Research workbench
Crystal structure of a class C beta-lactamase in complex with cefoxitin
Analyse Crystal structure of a class C beta-lactamase in complex with cefoxitin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6KA5
- Type
- protein
- Length
- 354 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q9XB24
- Ligands
- 1S7
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 354 | — | Q9XB24 |
Ligands and binding sites
- 1S7 · (2R)-2-{(1S)-1-methoxy-2-oxo-1-[(thiophen-2-ylacetyl) amino]ethyl}-5-methylidene-5,6-dihydro-2H-1,3-thiazine-4-carboxylic acid · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6KA5 · Crystal structure of a class C beta-lactamase in complex with cefoxitin · 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 Q9XB24
- Elsewhere: RCSB PDB 6KA5 · PDBe 6KA5 · UniProt Q9XB24
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