MolNFT v1 · #32737 · protein
Ligand-free structure of sterol 14ALPHA-demethylase from mycobacterium tuberculosis in P2(1) space group
2BZ9: “Ligand-free structure of sterol 14ALPHA-demethylase from mycobacterium tuberculosis in P2(1) space group”. X-ray diffraction, 1 ligand (HEM), 8 pockets (best druggability 0.79). MolNFT v1 #32737 on GenesisL1: 3D structure, binding…
- PDB
- 2BZ9
- Type
- protein
- Length
- 861 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Sterol 14ALPHA-demethylase
- EC
- 1.14.13.70
- UniProt
- P0A512
- Ligands
- HEM
- Pockets
- 8 · best druggability 0.79
Structure
x-ray diffraction · 2 distinct chains · 51% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Sterol 14ALPHA-demethylase (EC 1.14.13.70) | protein | 429 | 51% helix, 13% strand | P0A512 |
| B | Sterol 14ALPHA-demethylase (EC 1.14.13.70) | protein | 432 | 52% helix, 13% strand | P0A512 |
Ligands and binding sites
- HEM · Protoporphyrin IX containing Fe · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 696 | 0.79 | 0.84 | 64 | HEM |
| 2 | 560 | 0.75 | 0.82 | 50 | HEM |
| 3 | 158 | 0.56 | 0.81 | 25 | empty |
| 4 | 186 | 0.48 | 0.76 | 27 | empty |
| 5 | 157 | 0.44 | 0.75 | 23 | empty |
Interfaces
1 interface between chains.
- A–B · 566 Ų buried · 8 hydrogen bonds · protein-protein
Compared structures
- 2BZ9 · Ligand-free structure of sterol 14alpha-demethylase from Mycobacterium tuberculosis in… · 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 P0A512
- Elsewhere: RCSB PDB 2BZ9 · PDBe 2BZ9 · UniProt P0A512
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