Research workbench
Heteroyohimbine synthase THAS1 from catharanthus roseus - complex with NADP+
Analyse Heteroyohimbine synthase THAS1 from catharanthus roseus - complex with NADP+ in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5FI3
- Type
- protein
- Length
- 688 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tetrahydroalstonine synthase
- UniProt
- A0A0F6SD02
- Ligands
- NAP, ZN
- Pockets
- 6 · best druggability 0.78
Structure
x-ray diffraction · 1 distinct chain · 31% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Tetrahydroalstonine synthase | protein | 344 | 31% helix, 29% strand | A0A0F6SD02 |
Ligands and binding sites
- NAP · Nadp nicotinamide-adenine-dinucleotide phosphate · ligand · 2 copies · chains A, B
- ZN · Zinc ion · metal · 4 copies · chains A, B
- EDO · 1,2-ethanediol · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 867 | 0.78 | 0.81 | 92 | NAP, EDO |
| 2 | 827 | 0.76 | 0.80 | 95 | NAP |
| 3 | 90 | 0.46 | 0.81 | 23 | empty |
| 4 | 144 | 0.46 | 0.77 | 21 | empty |
| 5 | 90 | 0.45 | 0.80 | 23 | empty |
Interfaces
1 interface between chains.
- A–B · 1319 Ų buried · 13 hydrogen bonds · protein-protein
Compared structures
- 5FI3 · Heteroyohimbine synthase THAS1 from catharanthus roseus - complex with NADP+ · 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 A0A0F6SD02
- Elsewhere: RCSB PDB 5FI3 · PDBe 5FI3 · UniProt A0A0F6SD02
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