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Structural, thermodynamic and kinetic analysis of the picomolar binding affinity interaction of the beta-lactamase inhibitor protein- II (blip-II) with class a beta-lactamases
Analyse Structural, thermodynamic and kinetic analysis of the picomolar binding… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3QHY
- Type
- protein
- Length
- 529 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q93T42, O87916
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 258 | — | Q93T42 |
| B | — | protein | 271 | — | O87916 |
Compared structures
- 3QHY · Structural, thermodynamic and kinetic analysis of the picomolar binding affinity… · 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 Q93T42
- Every structure of UniProt O87916
- Elsewhere: RCSB PDB 3QHY · PDBe 3QHY · UniProt Q93T42 · UniProt O87916
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