Research workbench
Rifr - type II thioesterase from rifamycin NRPS/PKS biosynthetic pathway - form 2
Analyse Rifr - type II thioesterase from rifamycin NRPS/PKS biosynthetic pathway - form… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3FLB
- Type
- protein
- Length
- 245 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Rifr
- EC
- 3.1.2.-
- UniProt
- Q7BUF9
- Ligands
- CL
- Pockets
- 1 · best druggability 0.54
Structure
x-ray diffraction · 1 distinct chain · 47% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Rifr (EC 3.1.2.-) | protein | 245 | 47% helix, 16% strand | Q7BUF9 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 88 | 0.54 | 0.84 | 14 | PG4 |
Compared structures
- 3FLB · RifR - Type II thioesterase from Rifamycin NRPS/PKS biosynthetic pathway - Form 2 · 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 Q7BUF9
- Elsewhere: RCSB PDB 3FLB · PDBe 3FLB · UniProt Q7BUF9
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