound and ligand- free I105F mutant of sterol 14-alpha demethylase (CYP51) from trypanosoma cruzi
Analyse Crystal structure of the substrate (obtusifoliol)-bound and ligand- free I105F… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6FMO
- Type
- protein
- Length
- 1,792 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Sterol 14ALPHA-demethylase
- EC
- 1.14.13.70
- UniProt
- M1FYE4
- Ligands
- HEM, DVE
- Pockets
- 20 · best druggability 0.87
Structure
x-ray diffraction · 1 distinct chain · 50% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Sterol 14ALPHA-demethylase (EC 1.14.13.70) | protein | 448 | 50% helix, 12% strand | M1FYE4 |
Ligands and binding sites
- HEM · Protoporphyrin IX containing Fe · ligand · 4 copies · chains A, B, C, D
- DVE · Obtusifoliol · ligand · 3 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 14 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1044 | 0.87 | 0.87 | 96 | HEM, DVE |
| 2 | 920 | 0.86 | 0.87 | 77 | HEM, DVE |
| 3 | 921 | 0.85 | 0.86 | 78 | HEM, DVE |
| 4 | 1028 | 0.85 | 0.85 | 82 | HEM |
| 5 | 956 | 0.81 | 0.82 | 102 | empty |
Interfaces
4 interfaces between chains.
- A–B · 715 Ų buried · 11 hydrogen bonds · protein-protein
- C–D · 461 Ų buried · 5 hydrogen bonds · protein-protein
- B–C · 455 Ų buried · 0 hydrogen bonds · protein-protein
- B–D · 400 Ų buried · 5 hydrogen bonds · protein-protein
Compared structures
- 6FMO · Crystal structure of the substrate (obtusifoliol)-bound and ligand-free I105F mutant of… · 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 M1FYE4
- Elsewhere: RCSB PDB 6FMO · PDBe 6FMO · UniProt M1FYE4
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