Research workbench
Nmc-a carbapenemase from enterobacter cloacae
Analyse Nmc-a carbapenemase from enterobacter cloacae in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1BUE
- Type
- protein
- Length
- 265 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein (imipenem-hydrolysing beta-lactamase)
- EC
- 3.5.2.6
- UniProt
- P52663
Structure
x-ray diffraction · 1 distinct chain · 42% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein (imipenem-hydrolysing beta-lactamase) (EC 3.5.2.6) | protein | 265 | 42% helix, 17% strand | P52663 |
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
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 P52663
- Elsewhere: RCSB PDB 1BUE · PDBe 1BUE · UniProt P52663
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