Research workbench
CYP76AH1-4PI from salvia miltiorrhiza
Analyse CYP76AH1-4PI from salvia miltiorrhiza in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5YM3
- Type
- protein
- Length
- 466 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ferruginol synthase
- EC
- 1.14.13.190
- UniProt
- S4UX02
- Ligands
- HEM, PIM, MN
- Pockets
- 3 · best druggability 0.87
Structure
x-ray diffraction · 1 distinct chain · 55% helix, 9% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ferruginol synthase (EC 1.14.13.190) | protein | 466 | 55% helix, 9% strand | S4UX02 |
Ligands and binding sites
- HEM · Protoporphyrin IX containing Fe · ligand · chains A
- PIM · 4-phenyl-1H-imidazole · ligand · chains A
- MN · Manganese (II) ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1079 | 0.87 | 0.88 | 89 | HEM, PIM |
| 2 | 186 | 0.47 | 0.75 | 25 | empty |
| 3 | 75 | 0.36 | 0.77 | 16 | empty |
Compared structures
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 S4UX02
- Elsewhere: RCSB PDB 5YM3 · PDBe 5YM3 · UniProt S4UX02
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