MolNFT v1 · #25066 · protein
Crystal structure analysis of bacillus cereus beta-amylase at the optimum pH (6.5)
1VEM: “Crystal structure analysis of bacillus cereus beta-amylase at the optimum pH (6.5)”. X-ray diffraction, 2 ligands (GLC, CA), 3 pockets (best druggability 0.73). MolNFT v1 #25066 on GenesisL1: 3D structure, binding sites and pockets…
- PDB
- 1VEM
- Type
- protein
- Length
- 516 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Beta-amylase
- EC
- 3.2.1.2
- UniProt
- P36924
- Ligands
- GLC, CA
- Pockets
- 3 · best druggability 0.73
Structure
x-ray diffraction · 1 distinct chain · 37% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Beta-amylase (EC 3.2.1.2) | protein | 516 | 37% helix, 19% strand | P36924 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 288 | 0.73 | 0.86 | 42 | GLC |
| 2 | 74 | 0.33 | 0.74 | 14 | empty |
| 3 | 51 | 0.24 | 0.72 | 15 | GLC |
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 1VEM · Crystal Structure Analysis of Bacillus Cereus Beta-Amylase at the optimum pH (6.5) · the same entry in another collection · chain A against A, TM-score 1.00
- P36924 · AlphaFold monomer V2.0 prediction for beta-amylase (P36924) · 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 P36924
- Elsewhere: RCSB PDB 1VEM · PDBe 1VEM · UniProt P36924
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