Research workbench
AlphaFold monomer V2.0 prediction for biodegradative arginine decarboxylase (P28629)
Analyse AlphaFold monomer V2.0 prediction for biodegradative arginine decarboxylase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P28629
- Type
- protein
- Length
- 755 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x42b99fCBf328028516680849Fb75A6A83F1A1bF1
- UniProt
- P28629
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 755 | — | P28629 |
Compared structures
- 2VYC · Crystal Structure of Acid Induced Arginine Decarboxylase from E. coli · an experimental structure of the same protein · chain A against I, TM-score 0.98
- 2VYC · Crystal structure of acid induced arginine decarboxylase from E. COLI · an experimental structure of the same protein · chain A against I, TM-score 0.98
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 P28629
- Elsewhere: UniProt P28629 · AlphaFold DB P28629
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