Research workbench
Structures of the acyl-enzyme complex of the staphylococcus aureus beta-lactamase mutant GLU166ASP:ASN170GLN with degraded benzylpenicillin
Analyse Structures of the acyl-enzyme complex of the staphylococcus aureus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1GHP
- Type
- protein
- Length
- 257 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P00807
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 257 | — | P00807 |
Compared structures
- 1GHP · Structures of the acyl-enzyme complex of the staphylococcus aureus beta-lactamase mutant… · the same entry in another collection · chain A against A, TM-score 1.00
- P00807 · AlphaFold monomer V2.0 prediction for beta-lactamase (P00807) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 P00807
- Elsewhere: RCSB PDB 1GHP · PDBe 1GHP · UniProt P00807
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