Research workbench
Crystal structure of beta-lactamase from francisella tularensis
Analyse Crystal structure of beta-lactamase from francisella tularensis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3P09
- Type
- protein
- Length
- 528 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Beta-lactamase
- EC
- 3.5.2.6
- UniProt
- Q5NH60
- Ligands
- SO4
- Pockets
- 2 · best druggability 0.70
Structure
x-ray diffraction · 2 distinct chains · 46% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Beta-lactamase (EC 3.5.2.6) | protein | 264 | 46% helix, 17% strand | Q5NH60 |
| B | Beta-lactamase (EC 3.5.2.6) | protein | 264 | 46% helix, 17% strand | Q5NH60 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 672 | 0.70 | 0.78 | 77 | SO4 |
| 2 | 70 | 0.29 | 0.74 | 16 | SO4 |
Interfaces
1 interface between chains.
- A–B · 351 Ų buried · 4 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 modified, 2 disulfide (engineered, disulfide).
Compared structures
- 3P09 · Crystal Structure of Beta-Lactamase from Francisella tularensis · the same entry in another collection · 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 Q5NH60
- Elsewhere: RCSB PDB 3P09 · PDBe 3P09 · UniProt Q5NH60
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.