Research workbench
Crystal structure of pullulanase from anoxybacillus sp. LM18-11
Analyse Crystal structure of pullulanase from anoxybacillus sp. LM18-11 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3WDH
- Type
- protein
- Length
- 698 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Type I pullulanase
- EC
- 3.2.1.41
- UniProt
- K9L0H1
- Ligands
- CA
- Pockets
- 6 · best druggability 0.66
Structure
x-ray diffraction · 1 distinct chain · 28% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Type I pullulanase (EC 3.2.1.41) | protein | 698 | 28% helix, 25% strand | K9L0H1 |
Ligands and binding sites
- CA · Calcium ion · metal · chains A
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 | 53 | 0.66 | 0.95 | 17 | empty |
| 2 | 232 | 0.53 | 0.76 | 34 | empty |
| 3 | 135 | 0.45 | 0.77 | 25 | empty |
| 4 | 100 | 0.41 | 0.77 | 19 | empty |
| 5 | 92 | 0.34 | 0.74 | 20 | empty |
Compared structures
- 3WDH · Crystal structure of Pullulanase from Anoxybacillus sp. LM18-11 · 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 K9L0H1
- Elsewhere: RCSB PDB 3WDH · PDBe 3WDH · UniProt K9L0H1
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