Research workbench
Substrate binding induces conformational changes in a class a beta lactamase that primes it for catalysis
Analyse Substrate binding induces conformational changes in a class a beta lactamase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6C78
- Type
- protein
- Length
- 259 residues
- Chains
- 1
- Method
- neutron diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Beta-lactamase toho-1
- EC
- 3.5.2.6
- UniProt
- Q47066
- Pockets
- 1 · best druggability 0.33
Structure
neutron diffraction · 1 distinct chain · 42% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Beta-lactamase toho-1 (EC 3.5.2.6) | protein | 259 | 42% helix, 19% strand | Q47066 |
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 | 79 | 0.33 | 0.75 | 19 | empty |
Compared structures
- 6C78 · Substrate Binding Induces Conformational Changes In A Class A Beta Lactamase That Primes… · the same entry in another collection · chain A against A, TM-score 1.00
- Q47066 · AlphaFold monomer V2.0 prediction for beta-lactamase toho-1 (Q47066) · 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 Q47066
- Elsewhere: RCSB PDB 6C78 · PDBe 6C78 · UniProt Q47066
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