Research workbench
S. cerevisiae CYP51 complexed with vt-1161
Analyse S. cerevisiae CYP51 complexed with vt-1161 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5UL0
- Type
- protein
- Length
- 528 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- A6ZSR0
- Ligands
- HEM, VT1
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 528 | — | A6ZSR0 |
Ligands and binding sites
- HEM · Protoporphyrin IX containing Fe · ligand · chains A
- VT1 · (R)-2-(2,4-Difluorophenyl)-1,1-difluoro-3-(1H-tetrazol-1-yl)-1-(5-(4-(2,2,2-trifluoroethoxy)phenyl)pyridin-2-yl)propan-2-ol · ligand · chains A
- 1PE · Pentaethylene glycol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5UL0 · S. cerevisiae CYP51 complexed with vt-1161 · 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 A6ZSR0
- Elsewhere: RCSB PDB 5UL0 · PDBe 5UL0 · UniProt A6ZSR0
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