MolNFT v1 · #25102 · protein
Crystal structure of thermoactinomyces vulgaris R-47 alpha-amylase 2/BETA-cyclodextrin complex
1VFO · Neopullulanase 2: “Crystal structure of thermoactinomyces vulgaris R-47 alpha-amylase 2/BETA-cyclodextrin complex”. X-ray diffraction, 3 ligands (GLC, BGC, CA), 14 pockets (best druggability 0.88). MolNFT v1 #25102 on GenesisL1: 3D…
- PDB
- 1VFO
- 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, BGC, CA
- Pockets
- 14 · best druggability 0.88
Structure
x-ray diffraction · 1 distinct chain · 29% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Neopullulanase 2 (EC 3.2.1.135) | protein | 585 | 29% helix, 25% strand | Q08751 |
Ligands and binding sites
- GLC · alpha-D-glucopyranose · sugar · 13 copies · chains A, B
- BGC · beta-D-glucopyranose · sugar · chains A
- 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
14 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 589 | 0.88 | 0.93 | 92 | empty |
| 2 | 245 | 0.81 | 0.93 | 45 | empty |
| 3 | 264 | 0.64 | 0.82 | 34 | GLC |
| 4 | 229 | 0.56 | 0.78 | 40 | GLC |
| 5 | 206 | 0.55 | 0.79 | 23 | empty |
Interfaces
1 interface between chains.
- A–B · 2333 Ų buried · 51 hydrogen bonds · protein-protein
Compared structures
- 1VFO · Crystal structure of Thermoactinomyces vulgaris R-47 alpha-amylase 2/beta-cyclodextrin… · the same entry in another collection · chain A against A, 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 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 Q08751
- Elsewhere: RCSB PDB 1VFO · PDBe 1VFO · UniProt Q08751
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