Research workbench
AlphaFold monomer V2.0 prediction for inducible lysine decarboxylase (P0A9H3)
Analyse AlphaFold monomer V2.0 prediction for inducible lysine decarboxylase (P0A9H3) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P0A9H3
- Type
- protein
- Length
- 715 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x8b27E975435FC92C447D6b738427Bc706002Ac3F
- UniProt
- P0A9H3
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 715 | — | P0A9H3 |
Compared structures
- 6YN5 · Inducible lysine decarboxylase LdcI decamer, pH 7.0 · an experimental structure of the same protein · chain A against H, TM-score 0.99
- 6YN5 · Inducible lysine decarboxylase ldci decamer, pH 7.0 · an experimental structure of the same protein · chain A against A, TM-score 0.99
- 3N75 · X-ray Crystal Structure of the Escherichia coli Inducible Lysine Decarboxylase LdcI · an experimental structure of the same protein · chain A against A, TM-score 0.99
- 3N75 · X-ray crystal structure of the escherichia COLI inducible lysine decarboxylase ldci · an experimental structure 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 P0A9H3
- Elsewhere: UniProt P0A9H3 · AlphaFold DB P0A9H3
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