MolNFT v1 · #34051 · protein
Crystal structure of maltohexaose-producing amylase from bacillus SP.707 complexed with maltopentaose.
2D3L · Glucan 1,4-alpha-maltohexaosidase: “Crystal structure of maltohexaose-producing amylase from bacillus SP.707 complexed with maltopentaose.”. X-ray diffraction, 3 ligands (GLC, CA, NA), 1 pocket (best druggability 0.49). MolNFT v1…
- PDB
- 2D3L
- Type
- protein
- Length
- 481 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glucan 1,4-alpha-maltohexaosidase
- EC
- 3.2.1.98
- UniProt
- P19571
- Ligands
- GLC, CA, NA
- Pockets
- 1 · best druggability 0.49
Structure
x-ray diffraction · 1 distinct chain · 27% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glucan 1,4-alpha-maltohexaosidase (EC 3.2.1.98) | protein | 481 | 27% helix, 25% strand | P19571 |
Ligands and binding sites
- GLC · alpha-D-glucopyranose · sugar · 10 copies · chains A
- CA · Calcium ion · metal · 3 copies · chains A
- NA · Sodium ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 186 | 0.49 | 0.76 | 25 | GLC |
Compared structures
- 2D3L · Crystal structure of maltohexaose-producing amylase from Bacillus sp.707 complexed with… · the same entry in another collection · chain A against A, TM-score 1.00
- P19571 · AlphaFold monomer V2.0 prediction for glucan 1,4-alpha- maltohexaosidase (P19571) · 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 P19571
- Elsewhere: RCSB PDB 2D3L · PDBe 2D3L · UniProt P19571
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