Research workbench
The type III pullulan hydrolase from thermococcus kodakarensis
Analyse The type III pullulan hydrolase from thermococcus kodakarensis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5OT1
- Type
- protein
- Length
- 572 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Pullulanase type II, GH13 family
- UniProt
- Q5JID9
- Ligands
- CA
- Pockets
- 4 · best druggability 0.54
Structure
x-ray diffraction · 1 distinct chain · 30% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Pullulanase type II, GH13 family | protein | 572 | 30% helix, 24% strand | Q5JID9 |
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
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 228 | 0.54 | 0.77 | 28 | empty |
| 2 | 97 | 0.42 | 0.77 | 17 | empty |
| 3 | 83 | 0.41 | 0.79 | 19 | empty |
| 4 | 62 | 0.34 | 0.78 | 13 | empty |
Compared structures
- 5OT1 · The type III pullulan hydrolase from Thermococcus kodakarensis · 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 Q5JID9
- Elsewhere: RCSB PDB 5OT1 · PDBe 5OT1 · UniProt Q5JID9
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