Research workbench
Acanthamoeba castellanii CYP51 (ACCYP51)-imidazole complex
Analyse Acanthamoeba castellanii CYP51 (ACCYP51)-imidazole complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7LES
- Type
- protein
- Length
- 1,793 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- L8GJB3
- Ligands
- HEM
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | — | protein | 449 | — | L8GJB3 |
| B | — | protein | 448 | — | L8GJB3 |
| D | — | protein | 447 | — | L8GJB3 |
Ligands and binding sites
- HEM · Protoporphyrin IX containing Fe · ligand · 4 copies · chains A, B, C, D
- PEG · Di(hydroxyethyl)ether · additive · 6 copies · chains A, B, C, D
- IMD · Imidazole · additive · 4 copies · chains A, B, C, D
- FMT · Formic acid · additive · 3 copies · chains A, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7LES · Acanthamoeba castellanii CYP51 (AcCYP51)-Imidazole complex · 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 L8GJB3
- Elsewhere: RCSB PDB 7LES · PDBe 7LES · UniProt L8GJB3
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