Research workbench
Crystal structure of neopullulanase E357Q complex with maltotetraose
Analyse Crystal structure of neopullulanase E357Q complex with maltotetraose in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1J0J
- Type
- protein
- Length
- 1,176 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Neopullulanase
- EC
- 3.2.1.135
- UniProt
- P38940
- Ligands
- GLC
- Pockets
- 10 · best druggability 0.85
Structure
x-ray diffraction · 1 distinct chain · 29% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Neopullulanase (EC 3.2.1.135) | protein | 588 | 29% helix, 26% strand | P38940 |
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.
Pockets
10 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 790 | 0.85 | 0.88 | 92 | empty |
| 2 | 908 | 0.81 | 0.83 | 96 | GLC |
| 3 | 329 | 0.79 | 0.90 | 38 | empty |
| 4 | 86 | 0.71 | 0.94 | 22 | empty |
| 5 | 222 | 0.71 | 0.87 | 39 | empty |
Interfaces
1 interface between chains.
- A–B · 2817 Ų buried · 43 hydrogen bonds · protein-protein
Compared structures
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 P38940
- Elsewhere: RCSB PDB 1J0J · PDBe 1J0J · UniProt P38940
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