Research workbench
Alpha-glucan recognition by a family 41 carbohydrate-binding module from thermotoga maritima pullulanase pula
Analyse Alpha-glucan recognition by a family 41 carbohydrate-binding module from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2J72
- Type
- protein
- Length
- 205 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Pullulanase
- EC
- 3.2.1.41
- UniProt
- O33840
- Ligands
- GLC
Structure
x-ray diffraction · 2 distinct chains · 0% helix, 58% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Pullulanase (EC 3.2.1.41) | protein | 102 | 0% helix, 58% strand | O33840 |
| B | Pullulanase (EC 3.2.1.41) | protein | 103 | 0% helix, 57% strand | O33840 |
Ligands and binding sites
- GLC · alpha-D-glucopyranose · sugar · 8 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 544 Ų buried · 3 hydrogen bonds · protein-protein
Compared structures
- 2J72 · alpha-glucan recognition by a family 41 carbohydrate-binding module from Thermotoga… · the same entry in another collection · chain A against A, TM-score 1.00
- O33840 · AlphaFold monomer V2.0 prediction for pullulanase (O33840) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 O33840
- Elsewhere: RCSB PDB 2J72 · PDBe 2J72 · UniProt O33840
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