Research workbench
Precursor mutant CYS1SER of penicillin V acylase from bacillus sphaericus
Analyse Precursor mutant CYS1SER of penicillin V acylase from bacillus sphaericus in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2IWM
- Type
- protein
- Length
- 1,334 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P12256
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | — | protein | 334 | — | P12256 |
| C, D | — | protein | 333 | — | P12256 |
Compared structures
- 2IWM · precursor mutant Cys1Ser of Penicillin V Acylase from Bacillus sphaericus · the same entry in another collection · chain A against A, TM-score 1.00
- P12256 · AlphaFold monomer V2.0 prediction for penicillin acylase (P12256) · 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 P12256
- Elsewhere: RCSB PDB 2IWM · PDBe 2IWM · UniProt P12256
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