MolNFT v1 · #34021 · protein
Structure of a complex of thermoactinomyces vulgaris R-47 alpha- amylase 2 with maltohexaose demonstrates the important role of aromatic residues at the reducing end of the substrate binding cleft
2D2O · Neopullulanase 2: “Structure of a complex of thermoactinomyces vulgaris R-47 alpha- amylase 2 with maltohexaose demonstrates the…”. X-ray diffraction, 2 ligands (GLC, CA), 10 pockets (best druggability 0.91). MolNFT v1 #34021 on…
- PDB
- 2D2O
- Type
- protein
- Length
- 1,170 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Neopullulanase 2
- EC
- 3.2.1.135
- UniProt
- Q08751
- Ligands
- GLC, CA
- Pockets
- 10 · best druggability 0.91
Structure
x-ray diffraction · 1 distinct chain · 29% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Neopullulanase 2 (EC 3.2.1.135) | protein | 585 | 29% helix, 26% strand | Q08751 |
Ligands and binding sites
- GLC · alpha-D-glucopyranose · sugar · 12 copies · chains A, B
- CA · Calcium ion · metal · 2 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, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1004 | 0.91 | 0.93 | 142 | empty |
| 2 | 155 | 0.54 | 0.80 | 25 | GLC |
| 3 | 236 | 0.51 | 0.76 | 31 | empty |
| 4 | 123 | 0.51 | 0.81 | 24 | GLC |
| 5 | 179 | 0.50 | 0.77 | 26 | empty |
Interfaces
1 interface between chains.
- A–B · 2449 Ų buried · 42 hydrogen bonds · protein-protein
Compared structures
- 2D2O · Structure of a complex of Thermoactinomyces vulgaris R-47 alpha-amylase 2 with… · the same entry in another collection · chain B against B, TM-score 1.00
- Q08751 · AlphaFold monomer V2.0 prediction for neopullulanase 2 (Q08751) · 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 Q08751
- Elsewhere: RCSB PDB 2D2O · PDBe 2D2O · UniProt Q08751
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