Research workbench
Crystal structure of thermoactinomyces vulgaris R-47 alpha- amylase 2/ACARBOSE complex
Analyse Crystal structure of thermoactinomyces vulgaris R-47 alpha- amylase 2/ACARBOSE… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3A6O
- 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
- ARE, CA
- Pockets
- 12 · best druggability 0.91
Structure
x-ray diffraction · 1 distinct chain · 30% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Neopullulanase 2 (EC 3.2.1.135) | protein | 585 | 30% helix, 26% strand | Q08751 |
Ligands and binding sites
- ARE · Acarbose derived pentasaccharide · ligand · 2 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
12 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 931 | 0.91 | 0.93 | 134 | empty |
| 2 | 211 | 0.58 | 0.80 | 34 | empty |
| 3 | 222 | 0.53 | 0.78 | 29 | empty |
| 4 | 89 | 0.51 | 0.83 | 21 | ARE |
| 5 | 89 | 0.48 | 0.82 | 21 | ARE |
Interfaces
1 interface between chains.
- A–B · 2412 Ų buried · 42 hydrogen bonds · protein-protein
Compared structures
- 3A6O · Crystal structure of Thermoactinomyces vulgaris R-47 alpha-amylase 2/acarbose complex · 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 3A6O · PDBe 3A6O · UniProt Q08751
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