Research workbench
Crystal structure of stabilized TEM-1 beta-lactamase variant v.13 carrying R164S/G238S mutations
Analyse Crystal structure of stabilized TEM-1 beta-lactamase variant v.13 carrying… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4OQI
- Type
- protein
- Length
- 263 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.13
- Source
- Escherichia coli
- Molecule
- TEM-94 ES-beta-lactamase
- UniProt
- Q8KMX3
- Ligands
- CA, SO4
- Pockets
- 1 · best druggability 0.42
Structure
x-ray diffraction · resolution 1.13 · 1 distinct chain · 42% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | TEM-94 ES-beta-lactamase | protein | 263 | 42% helix, 17% strand | Q8KMX3 |
Ligands and binding sites
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 | 116 | 0.42 | 0.77 | 19 | SO4 |
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 4OQI · Crystal structure of stabilized tem-1 beta-lactamase variant V.13 carrying R164S/G238S… · 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 Q8KMX3
- Elsewhere: RCSB PDB 4OQI · PDBe 4OQI · UniProt Q8KMX3
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