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Crystal structure of prenyltransferase prib ternary complex with L- tryptophan and dimethylallyl thiolodiphosphate (dmspp)
Analyse Crystal structure of prenyltransferase prib ternary complex with L- tryptophan… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5INJ
- Type
- protein
- Length
- 355 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Prenyltransferase
- Ligands
- TRP, DST
- Pockets
- 2 · best druggability 0.78
Structure
x-ray diffraction · 1 distinct chain · 38% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Prenyltransferase | protein | 355 | 38% helix, 21% strand | — |
Ligands and binding sites
- TRP · Tryptophan · ligand · chains A
- DST · Dimethylallyl S-thiolodiphosphate · ligand · chains A
- TRS · 2-amino-2-hydroxymethyl-propane-1,3-diol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 260 | 0.78 | 0.90 | 48 | TRP, DST |
| 2 | 134 | 0.49 | 0.79 | 26 | empty |
Compared structures
- 5INJ · Crystal Structure of Prenyltransferase PriB Ternary Complex with L-Tryptophan and… · 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
- Elsewhere: RCSB PDB 5INJ · PDBe 5INJ
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