Research workbench
Beta-lactamase from bacillus licheniformis BS3
Analyse Beta-lactamase from bacillus licheniformis BS3 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1I2S
- Type
- protein
- Length
- 510 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Beta-lactamase
- EC
- 3.5.2.6
- UniProt
- P00808
- Ligands
- NA
- Pockets
- 5 · best druggability 0.68
Structure
x-ray diffraction · 1 distinct chain · 43% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Beta-lactamase (EC 3.5.2.6) | protein | 255 | 43% helix, 18% strand | P00808 |
Ligands and binding sites
- NA · Sodium ion · metal · 2 copies · chains A, B
- CIT · Citric acid · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 310 | 0.68 | 0.83 | 59 | empty |
| 2 | 79 | 0.44 | 0.80 | 15 | empty |
| 3 | 76 | 0.43 | 0.80 | 15 | empty |
| 4 | 60 | 0.31 | 0.76 | 15 | CIT |
| 5 | 74 | 0.30 | 0.74 | 18 | CIT |
Interfaces
1 interface between chains.
- A–B · 675 Ų buried · 10 hydrogen bonds · protein-protein
Compared structures
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 P00808
- Elsewhere: RCSB PDB 1I2S · PDBe 1I2S · UniProt P00808
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.