Research workbench
Structural characterisation of btrk decarboxylase from butirosin biosynthesis
Analyse Structural characterisation of btrk decarboxylase from butirosin biosynthesis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2J66
- Type
- protein
- Length
- 390 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Btrk
- EC
- 4.1.-.-
- UniProt
- Q4H4E6
- Ligands
- PLP
- Pockets
- 3 · best druggability 0.50
Structure
x-ray diffraction · 1 distinct chain · 37% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Btrk (EC 4.1.-.-) | protein | 390 | 37% helix, 26% strand | Q4H4E6 |
Ligands and binding sites
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 | 96 | 0.50 | 0.82 | 26 | PLP |
| 2 | 88 | 0.38 | 0.76 | 16 | empty |
| 3 | 85 | 0.38 | 0.76 | 17 | empty |
Modifications
Observed in the structure: 1 cofactor (pyridoxal phosphate Schiff base).
Compared structures
- 2J66 · Structural characterisation of BtrK decarboxylase from butirosin biosynthesis · 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 Q4H4E6
- Elsewhere: RCSB PDB 2J66 · PDBe 2J66 · UniProt Q4H4E6
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