Research workbench
Pullulanase from bacillus acidopullulyticus
Analyse Pullulanase from bacillus acidopullulyticus in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2WAN
- Type
- protein
- Length
- 810 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Pullulanase
- EC
- 3.2.1.41
- Ligands
- SO4
- Pockets
- 7 · best druggability 0.61
Structure
x-ray diffraction · 1 distinct chain · 24% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Pullulanase (EC 3.2.1.41) | protein | 810 | 24% helix, 29% strand | — |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 4 copies · chains A
- GOL · Glycerol · additive · 8 copies · chains A
- ACT · Acetate ion · additive · 4 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 262 | 0.61 | 0.80 | 41 | GOL |
| 2 | 99 | 0.42 | 0.78 | 22 | empty |
| 3 | 97 | 0.38 | 0.76 | 19 | empty |
| 4 | 102 | 0.38 | 0.75 | 23 | empty |
| 5 | 102 | 0.35 | 0.74 | 19 | empty |
Modifications
Observed in the structure: 1 modified (oxidation).
Compared structures
- 2WAN · Pullulanase from Bacillus acidopullulyticus · 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 2WAN · PDBe 2WAN
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