Research workbench
Crystal structures of chimeric beta-lactamase ctem-19M showing different conformations
Analyse Crystal structures of chimeric beta-lactamase ctem-19M showing different… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4QY6
- Type
- protein
- Length
- 263 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Beta-lactamase tem, beta-lactamase pse-4
- EC
- 3.5.2.6
- UniProt
- P62593, P16897
- Ligands
- MG, CL
- Pockets
- 1 · best druggability 0.52
Structure
x-ray diffraction · 1 distinct chain · 43% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Beta-lactamase tem, beta-lactamase pse-4 (EC 3.5.2.6) | protein | 263 | 43% helix, 17% strand | P62593, P16897 |
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, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 192 | 0.52 | 0.78 | 33 | CL |
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 4QY6 · Crystal structures of chimeric beta-lactamase cTEM-19m showing different conformations · the same entry in another collection · chain A against A, TM-score 1.00
- P62593 · AlphaFold monomer V2.0 prediction for beta-lactamase tem (P62593) · a predicted model of the same protein · chain A against A, TM-score 0.99
- P16897 · AlphaFold monomer V2.0 prediction for beta-lactamase pse-4 (P16897) · a predicted model of the same protein · chain A against A, TM-score 0.96
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 P62593
- Every structure of UniProt P16897
- Elsewhere: RCSB PDB 4QY6 · PDBe 4QY6 · UniProt P62593 · UniProt P16897
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